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The structural changes of macromolecules (starch, dietary fiber and protein) in purple corn flour (PCF) modified by a low temperature impact mill (LTIM) at different air classifier speed (ACS) were investigated. LTIM changed the multi-scale structure of starch, which was characterized by increased starch damage, stronger destruction of relative crystallinity (from 37.85 % to 15.53 %) and short-range ordered structure (R 1047/1022 , from 1.21 to 0.73) with the increased ACS. The structure of dietary fiber was also destroyed on multi-level, including decreased particle size, destructive morphology, and slightly changed crystalline structure. Additionally, LTIM showed high damage on the senior structure (surface hydrophobicity, disulfide bond, secondary structure) of protein. Due to the structure changes modified by LTIM, starch, dietary fiber and protein played different role on hydration property of PCF. Starch had positive effect, while dietary fiber and protein had negative effect. Our experimental results may provide valuable information for further analysis of other quality changes (oil holding capacity, cation exchange capacity, ability to produce high-quality dough or end-out products, etc.) of purple corn flour after LTIM treatment. • LTIM destroyed the multi-scale structure of starch. • The structure of dietary fiber was disrupted after LTIM on multi-level. • LTIM induced the changes of senior structure of protein. • Starch, dietary fiber, protein had different effect on hydration property of PCF. [ABSTRACT FROM AUTHOR]

The exceptional network assembly of natural polysaccharides/proteins-based hydrogels offers favorable biological characteristics and tunable physical properties making them ideal candidates for food and biomedical applications. Rheological analysis can provide quantitative information insights into the assembled network, which are critical for determining hydrogel properties and their suitability for food or biomedical use. This review introduced some concepts of rheology and brought together the hydrogels based on more than ten natural biopolymers, such as starch, pectin, gellan, xanthan, alginate, gelatin, carrageenan, soy protein, casein protein, whey protein, agar, cellulose, konjac glucomannan, and their related rheological studies. In addition, combined with our previous work, the effect of diverse cross-linking strategies on rheology and the role of various rheological characteristics (such as modulus variations, shear behavior changes, thixotropy and creep recovery capabilities, etc.) in gel design and application (such as 3D printing-based foods, active ingredients carrier, etc.) were also discussed. [ABSTRACT FROM AUTHOR]

Protein-based biomaterials have emerged as a promising alternative because of their inherent cell-to-cell interaction, structural support, and cellular communications. Over the last century, advances in the extraction, purification, and characterization of keratin proteins from wool, feathers, horns, and other animal sources have created a keratin-based biomaterials platform. Keratins, like many other naturally generated macromolecules, have biological activity and biocompatibility built-in. Furthermore, isolated keratins can self-assemble into structures that control cellular identification and behaviour. As a result, keratin biomaterials with applications in wound healing, drug delivery, tissue engineering, trauma, and medical devices have been developed due to these properties. This review examines the function of keratin in the human body in-depth, focusing on the history of keratin research and a current evaluation of emerging approaches in biomedical fields like tissue engineering, medical science, regenerative medicine, and drug delivery. • Keratin is the most common and significant biopolymer found in integumentary system of animals. • Due to cysteine disulphide bonds keratin shows more stability and lesser solubility. • Mutation in keratin genes may form novel keratins and may cause serious health conditions. • Pharmaceutical companies can utilise keratin from keratin waste for sustainable applications. • So far hydrogel, nanoparticles, films and tissue scaffold have been prepared from keratin. [ABSTRACT FROM AUTHOR]

Added protein to starch has abundantly applied to size the yarns. However, scarce information is available about the impact of proteins on the enzyme desizing of starch. Thus, the objective of this study was to explore the effect of corn gluten, soybean protein and bone glue on enzyme desizing and reveal the interference mechanism. The desizing efficiency of starch was detected after added proteins. The contact angle, swelling ability, protein content and structure of starch adhesion on desized yarn were measured to analyze the effect of protein on desizing. In addition, the binding forces between protein and starch were detected, and the inhibition mechanism was analyzed. Experimental results showed that desizing efficiencies of starch were decreased after adding the protein. Corn gluten had the strongest influence in hindering desizing due to the weakest promotion in the swelling of film and the stronger binding force between protein and starch, mainly through hydrophobic interaction and hydrogen bond. Improving the swelling ability of film and inhibiting the binding between starch and protein may be feasible ways to reduce the inhibition of protein on desizing. [ABSTRACT FROM AUTHOR]

Neurodegenerative diseases (NDDs) are increasingly prevalent with global aging, demanding effective treatments. Exosomes, which contain biological macromolecules such as RNA (including miRNAs) and proteins like α-synuclein, tau, and amyloid-beta, are gaining attention as innovative therapeutics. This comprehensive review systematically explores the potential roles of exosomes in NDDs, with a particular focus on their role in synaptic dysfunction. We present the synaptic pathophysiology of NDDs and discuss the mechanisms of exosome formation, secretion, and action. Subsequently, we review the roles of exosomes in different types of NDDs, such as Alzheimer's disease and Parkinson's disease, with a special focus on their regulation of synaptic function. In addition, we explore the potential use of exosomes as biomarkers, as well as the challenges and opportunities in their clinical application. We provide perspectives on future research directions and development trends to provide a more comprehensive understanding of and guidance for the application of exosomes in the treatment of NDDs. In conclusion, exosomes rich in biological macromolecules, as a novel therapeutic strategy, have opened up new possibilities for the treatment of NDDs and brought new hope to patients., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 The Author(s). Published by Elsevier B.V. All rights reserved.)

The facile development of a sustainable and durable flame-retardant approach for protein silk is of interest. Inspired by silk tin-weighting technology, this study developed a novel and sustainable in-situ deposition strategy based on biomass phytic acid to impart durable flame-retardant performance to silk fabrics. The chemical structure of insoluble chelating precipitation, and the surface morphology, thermal stability, combustion behavior, flame-retardant capacity, laundering resistance, and flame-retardant mode of action of the tin-weighting silk samples, were explored. The Sn-, P-, Si-containing insoluble chelating precipitation formed within the fiber interior and combined with silk fibers through electrostatic attraction and metal salt chelation. As a result, the tin-weighting silk displayed excellent self-extinguishing capacity, with the damaged length reduced to 9.2 cm and the LOI increased to 31.6 %; it also achieved self-extinguishing after 30 washing cycles, demonstrating high flame-retardant efficacy and laundering resistance. Moreover, the tin-weighting silk also showed the obvious suppression in smoke and heat generation by 55.6 % and 35.7 %, respectively. The synergistic charring action of phosphate groups, tin metal salts, and silicates was beneficial for enhancing the fire safety of silk. The tin-weighting treatment also displayed a minor impact on mechanical performance of silk fabrics., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier B.V. All rights reserved.)

Bacterial FT-IR signals are extremely specific and highly reproducible, making FT-IR an efficient tool for bacterial typing at the subspecies level. The polysaccharide and nucleic acid FT-IR regions (1200–900 cm−1) are recommended as a precise and reproducible pattern for bacterial typing. However, proteins are the major macromolecules present in bacteria, and the FT-IR spectral region of proteins (1800–1300 cm−1) is conceivably an important factor in bacterial typing. In this study, we investigated the influence of water on bacterial protein amide bands by comparing spectra obtained with and without FT-IR system dehydration. Eight Escherichia coli , ten Klebsiella pneumoniae , and eleven Staphylococcus aureus strains were typed by FT-IR under different conditions in a blinded experimental setup. Hierarchical clustering analysis (HCA) showed that, when protein signals were included (1800–900 cm−1), the typing accuracies for select E. coli , K. pn and S. aureus strains without system dehydration were 50%, 30% and 18.2%, respectively. However, the accuracies greatly improved to 100%, 90% and 90.9% when the FT-IR system was dehydrated. These results indicate that the FT-IR signals of protein amide bands are beneficial for bacterial typing. [Display omitted] • The FT-IR signals of protein amide I and II bands are beneficial to bacterial typing. • The main factor interfering with bacterial protein FT-IR signals is water. • Dehydration of the FT-IR system greatly enhances the accuracy of FT-IR-based bacterial typing. [ABSTRACT FROM AUTHOR]

