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Summary: Phytoproteins have been widely implemented in the food industry benefiting from their good functionalities, vast reserves and relatively low cost. However, phytoproteins frequently experience poor solubility, which limits their applications. In our study, the solubility of soy protein isolate (SPI) treated with pH‐shifting increased over 1.8 times; however, the transglutaminase‐induced gel properties were sacrificed. To solve this problem, walnut protein (WP) was used to co‐assemble with SPI during the treatment. The co‐assembly hybrid protein shows significantly better solubility, meanwhile, maintaining the transglutaminase‐induced gel properties and improving the cohesiveness and resilience properties compared with untreated SPI, which behaved an improved water holding capacity during storage. The detailed mechanisms were investigated with rheological analysis, SEM, textural analysis and Fourier transform infrared spectroscopy (FTIR). Overall, our study provided a promising strategy to develop SPI/WP hybrid composites with high solubility and improved gel properties to extend the application of SPI in the food industry. [ABSTRACT FROM AUTHOR]

As a typical bioactive compound from the bark and leaves of the trees of the genus Cinnamomum, cinnamaldehyde (CIN) is natural and safe. Its excellent antibacterial activity against various foodborne microorganisms is growingly regarded as a promising additive for improving and enhancing the properties of bio-based packaging films/coatings. This review systematically summarized the bio-based food packaging films/coatings containing CIN developed recently. The effects of CIN incorporation on physical and chemical properties of the antibacterial food packaging films/coatings, including thickness, color index, transparency, water content, water solubility, water contact angle, mechanical performances, water barrier performances, and antibacterial performances, were discussed. Simultaneously, this work also concluded that an explanation of the antibacterial mechanism of CIN and preparation methods of bio-based packaging films/coatings containing CIN/CIN carriers. Notably, the incorporation of CIN into the films/coatings could enhance their antibacterial performance extend the shelf-life of various foods, such as fish, meats, vegetables, fruits, and other perishable food