Aromatic interaction plays a crucial role in controlling protein interaction by additives. Here we investigated the interaction of protein salting-in (solubilizing) additives with tryptophan (Trp), tyrosine (Tyr), indole, and proteins based on their fluorescence spectra. Five salting-in additives, i.e., arginine (Arg), urea, guanidine (Gdn), ethylene glycol (EG), and magnesium chloride (MgCl 2), showed different effects on the fluorescence properties of Trp and Tyr. Arg significantly reduced fluorescence intensity of Trp and Tyr, as was the case for glycine to a lesser extent. MgCl 2 and calcium chloride (CaCl 2) showed little effect on the aromatic fluorescence spectra. Gdn also showed little effect on the aromatic fluorescence spectra of Trp and Tyr even at high concentrations. EG increased the aromatic fluorescence intensity of Trp and Tyr with blue-shifted emission wavelength. Urea enhanced fluorescence of Trp and Tyr without altering emission wavelength. These results indicate that the protein solubilizing additives interact with aromatic groups differently. • Arg and Gly quenched the fluorescence of Trp, Tyr, and indole. • MgCl 2 , CaCl 2 , and Gdn showed little effect on the aromatic fluorescence. • Urea enhanced fluorescence without altering emission wavelength. • Ethylene glycol increased the aromatic fluorescence intensities with blue-shifted emission wavelength. • Protein solubilizing additives interact differently with the aromatic groups. [ABSTRACT FROM AUTHOR]

The molecular mechanism of the formation of protein corona by the interaction of gold nanorods (AuNRs) with fibrinogen and transferrin was studied by spectroscopic methods and molecular docking. Studies have shown that AuNRs can be used as quencher to quench the fluorescence of fibrinogen/transferrin. The quenching mechanism mainly comes from static quenching. Fibrinogen has two different binding sites on the longitudinal and the transverse plane of AuNRs respectively, while transferrin has only one binding site on the surface of AuNRs. The adsorption process conforms to Freundlich adsorption isotherm and the pseudo-second-order reaction. The chemisorption is the rate-limiting step. Fibrinogen/transferrin may be a component of the "hard corona" because they bind AuNRs with high binding affinity. The formation of protein corona leads to a decrease in the hydrophobicity of the microenvironment around transferrin tryptophan (Trp) residues and an increase in the hydrophobicity of the microenvironment around fibrinogen/transferrin tyrosine (Tyr) residues, affecting the tertiary and secondary structure of fibrinogen/transferrin. Molecular docking can clearly see the specific amino acid residues of fibrinogen and transferrin adsorbed on AuNRs, and verify the experimental results. • Fibrinogen has two binding sites, and transferrin has one binding site on AuNRs. • The adsorption process conforms to Freundlich adsorption isotherm model. • The adsorption process conforms to pseudo-second-order reaction model. • Fibrinogen/transferrin may be a component of the hard corona of AuNRs. • The structure of fibrinogen/transferrin is effected by protein corona. [ABSTRACT FROM AUTHOR]

Protein and polysaccharides are the mostly used biopolymers for developing packaging film and their combination-based composite produced better quality film compared to their single counterpart. The combination of protein and polysaccharides are superior owing to the better physical properties like water resistance, mechanical and barrier properties of the film. The protein/polysaccharide-based composite film showed promising result in active and smart food packaging regime. This work discussed the recent advances on the different types of protein/polysaccharide combinations used for making bio-based sustainable packaging film formulation and further utilized in food packaging applications. The fabrication and properties of various protein/polysaccharide combination are comprehensively discussed. This review also presents the use of the multifunctional composite film in meat, fish, fruits, vegetables, milk products, and bakery products, etc. Developing composite is a promising approach to improve physical properties and practical applicability of packaging film. The low water resistance properties, mechanical performance, and barrier properties limit the real-time use of biopolymer-based packaging film. The combination of protein/polysaccharide can be one of the promising solutions to the biopolymer-based packaging and thus recently many works has been published which is suitable to preserve the shelf life of food as well trace the food spoilage during food storage. • Fabrication process of protein/polysaccharide (Pro-Pol)-based packaging were described. • Effect of fillers on the physical and functional properties of Pro-Pol-based films was discussed. • Application of Pro-Pol-based film can track the freshness and increase the shelf life of different food samples. • Limitations, and future research opportunities for using Pro-Pol-based film in food packaging were discussed. [ABSTRACT FROM AUTHOR]

Cryogel-templated oleogels (CTO) were fabricated via a facile polyphenol crosslinking strategy, where apple polyphenol was utilized to crosslink the gelatin/egg white protein conjugates without forming hydrogels. After freeze-drying, cryogel templates were obtained and used to construct CTO by oil absorption. Apple polyphenol crosslinking improved the emulsion-related properties with appearance changes on samples, and infrared spectroscopy further confirmed the interactions between proteins and apple polyphenol. The crosslinked cryogels presented porous microstructures (porosity of over 96 %), enhanced thermal/mechanical stabilities, and could absorb a high content of oil (14.41 g/g) with a considerable oil holding capacity (90.98 %). Apple polyphenol crosslinking also influenced the rheological performances of CTO, where the highly crosslinked samples owned the best thixotropic recovery of 85.88 %. Moreover, after the rapid oxidation of oleogels, the generation of oxidation products was effectively inhibited by crosslinking (POV: 0.48 nmol/g, and TBARS: 0.53 mg/L). The polyphenol crosslinking strategy successfully involved egg white protein and gelatin to fabricate CTO with desired physical/chemical properties. Apple polyphenol acted as both a crosslinker and an antioxidant, which provided a good reference for fabricating pure protein-based CTO. [Display omitted] • Protein-based cryogel-templated oleogel (CTO) was formed by polyphenol crosslinking. • The crosslinking led to improved mechanical, thermal, and oil-related properties. • The highly crosslinked CTO owned the best thixotropic recovery/oxidation resistance. [ABSTRACT FROM AUTHOR]

Reversing the bacterial resistance is of great significance and importance. Fusidic acid (FA) is commonly effective against Gram-positive bacterial infections, but most Gram-negative bacteria have intrinsic resistance to FA, primarily due to the strong cell membrane-FA interactions, which highly inhibit the intracellular transport of FA. Herein, we use albumin (bovine serum albumin, BSA) as a bifunctional carrier to solubilize FA and facilitate its transmembrane delivery into Gram-negative bacterial cells. The water solubility of FA is significantly enhanced from 11.87 to 442.20 μg/mL by 5 mg/mL BSA after forming FA-BSA complex. Furthermore, FA-BSA (200 μg/mL) causes 99.96 % viability loss to the model pathogen E. coli upon incubation for 3 h, while free FA or BSA alone shows little activity. Elongation of E. coli cells after treated by FA-BSA is demonstrated by SEM, and the transmembrane transport of FA-BSA is demonstrated by CLSM. Interestingly, increasing the BSA amount substantially reduce the antibacterial activity of FA-BSA, implying an albumin-based transmembrane delivery mechanism may exist. This is the first report regarding successfully reversing the intrinsic resistance of Gram-negative bacteria to FA in the form of FA-BSA. The ready availability of albumin and the simple preparation allows FA-BSA to have great potentials for clinical use. [ABSTRACT FROM AUTHOR]

The food industry is undergoing a significant transformation with the advancement of 3D technology. Researchers in the field are increasingly interested in using protein and protein-polysaccharide composite materials for 3D printing applications. However, maintaining nutritional and sensory properties while guaranteeing printability of these materials is challenging. This review examines the commonly used protein and composite materials in food 3D printing and their roles in printing inks. This review also outlines the essential properties required for 3D printing, including extrudability, appropriate viscoelasticity, thixotropic properties, and gelation properties. Furthermore, it explores the wide range of potential applications for 3D printing technology in novel functional foods such as space food, dysphagia food, kid's food, meat analogue, and other specialized food products. [Display omitted] • Protein and protein-polysaccharide composite materials are used for 3D printing food applications • This article examines the roles of these commonly used protein and composite materials in food 3D printing are examined. • The crucial properties essential for successful 3D printing are outlined. • The diverse applications of 3D printing technology in creating novel functional foods are explored. [ABSTRACT FROM AUTHOR]

The thermal stability of trimeric lectin BC2L-CN was investigated and found to be considerably altered when mutating residue 83, originally a threonine, located at the fucose-binding loop. Mutants were analyzed using differential scanning calorimetry and isothermal microcalorimetry. Although most mutations decreased the affinity of the protein for oligosaccharide H type 1, six mutations increased the melting temperature (T m) by >5 °C; one mutation, T83P, increased the T m value by 18.2 °C(T83P, T m = 96.3 °C). In molecular dynamic simulations, the investigated thermostable mutants, T83P, T83A, and T83S, had decreased fluctuations in the loop containing residue 83. In the T83S mutation, the side-chain hydroxyl group of serine formed a hydrogen bond with a nearby residue, suggesting that the restricted movement of the side-chain resulted in fewer fluctuations and enhanced thermal stability. Residue 83 is located at the interface and near the upstream end of the equivalent loop in a different protomer; therefore, fluctuations by this residue likely propagate throughout the loop. Our study of the dramatic change in thermal stability by a single amino acid mutation provides useful insights into the rational design of protein structures, especially the structures of oligomeric proteins. • Residue 83 of the trimeric lectin BC2L-CN plays a key role in thermal stability. • Six mutations at the residue show increased melting temperature by >5 °C. • These mutations restricted dynamics of the loop containing residue 83. • The residue is in a position to spread fluctuation throughout its own loop. [ABSTRACT FROM AUTHOR]

This study describes the synthesis of Chitosan - corn protein (CSZ-TG) composites using TG enzyme (TG) as a cross-linking agent and the preparation of chitosan-based composite membrane material (CSZEO-TG) by blending citrus essential oil (EO) with the synthesized CSZ-TG. The prepared composite membrane material was used for fresh strawberry preservation and characterized by scanning electron microscopy, Fourier transform infrared spectroscopy, X-spectral diffraction, tensile properties, and water vapor and CO 2 permeability. Scanning electron microscopy results showed a smooth surface of the composite membrane material after the addition of TG enzyme, while Fourier transforms infrared spectroscopy results showed a structural change of the composite membrane material after the addition of corn protein (Z). The tensile results showed an increase in the tensile strength of the composite membrane material after the addition of TG enzyme, while the flexibility of the composite membrane material was enhanced after the addition of EO. Compared with the pure chitosan membrane (CS), the water vapor and CO 2 barrier properties of the composite membrane material after the addition of Z, TG, and EO did not change much, and they all showed better water vapor barrier properties. The results of the antioxidant analysis of the solution of the CSZEO-TG composite membrane material showed that the composite membrane material had efficient antioxidant properties. The effects of the composite film material on the storage period and quality of strawberries were evaluated by the indicators of weight loss, hardness, decay rate, soluble solids, titratable acid content, MDA content, and the content of four enzymes, SOD, POD, PPO and CAT. Comprehensive freshness data analysis showed that CSZEO-TG had the best freshness preservation performance and effectively extended the shelf life of strawberries. [ABSTRACT FROM AUTHOR]

Anthocyanins, natural plant pigments responsible for the vibrant hues in fruits, vegetables, and flowers, boast antioxidant properties with potential human health benefits. However, their susceptibility to degradation under conditions such as heat, light, and pH fluctuations necessitates strategies to safeguard their stability. Recent investigations have focused on exploring the interactions between anthocyanins and biomacromolecules, specifically proteins and polysaccharides, with the aim of enhancing their resilience. Notably, proteins like soy protein isolate and whey protein, alongside polysaccharides such as pectin, starch, and chitosan, have exhibited promising affinities with anthocyanins, thereby enhancing their stability and functional attributes. High-pressure processing (HPP), emerging as a non-thermal technology, has garnered attention for its potential to modulate these interactions. The application of high pressure can impact the structural features and stability of anthocyanin-protein/polysaccharide complexes, thereby altering their functionalities. However, caution must be exercised, as excessively high pressures may yield adverse effects. Consequently, while HPP holds promise in upholding anthocyanin stability, further exploration is warranted to elucidate its efficacy across diverse anthocyanin variants, macromolecular partners, pressure regimes, and their effects within real food matrices. [Display omitted] • Interaction between anthocyanins and macromolecules enhances anthocyanin stability. • High pressure affects the interaction between anthocyanins and proteins/polysaccharides. • High pressure can enhance the stability/functionality of anthocyanin complexes. • Excessive pressures exert negative effects on anthocyanin-macromolecule complexes. [ABSTRACT FROM AUTHOR]

In the context of starch–protein composite gels, the influence of protein on gel formation significantly shapes the textural attributes of starch gels, leading to distinct outcomes. This study aimed to evaluate how different ratios of pea protein (PP) affect the properties and structures of starch–protein composite gels at low (10 wt%) and high (40 wt%) solid concentrations. The addition of PP had opposite effects on the two gels. Compared to the pure starch gel, the low-concentration composite gel (LCG) with 20 % PP experienced a 48.90 ± 0.33 % reduction in hardness, and the storage modulus (G′) decreased from 14,100 Pa to 5250 Pa, indicating a softening effect of PP on LCG. Conversely, the hardness of the high-concentration composite gel (HCG) with 20 % PP exhibited a 62.19 ± 0.03 % increase in hardness, and G′ increased from 12,100 Pa to 41,700 Pa, highlighting the enhancing effect of PP on HCG. SEM and fluorescence microscopy images showed that PP induced uneven network sizes in LCG, while HCG with a PP content of 20 %, PP, together with starch, formed a three-dimensional network. This study provides valuable insights and guidance for the design and production of protein-enriched starch gel products with different textural properties. • Pea protein affected gel strength by influencing the starch pasting process • Pea protein reduced hardness of low-concentration composite gel. • Pea protein improved the strength of high-concentration composite gel. • Gels with high solid concentration had no free water. [ABSTRACT FROM AUTHOR]

This review addresses the current trend of replacing petroleum-based polymers in food packaging with bio-based alternatives, specifically focusing on proteins and polysaccharides. While these biopolymers exhibit excellent film-forming properties and are abundant in nature, their individual use in packaging lacks ideal plastic-like characteristics, especially in terms of mechanical and barrier properties. A recent solution involves the formulation of biocomposites through the reinforcement of one biopolymer with another (e.g., protein with a polysaccharide), significantly enhancing the physical, mechanical, and barrier properties of packaging materials. The review concentrates on the integration of proteins and polysaccharides in biocomposite materials, emphasizing their potential applications in active and intelligent food packaging systems. It covers sources, manufacturing methods, interaction mechanisms, recent developments, perspectives, and opportunities. The exploration extends to practical implementations of these biocomposites in enhancing food quality, safety, and shelf life—a green technological approach contributing to the reduction of food waste and loss. [Display omitted] [ABSTRACT FROM AUTHOR]

The impact of Dielectric-Barrier Discharge (DBD) plasma treatment on the prevention of heat-induced aggregation of Ovalbumin (OVA) and improvement in emulsification properties was investigated. Results highlighted the effective inhibition of thermal aggregation of OVA following exposure to plasma. Structural analysis revealed that the plasma-induced oxidation of sulfhydryl and intermolecular disulfide bonds played a pivotal role in inhibiting the thermal aggregation, considered by Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis (SDS-PAGE), multiplies spectroscopy, and analysis of dynamic exchange of sulfhydryl-disulfide bonds. Meanwhile, the oxidation of exposed hydrophobic sites due to plasma treatment resulted in the transformation of the OVA molecule's surface from hydrophobic to hydrophilic, contributing significantly to the aggregation inhibition. Additionally, compared to an untreated sample of OVA, almost one-fold increase in emulsifying ability (EAI) and 1.5-fold in emulsifying stability (ESI) was observed after 4 min of plasma treatment. These findings demonstrated that plasma treatment not only enhanced the thermal stability of OVA, but also improved its emulsification properties. [ABSTRACT FROM AUTHOR]

Pickering emulsion is a type of emulsion that uses solid particles or colloidal particles as emulsifiers rather than surfactants to adhere at oil-water interface. Pickering emulsions have gathered significant research attention recently due to their excellent stability and wide range of potential uses compared to traditional emulsions. Major advancements have been made in development of innovative Pickering emulsions using different colloidal particles by various techniques including homogenization, emulsification and ultrasonication. Use of biopolymer particles gives Pickering emulsions a more escalating possibilities. In this review paper, we seek to present a critical overview of development in food-grade particles that have been utilized to create Pickering emulsions with a focus on techniques and application of Pickering emulsions. Particularly, we have evaluated protein, lipid, polysaccharide-based particles and microalgal proteins that have emerged in recent years with respect to their potential to stabilize and add novel functionalities to Pickering emulsions. Some preparation methods of Pickering emulsions in brief, applications of Pickering emulsions are also highlighted. Encapsulation and delivery of bioactive compounds, fat substitutes, film formation and catalysis are potential applications of Pickering emulsions. Pickering double emulsions, nutraceutical and bioactive co-delivery, and preparation of porous materials are among research trends of food-grade Pickering emulsions. • Preparation of Pickering Emulsion is done by solid particles as stabilizers • Nanoparticle stabilized Pickering emulsions are becoming increasingly responsive because of their outstanding stability. • Solid particles can br reduced in size by different mechanical and chemical methods • Various techniques for Pickering emulsion preparation are ultrasonic emulsification, rotor stator, High-pressure homogenization, membrane emulsification. • Pickering emulsions can be effectively used in delivery and sustained release, fat replacers, film forming and catalytic efficiency. [ABSTRACT FROM AUTHOR]

Durum wheat, less immunogenically intolerant than bread wheat, originates from diploid progenitors known for nutritional quality and stress tolerance. Present study involves the analysis of major grain parameters, viz. size, weight, sugar, starch, and protein content of Triticum durum (AABB genome) and its diploid progenitors, Triticum monococcum (AA genome) and Aegilops speltoides (BB genome). Samples were collected during 2–5 weeks after anthesis (WAA), and at maturity. The investigation revealed that T. durum displayed the maximum grain size and weight. Expression analysis of Grain Weight 2 (GW2) and Glutamine Synthase (GS2), negative and positive regulators of grain weight and size, respectively, revealed higher GW2 expression in Ae. speltoides and higher GS2 expression in T. durum. Further we explored total starch, sugar and protein content, observing higher levels of starch and sugar in durum wheat while AA genome species exhibited higher protein content dominated by the fractions of albumin/globulin. HPLC profiling revealed unique sub-fractions in all three genome species. Additionally, a comparative transcriptome analysis also corroborated with the starch and protein content in the grains. This study provides valuable insights into the genetic and biochemical distinctions among durum wheat and its diploid progenitors, offering a foundation for their nutritional composition. [ABSTRACT FROM AUTHOR]

Protein aggregation poses a significant concern in the field of food sciences, and various factors, such as synthetic food dyes, can contribute to protein aggregation. One such dye, Sunset Yellow (SY), is commonly employed in the food industry. Trypsin was used as a model protein to assess the impact of SY. We employed several biophysical techniques to examine the binding and aggregation mechanisms between SY and trypsin at different pHs. Results from intrinsic fluorescence measurements indicate a stronger interaction between SY and trypsin at pH 2.0 compared to pH 6.0. Turbidity data reveal trypsin aggregation in the presence of 0.05–3.0 mM SY at pH 2.0, while no aggregation was observed at pH 6.0. Kinetic data demonstrate a rapid, lag-phase-free SY-induced aggregation of trypsin. Circular dichroism analysis reveals that trypsin adopts a secondary structure in the presence of SY at pH 6.0, whereas at pH 2.0, the secondary structure was nearly lost with increasing SY concentrations. Furthermore, turbidity and kinetics data suggest that trypsin aggregation depends on trypsin concentrations and pH. Our study highlights potential health risks associated with the consumption of SY, providing insights into its impact on human health and emphasizing the necessity for further research in this field. [ABSTRACT FROM AUTHOR]

Due to their excellent emulsification, biocompatibility, and biological activity, proteins are widely used as microcapsule wall materials for encapsulating drugs, natural bioactive substances, essential oils, probiotics, etc. In this review, we summarize the protein-based microcapsules, discussing the types of proteins utilized in microcapsule wall materials, the preparation process, and the main factors that influence their properties. Additionally, we conclude with examples of the vital role of protein-based microcapsules in advancing the food industry from primary processing to deep processing and their potential applications in the biomedical, chemical, and textile industries. However, the low stability and controllability of protein wall materials lead to degraded performance and quality of microcapsules. Protein complexes with polysaccharides or modifications to proteins are often used to improve the thermal instability, pH sensitivity, encapsulation efficiency and antioxidant capacity of microcapsules. In addition, factors such as wall material composition, wall material ratio, the ratio of core to wall material, pH, and preparation method all play critical roles in the preparation and performance of microcapsules. The application area and scope of protein-based microcapsules can be further expanded by optimizing the preparation process and studying the microcapsule release mechanism and control strategy. • Introduction to protein-based microcapsules' materials, methods, and applications. • Protein-polysaccharide interactions enhance microcapsule stability and sensitivity. • Multi-stimulus-responsive microcapsules offer better targeting and controllability. • Rational design of methods and wall material improves microcapsules properties. [ABSTRACT FROM AUTHOR]

Agarose is a seaweed-based polysaccharide and is widely used for the separation of nucleic acids in molecular biology. Cross-linked agarose beads are also used as solid-phase matrices in size exclusion chromatography for the separation of proteins. To find the application of agarose for the separation of oil/water emulsion and protein, herein hydrophobic derivative of the seaweed biopolymer [M W (1.27 ± 0.17) × 10 5 g/mol; sulphate content (0.29 ± 0.09) %, gel strength (2242 ± 21) g/cm2] is prepared by reacting the biopolymer with stearic acid and was used to prepare a composite membrane on polyester fabric. The oil and BSA rejection performance of the composite membrane was greater than 98%. The rejection rate increased with the increase in polymer content in the respective membranes for both oil/water and protein separation. The composite membrane showed a stable oil/water emulsion and protein separation performance over a period of six hours. Due to the biodegradable nature of the major components of the membrane, it has the potential for industrial applications. A hydrophobic derivative of the agarose is prepared by reacting the biopolymer with stearic acid and was used to prepare membrane by casting on polyester fabric. The composite membranes thus produced were found to separate oil from oil/water emulsion and protein from aqueous protein solution with rejection rate more than 98%. [Display omitted] • A hydrophobic derivative of the agarose is prepared with stearic acid. • The derivative was used to prepare membrane by casting on polyester fabric. • The composite membranes can separate oil and protein from mixtures. [ABSTRACT FROM AUTHOR]

In this work, the effect of Inca peanut seed albumin fraction (IPA) on the rheological, thermal and microstructural properties of native corn starch (NCS) was firstly studied. Compared to the NCS, IPA addition could obviously decrease the transparency of NCS, and the transparency of NCS and NCS-IPA suspensions decreased during the storage time. The textural paraments of NCS pastes with or without IPA reached to the maximum at a concentration of 5%. Steady shear rheological tests showed that all systems were non-Newtonian fluid, and the consistency coefficient (K) values reached to the maximum at 5% IPA concentration. The storage and loss modulus values of NCS-IPA pastes were higher than those of NCS pastes, and curves of loss angle (tan δ) indicated that all pastes were typical weak gel. With the increasing addition of IPA, DSC analysis showed that the thermal properties (To , Tp and Tc) of NCS were significantly changed, whereas, there was no distinct difference in the enthalpy. Microscopy illustrated that there were some wrinkle shrinkage and severe folds on the NCS-IPA granules. Fourier-transform infrared (FT-IR) spectroscopy showed that the hydrogen bonding was primarily interaction forces between IPA and NCS molecules. • The interaction between Inca peanut seed albumin fraction (IPA) and native corn starch (NCS) was firstly studied. • Physicochemical properties of NCS were changed after adding IPA. • The structure of starch molecules was changed after additional of IPA. • The molecular interaction forces between NCS and IPA were hydrogen bonds. [ABSTRACT FROM AUTHOR]

Chitin, an abundant biopolymer on Earth, represents a resource for sustainable functional materials. However, traditional β-chitin production methods involve alkaline treatment at approximately 90 °C for its separation from the protein, thus not suitable as a functional peptide, as it is mixed with an alkaline aqueous solution. This study examined the conversion of squid pen into solid β-chitin and water-soluble peptides using only water at temperatures of 150–250 °C for 30–120 min. Solid β-chitin was converted to its nanofiber form and the physicochemical properties of the β-chitin nanofibers were almost the same as those produced by the traditional method. Because this method uses only water, the protein in the squid pen may also be a functional peptide for lowering blood pressure, by inhibiting the Angiotensin-1 converting enzyme. High-temperature water treatment is a promising environment-friendly technique for complete utilization of squid pen components, including β-chitin and protein. [Display omitted] [ABSTRACT FROM AUTHOR]

Understanding nonionic surfactant-protein interactions is fundamental from both technological and scientific points of view. However, there is a complete absence of kinetic data for such interactions. We employed surface plasmon resonance (SPR) to determine the kinetic and thermodynamic parameters of bovine lactoferrin-Brij58 interactions at various temperatures under physiological conditions (pH 7.4). The adsorption process was accelerated with increasing temperature, while the desorption rate decreased, resulting in a more thermodynamically stable complex. The kinetic energetic parameters obtained for the formation of the activated complex, [bLF-Brij58]‡, indicated that the potential energy barrier for [bLF-Brij58]‡ formation arises primarily from the reduction in system entropy. [bLF-Brij58]○ formation was entropically driven, indicating that hydrophobic interactions play a fundamental role in bLF interactions with Brij58. [Display omitted] • Lactoferrin-Brij58 interaction form a entropically driven complex, [bLF-Brij58]○. • Stability of [bLF-Brij58]○ increases at elevated temperatures. • [bLF-Brij58]○ is formed via the transition state intermediate [bLF-Brij58]‡. • [bLF-Brij58]‡.enthalpic barrier is higher in the adsorption step. • Transition state entropic barrier is dominated by conformation change. [ABSTRACT FROM AUTHOR]

To explore in vivo application of quantum dots (QDs), it is essential to understand the dynamics and energetics of interactions between QDs and proteins. Here, surface plasmon resonance (SPR) and molecular docking were employed to investigate the kinetics and thermodynamics of interactions between human serum albumin (HSA) and CdTe QDs (~3 nm) functionalized with mercaptopropionic acid (MPA) or thioglycolic acid (TGA). Kinetic analysis showed that HSA–QD interactions involved transition-complex formation. Despite the structural similarities between MPA and TGA, the [HSA−CdTe@TGA]‡ formation by association of free HSA and QDs demanded 70% more energy and higher entropic gain (E a − TGA ‡= 65.10 and T ∆ S a − TGA ‡= 28.62 kJ mol−1) than the formation of [HSA−CdTe@MPA]‡ (E a − MPA ‡ = 38.13 and T ∆ S a − MPA ‡ = 0.53kJ mol−1). While the [HSA−CdTe@MPA]° dissociation required higher energy and lower entropy loss (E d − MPA ‡ = 49.96 and T ∆ S d − MPA ‡ = − 32.18kJ mol−1) than the [HSA−CdTe@TGA]° dissociation (E d − TGA ‡= 30.78 and T ∆ S d − TGA ‡= − 51.12 kJ mol−1). The stability of [HSA−QDs]° was independent of the temperature and functionalizing group. However, the enthalpic and entropic components were highly affected by the substitution of MPA (ΔH ° = − 11.83 and TΔS ° = 32.72 kJ mol−1) with TGA (ΔH ° = 34.31 and TΔS ° = 79.73 kJ mol−1). Furthermore, molecular docking results indicated that the metal site on the QDs contributes to the stabilization of [HSA−QDs]°. Therefore, differences in QD functionalization and surface coverage densities can alter the HSA–QD interaction, thus their application. [Display omitted] • Human serum albumin (HSA) binds to CdTe quantum dots (QD) with high affinity. • [HSA − CdTe @ MPA]° stable complex formation was enthalpic and entropically favorable. • [HSA − CdTe @ TGA]° stable complex formation was entropically driven. • The QD surface coverage highly affects the thermodynamic and kinetic parameters. • The HSA-QD interaction mechanism is altered by the QD surface coverage density. [ABSTRACT FROM AUTHOR]

Structural proteins such as spider silk and silkworm silk are generally poorly soluble in aqueous and organic solutions, making them difficult to manipulate in manufacturing processes. Although some organic acids and alcohols, such as formic acid and hexafluoroisopropanol (HFIP), effectively solubilize poorly soluble proteins, little is known about their protein solubilization mechanism. In this study, the solubility of N -acetyl amino acid amide compounds in organic solvents—formic acid, acetic acid, HFIP and isopropanol—was measured to clarify the protein solubilization mechanism at the amino acid residue level. On the basis of thermodynamic analyses of the solubility in terms of the transfer free energy (from water to organic solvents), every organic solvent was found to be effective in thermodynamically stabilizing hydrophobic amino acid side chains in the liquid phase. Formic acid and HFIP were comparably effective in the stabilization of the polypeptide backbone, whereas acetic acid and isopropanol were ineffective. Therefore, the significant solubilizing effect of formic acid and HFIP on the structural proteins was attributed to their favorable interactions with hydrophobic amino acid side chains and with the polypeptide backbone of the proteins. The present findings are useful for the optimization of protein manipulation and amino acid sequence design. [Display omitted] • Formic acid and fluoroalcohol are effective in solubilizing structural proteins. • The protein solubilization mechanism should be elucidated at amino acid level. • The solubility of N -acetyl amino acid amides was determined in organic solvents. • Organic solvents thermodynamically stabilize hydrophobic amino acid side chains. • Formic acid and fluoroalcohol stabilize the polypeptide backbone. [ABSTRACT FROM AUTHOR]

The field of cancer therapy is advancing rapidly, placing a crucial emphasis on innovative drug delivery systems. The increasing global impact of cancer highlights the need for creative therapeutic strategies. Natural polymer-based nanotherapeutics have emerged as a captivating avenue in this pursuit, drawing substantial attention due to their inherent attributes. These attributes include biodegradability, biocompatibility, negligible toxicity, extended circulation time, and a wide range of therapeutic payloads. The unique size, shape, and morphological characteristics of these systems facilitate profound tissue penetration, complementing active and passive targeting strategies. Moreover, these nanotherapeutics exploit specific cellular and subcellular trafficking pathways, providing precise control over drug release kinetics. This comprehensive review emphasizes the utilization of naturally occurring polymers such as polysaccharides (e.g., chitosan, hyaluronic acid, alginates, dextran, and cyclodextrin) and protein-based polymers (e.g., ferritin, gelatin, albumin) as the foundation for nanoparticle development. The paper meticulously examines their in vitro characteristics alongside in vivo efficacy, particularly focusing on their pivotal role in ameliorating diverse types of solid tumors within cancer therapy. The amalgamation of material science ingenuity and biological insight has led to the formulation of these nanoparticles, showcasing their potential to reshape the landscape of cancer treatment. [ABSTRACT FROM AUTHOR]

The stability of food emulsions is the basis for other properties. During their production and processing, emulsions tend to become unstable due to their thermodynamic instability, and it is usually necessary to add emulsifiers and proteins to stabilize emulsions. It becomes crucial to study the intrinsic mechanisms of emulsifiers and proteins and their joint stabilization of food emulsions. This paper summarizes the research on intrinsic mechanisms of food emulsions stabilized by emulsifiers and proteins in recent years. The destabilization and stabilization of emulsions are related to the added surfactants. The properties, type, and concentration of emulsifiers determine the stability of emulsions, and the emulsifiers can be classified into different types (e.g., ionic or nonionic, solid or liquid) according to their properties and sources. The physicochemical properties of proteins (e.g., spatial conformation, hydrophobicity) and the composition of proteins can also determine the stability of emulsions, and emulsions stabilized by emulsifiers and proteins together not only depend on these factors but also have a great relationship with the mutual combination and competition between the two. The instability and stability of emulsions are related to factors such as interfacial interaction forces, the rheological nature of the interface, and the added surfactant. [ABSTRACT FROM AUTHOR]

Proteinaceous liquid droplets, generated by liquid–liquid phase separation, function as membraneless compartments that are essential for diverse biological functions. Studies addressing droplet generation have used 1,6-hexanediol (1,6-HD) as a droplet-discerning agent owing to its capacity to induce droplet deformation. Despite the empirical utility of 1,6-HD, the mechanism underlying 1,6-HD-induced droplet deformation remains unknown. In this study, the solubilities of N -acetyl amino acid amides, which correspond to proteinogenic amino acid residues, were examined in the presence of 1,6-HD at 25 °C. Other solvents included ethanol, 1-propanol, and amides. Remarkably, 1,6-HD effectively solubilized hydrophobic species (particularly aromatic species) and exhibited reduced efficacy in solubilizing hydrophilic species and peptide bond moieties. These solubilizing effects are reflected in changes in protein solubility and structure. Specifically, 1,6-HD primarily targets the hydrophobic regions of a protein, increasing protein solubility without causing substantial structural changes. This solubilization mechanism is essential for elucidating the role of 1,6-HD as a droplet-discerning agent and recognizing its potential limitations. • N -acetyl amino acid amide solubility was examined in 1,6-hexanediol solutions. • 1,6-Hexanediol effectively solubilizes hydrophobic N -acetyl amino acid amides. • 1,6-Hexanediol is less effective with hydrophilic species and peptide bonds. • 1,6-Hexanediol can solubilize hydrophobic proteins with minimal structural changes. • This mechanism plays a role in the proteinaceous droplet deformation. [ABSTRACT FROM AUTHOR]

We herein evaluated the impact of adding wheat bran dietary fiber (WBDF) on the aggregation behavior of gluten in dough at various stages of the noodle-making process. Scanning electron microscopy and confocal laser scanning microscopy images confirmed the effective insertion of WBDF particles into the gluten matrix. Importantly, the gap between WBDF and gluten widened during the rolling process. The addition of WBDF led to a reduction in glutenin macropolymer (GMP) content and an elevation in sulfhydryl content, induced the depolymerization behaviors at the molecular level. Additionally, it facilitated the conversion of α-helices and β-turns into β-sheets and random coils within the dough. Moreover, the processing and addition of WBDF contributed to a decrease in weight loss, whereas the degradation temperature remained constant. Resting decreased the sulfhydryl content, whereas sheeting and cutting increased it, further fostering protein depolymerization in the presence of WBDF. These actions significantly increased the β-sheets and random coils content at the expense of β-turns and α-helices content. Significantly, controlled processing emerged as a crucial factor in enhancing gluten depolymerization induced by WBDF in the dough. This comprehensive study provides a nuanced perspective on controlling dough processing to strike a balance between dietary fiber-rich and high-quality foods. • GMP revealed that WBDF addition level had more influence than noodle-making process. • WBDF, and sheeting and cutting induced the transformation of α-helix and β-turn into β-sheet and random coil structure. • Resting resulted in a more uniform gluten network. • WBDF and processing had a synergistic effect on the gluten aggregation behavior of the dough. [ABSTRACT FROM AUTHOR]

In this work, we describe the synthesis, interactions with bovine serum albumin, and cytotoxicity of new ionic liquids based on 5-fluorouracil (API-ILs) with different cations (imidazolium, choline, isoquinolinium, guanidinium). The secondary and tertiary structure of BSA in solutions with different concentrations of API-ILs was monitored by the circular dichroism (CD) technique. The addition of API-ILs does not lead to structural changes in BSA. A quenching of fluorescence spectra intensity of BSA in presence of all API-ILs was observed, allowing the quantification of binding between API-ILs and BSA. The preferred localization of both ions in API-ILs differs significantly depending on the structure of the cation according to molecular docking. The aggregation of BSA in presence of API-ILs was analyzed by the dynamic light scattering (DLS) method, revealing a moderate increase in particle size. Cytotoxicity and selectivity of API-ILs on cancer and normal cell lines were estimated, showing a clear modification of the pharmaceutic activity of ionic liquid compared to 5-fluorouracil. [ABSTRACT FROM AUTHOR]

Staphylococcus aureus readily forms biofilms on tissue and indwelling catheter surfaces. These biofilms are resistant to antibiotics. Consequently, effective prevention and treatment strategies against staphylococcal biofilms are actively being pursued over the past two decades. One of the proposed strategies involve the incorporation of antibiotics and antiseptics into catheters, however, a persistent concern regarding the possible emergence of antimicrobial resistance is associated with these medical devices. In this study, we developed two types of silicone catheters: one with Lysostaphin (Lst) adsorbed onto the surface, and the other with Lst functionalized on the surface. To confirm the presence of Lst protein on the catheter surface, we conducted FTIR–ATR and SEM-EDS analysis. Both catheters exhibited hemocompatibility, biocompatibility, and demonstrated antimicrobial and biofilm prevention activities against both methicillin-sensitive and resistant strains of S. aureus. Furthermore, the silicone catheters that were surface-functionalized with Lst showed substantially better and more persistent anti-biofilm effects when compared to the catheters where Lst was surface-adsorbed, both under in vitro static and flow conditions, as well as in vivo in BALB/c mice. These results indicate that surface-functionalized Lst catheters have the potential to serve as a promising new medical device for preventing S. aureus biofilm infections in humans. [Display omitted] [ABSTRACT FROM AUTHOR]

Gel property is one of the most important abilities to endow protein-based food products with a unique texture and higher overall acceptability. Cereal β-glucan (BG) is widely applied in protein-based products to improve the stability of the protein gel by increasing water holding capacity, storage modulus (G'), loss modulus (G") and linking with protein through more exposed sites, making it easier to form a stronger three-dimensional gel network. In addition, BG may be cross-linked with proteins, or physically embedded and covered in protein network structures, interacting with proteins mainly through non-covalent bonds including hydrogen bonding and electrostatic interaction. Furthermore, the transition of the α-helix to the β-form in the protein secondary structure also contributes to the stability of the protein gel. The practical applications of BG from different cereals in protein-based products are summarized, and the rheological properties, microstructure of protein as well as the underlying interaction mechanisms between BG and protein are discussed. In conclusion, cereal BG is a promising polysaccharide in developing nutritional protein-based products with better sensory properties. [ABSTRACT FROM AUTHOR]

The study involves development of a green biorefinery process for obtaining fucoidan, laminarin, mannitol, alginate and protein from dry and fresh Fucus vesiculosus and Ascophyllum nodosum using hydrochloric acid and a green extraction solvent. After the extraction of fucoidan which was the targeted biomolecule, an extract and by-product (residual biomass) were obtained. The extract was passed through an ultrafiltration membrane, where fucoidan was obtained in the ultrafiltration retentate while ultrafiltration permeate was analysed for laminarin and mannitol. The residual biomass was used for obtaining alginate using ultrasound (20 kHz, 64 % amplitude and 32 min, optimum parameters for alginate extraction based on our previous study). All the samples, showed good results for alginate, laminarin and mannitol, indicating that the by-products can be utilised using this green extraction process. The comparison of both dry and fresh seaweed is relevant from an industry perspective, as fresh seaweed can directly be used for extraction, avoiding drying which adds significantly to the cost of the process. Life cycle impact assessment of the complete seaweed value chain has been carried out to identify the energy demand and key environmental hotspots. This biorefinery process can be used by industry to improve their processes and utilise the by-products generated efficiently. [ABSTRACT FROM AUTHOR]

Highland barley (HB) endosperm with an amylose content of 0–10 % is called waxy HB (WHB). WHB is a naturally slow-digesting grain, and the interaction between its endogenous non-starch composition and the WHB starch (WHBS) has an important effect on starch digestion. This paper focuses on the mechanisms by which the components of β-glucan, proteins and lipids affect the molecular, granular, crystalline structure and digestive properties of WHBS. After eliminating the main nutrients except for starch, the estimated glycemic index (eGI) of the samples rose from 62.56 % to 92.93 %, and the rapidly digested starch content increased from 60.81 % to 98.56 %, respectively. The resistant starch (RS) content, in contrast, dropped from 38.61 % to 0.13 %. Comparatively to lipids, β-glucan and protein contributed more to the rise in eGI and decline in RS content. The crystalline characteristics of starch were enhanced in the decomposed samples. The samples' gelatinization properties improved, as did the order of the starch molecules. Protein and β-glucan form a dense matrix on the surface of WHBS particles to inhibit WHBS digestion. In summary, this study revealed the mechanism influencing the digestibility of WHBS from the perspective of endogenous non-starch composition and provided a theoretical basis to develop slow-digesting foods. [Display omitted] • The endogenous non-starch components inhibited the in vitro digestibility of WHBS. • Protein and β-glucan showed the greatest effect on starch digestibility. • A continuous matrix formed by protein and β-glucan was present on the WHBS granules. • The physicochemical properties of WHBS were related with its in vitro digestibility. [ABSTRACT FROM AUTHOR]

Staphylococcus aureus (S. aureus) is one of the common causes of implant associated biofilm infections and their biofilms are resistant to antibiotics. S. aureus amidase (AM) protein, a cell wall hydrolase that cleaves the amide bond between N -acetylmuramic acid and L-alanine residue of the stem peptide, is several fold over-expressed under biofilm conditions. Previous studies demonstrated an autolysin mutant in S. aureus that lacks the AM protein, is highly impaired in biofilm development. We carried out a structure-based small molecule design using the crystal structure of AM protein catalytic domain to identify inhibitors that can block amidase activity and therefore inhibits S. aureus biofilm formation. Sequential virtual screening followed by pharmacokinetic analysis and bioassay studies filtered 25 small molecules from different databases. Two compounds from the SPECS database, SPECS-1 and SPECS-2, were selected based on the best docking score and minimum biofilm inhibitory concentration towards S. aureus biofilms. SPECS-1 and SPECS-2 were further tested for their structural/energetic stability in complex with the AM protein using molecular dynamics simulation and MM-GBSA techniques. In vitro, biofilm inhibition studies on different surfaces confirmed that treatment with SPECS-1 and SPECS-2 at a concentration of 250 μg/ml exhibited significant prevention and disruption of S. aureus biofilms. Finally, the in vitro anti-biofilm activities of these two compounds were validated against Methicillin-resistant S. aureus clinical isolates. We concluded that the discovered compounds SPECS-1 and SPECS-2 are safe and exhibit biofilm preventive and disruption activity for inhibiting the S. aureus biofilms and hence can be used to treat implant-associated biofilm infections. [ABSTRACT FROM AUTHOR]

The interaction between starch and protein during food processing is crucial for controlling food quality. This study aims to understand the interactions between corn starch and black bean protein isolate (BBPI) at various gelatinization phases and their effects on the physicochemical properties of the blends. BBPI reduced the rheological properties of the corn starch/BBPI mixed system during gelatinization, increasing light transmittance and gelatinization temperature, while decreasing total viscosity and enthalpy change. The changes in starch and protein microstructure during gelatinization indicated that BBPI adhered to the starch particle surface or partially penetrated the swollen starch particles. Fourier transform infrared spectroscopy (FT-IR) revealed that BBPI decreased the number of hydrogen bonds within starch, with no newly formed functional groups in the mixed system. Furthermore, BBPI reduced the composite relative crystallinity (RC). The effect of protein addition on water migration in the mixed system demonstrates that protein and starch compete for water during gelatinization, preventing water molecules from diffusing into starch particles. [ABSTRACT FROM AUTHOR]

The protein vital gluten is mainly used for food while interest for non-food applications, like biodegradable materials, increases. In general, the structure and functionality of proteins is highly dependent on thermal treatments during production or modification. This study presents conformational changes and corresponding rheological effects of vital wheat gluten depending on temperature. Dry samples analyzed by X-ray photoelectron spectroscopy (XPS), Fourier-transform infrared spectroscopy (FTIR) and thermalgravimetric analysis coupled with mass spectrometry (TGA-MS) show surface compositions and conformational changes from 25 to 250 °C. Above 170 °C, XPS reveals a decreased N content at the surface while FTIR band characteristics for β-sheets prove structural changes. At 250 °C, protein denaturation accompanied by a significant mass loss due to dehydration and decarbonylation reactions is observed. Oscillatory measurements of optimally hydrated vital gluten describing network properties of the material show two structural changes along a temperature ramp from 25 to 90 °C: at 56–64 °C, the temperature necessary to trigger structural changes increases with the ratio of gliadin to total protein mass, determined by reversed-phase high performance liquid chromatography (RP-HPLC). At a temperature of 79–81 °C, complete protein denaturation occurs. FTIR confirms the denaturation process by showing band shifts with both temperature steps. [ABSTRACT FROM AUTHOR]

Seaweed lectins are very promising biotechnological tools that also gain prominence when applied to the pharmacology field. The purpose of the present work was to isolate and characterize lectin from the red algae Amansia multifida and subsequently test it in general inflammation models. The lectin was purified by ion exchange chromatography, characterized with two-dimensional electrophoresis, automated analysis of amino acid sequences and circular dichroism spectroscopy. The pharmacological tests performed were paw edema induced by carrageenan or rapid inflammatory mediators, peritonitis induced by carrageenan and myeloperoxidase leukocyte count assays, glutathione and cytokine concentration. Our results have identified a 30 KDa molecular weight protein that presents a major secondary structure arranged in β-strand elements (~43%). A fragment of 20 amino acid residues was sequenced and presented low identity to the known classes of lectins from marine alga. This lectin was able to modulate inflammatory parameters such as paw edema, leukocyte migration, oxidative stress and proinflammatory cytokines. Thus, the lectin from the seaweed Amansia multifida has evident anti-inflammatory properties because it acts by reducing the formation of edema by modulating the effect of vascular mediators, migration of neutrophils, proinflammatory cytokines and oxidative stress control. [ABSTRACT FROM AUTHOR]

We report a facile approach for the preparation of protein conjugated glutaric acid functionalized Fe 3 O 4 magnetic nanoparticles (Pro-Glu-MNPs), having improved colloidal stability and heating efficacy. The Pro-Glu-MNPs were prepared by covalent conjugation of BSA protein onto the surface of glutaric acid functionalized Fe 3 O 4 magnetic nanoparticles (Glu-MNPs) obtained through thermal decomposition. XRD and TEM analyses confirmed the formation of crystalline Fe 3 O 4 nanoparticles of average size ~5 nm, whereas the conjugation of BSA protein to them was evident from XPS, FTIR, TGA, DLS and zeta-potential measurements. These Pro-Glu-MNPs showed good colloidal stability in different media (water, phosphate buffer saline, cell culture medium) and exhibited room temperature superparamagnetism with good magnetic field responsivity towards the external magnet. The induction heating studies revealed that the heating efficacy of these Pro-Glu-MNPs was strongly reliant on the particle concentration and their stabilizing media. In addition, they showed enhanced heating efficacy over Glu-MNPs as surface passivation by protein offers colloidal stability to them as well as prevents their aggregation under AC magnetic field. Further, Pro-Glu-MNPs are biocompatible towards normal cells and showed substantial cellular internalization in cancerous cells, suggesting their potential application in hyperthermia therapy. • Protein conjugated Fe 3 O 4 magnetic nanoparticles with good heating efficacy • Stable in water, phosphate buffer saline and Dulbecco's modified Eagle medium • Surface passivation by protein provide colloidal stability by preventing aggregation • Concentration and dispersing medium dependent heating under AC magnetic field • Biocompatible towards normal cell with substantial cellular uptake in cancerous cell [ABSTRACT FROM AUTHOR]

Since the specific proteins (carbohydrate antigens, ligands and interleukins) get raised up in body tissue or fluids in cancer cases, early detection of them will provide an effective treatment and survival rate. Sensitive and accurate determination of multiple cancer proteins can be engaged in chorus by simultaneous/multiplex detection in the biomedical fields. Bioassaying technology is one of the non-invasive, high-sensitive, and economical methods. Currently, extensive application of nanomaterial (biocompatible polymers, metallic and metal oxide) in bioassays resulted in ultra-high sensitive and selective diagnosis. This review article focuses on types of multiplex bioassays for delicate and specific determination of cancer proteins for diagnostic aims. It also covers two modes of multiplex bioassays as multi labeled bioassays and spatially-separated test zones (multi-electrode mode). In this review, the nanotechnological, structural, and technical perspectives in the multiplex analysis of cancer proteins were discussed. Finally, the use of different types of nanomaterials, polysaccharides, biopolymers and their advantages in signal amplification are discussed. Unlabelled Image • A comperhensive review of multiplex analysis of cancer biomarkers was conducted. • Multiplex evaluation of cancer biomarkers provide an effective treatment and survival rate. • Extensive use of nanomaterial in multiplex quantification of cancer biomarkers resulted in ultra-high sensitive diagnosis. • All of multiplex bioassays were categorized as two multi labeled bioassays and multi-electrode mode. [ABSTRACT FROM AUTHOR]

Chitosan, collagen, gelatin, polylactic acid and polyhydroxyalkanoates are notable examples of biopolymers, which are essentially bio-derived polymers produced by living cells. With the right techniques, these biological macromolecules can be exploited for nanotechnological advents, including for the fabrication of nanocarriers. In the world of nanotechnology, it is highly essential (and optimal) for nanocarriers to be biocompatible, biodegradable and non-toxic for safe in vivo applications, including for drug delivery, cancer immunotherapy, tissue engineering, gene delivery, photodynamic therapy and many more. The recent advancements in understanding nanotechnology and the physicochemical properties of biopolymers allows us to modify biological macromolecules and use them in a multitude of fields, most notably for clinical and therapeutic applications. By utilizing chitosan, collagen, gelatin, polylactic acid, polyhydroxyalkanoates and various other biopolymers as synthesis ingredients, the 'optimal' properties of a nanocarrier can easily be attained. With emphasis on the aforementioned biological macromolecules, this review presents the various biopolymers utilized for nanocarrier synthesis along with their specific synthetization methods. We further discussed on the characterization techniques and related applications for the synthesized nanocarriers. [ABSTRACT FROM AUTHOR]

The incorporation of plant-based extracts into polymer-based coatings is an efficient alternative to increase the shelf-life of stored fruit and to decrease or even prevent bacterial growth. Considering strawberries, it is also important to preserve their high antioxidant activity. Hence, this work evaluated the efficiency of a coating based on native cassava starch (NCS), gelatin, and sorbitol, containing different concentrations of Tetradenia riparia extract, in delaying the ripening process of strawberries stored under refrigerated conditions, and in preventing bacterial growth and antioxidant activity losses. Both concentrations of extract (500 or 1000 μg mL−1) increased the thickness, opacity, and water vapor transmission rate (WVTR) of the films when compared to the film without extract, but decreased the solubility. Even though the film without extract was expected to create a more efficient barrier to the coated fruits, the films containing the extract led to similar results of soluble solids (SS), titratable acidity (TA), and vitamin C. Nevertheless, the extract incorporation improved the control over bacterial growth, and preserved the high antioxidant activity of the strawberries within ten days of storage. [ABSTRACT FROM AUTHOR]

SP0845, a pneumococcal surface protein and a potential candidate vaccine for Streptococcus pneumoniae infection, was used to evaluate the role of histidine affinity tag on its biophysical properties and immunogenicity. The protein was expressed in E. coli with and without histidine affinity tag and purified to homogeneity. Size exclusion chromatographic studies revealed that tag free SP0845 was mainly monomeric in solution whereas, histidine tagged SP0845 stayed predominantly in an oligomeric form. Histidine-tagged SP0845 have higher β sheet content than the tag free protein. Removal of histidine tag increased the α-helical content of SP0845 from 35% to 46%. Histidine tagged SP0845 elicited higher serum antibody titer in comparison to the tag free SP0845 in mice. Effect of alum in improving the immunogenicity of tagged SP0845 was low in comparison to that observed with tag free protein. Immunogenicity of tag free SP0845 was enhanced by delivering it using polylactide polymeric particles. The presence of histidine tag thus influences the secondary structure and immunogenicity of protein and need careful consideration before use. [ABSTRACT FROM AUTHOR]

Wide sustainability and reusability of biomacromolecules such as carbohydrates and proteins-based biopolymers pave the way for providing maximal importance in the field of generating biopolymeric nanoparticles. As compared to synthetic nanomaterials, carbohydrate and protein based biopolymeric nanomaterials offer unique advantages that include antibacterial, biocompatible, immunogenicity, and biodegradable properties. Additionally, they have the significant property of more size distribution. Carbohydrate nanoparticles are primarily derived from the polysaccharide biopolymers such as alginate and chitosan; and protein nanoparticles are made from the diverse peptide biopolymers such as albumin, keratin, sericin, fibroin, gelatin and collagen. Advanced methods such as emulsification, desolvation, electrohydrodynamic atomization and coacervation are employed for the controlled fabrication of green biomacromolecules based nanoparticles. Suitability of biopolymeric nanoparticles in plethora of biotechnological applications are quite feasible with the advent of advanced technologies such as dynamic light scattering, scanning electron microscopy, transmission electron microscopy, atomic force microscopy, X-ray diffraction, Fourier transform infrared spectroscopy, and UV visible spectroscopy etc. Applications of such biomacromolecules nanoparticles are highly prevalent in agriculture, food, and biomedical industries. Thus, contributions of biopolymeric nanoparticles derived from carbohydrates and proteins biomacromolecules and their recent trends of patents granted in the biotechnological applications are critically discussed along with a promising future scope. [ABSTRACT FROM AUTHOR]

In this work, food-grade sunflower oil/W Pickering emulsions stabilized by xanthan gum-zein complex were developed. For this purpose, laser diffraction, rheological, multiple light scattering, confocal laser scanning microscopy (CLSM) and field emission scanning electron microscopy (FESEM) measurements were carried out. A response surface methodology was used to determine the optimized zein and oil concentration of the emulsion by using D 4,3 and Turbiscan Stability Index (TSI) as objective functions to minimize. Subsequently, the optimized formulation with minimum D 4,3 was selected and the biological macromolecule, advanced performance xanthan gum (APXG), was added. CLSM results of emulsions without gum showed the location of zein in the oil-water interface protecting droplets against coalescence as Pickering stabilizer. They also demonstrated that zein did not present important aggregation at the working pH. The addition of APXG changed the flow behaviour from Newtonian to shear thinning which fitted to the Cross model. This fact provoked the occurrence of viscoelastic properties and an increase in stability. FESEM results suggested the formation of a zein-gum complex, which forms a layer covering the droplets, protecting them against oxidation and physical destabilization. Therefore, this research supports the role of zein-APXG complex as a stabilizer of future emulsions. • Stable food emulsions formulated with zein-xanthan gum complex were developed. • Zein particles are located in the oil-water interface as Pickering stabilizer. • Zein-gum complex forms a layer covering and protecting the droplets. • Emulsions containing zein-gum complex present viscoelastic properties. [ABSTRACT FROM AUTHOR]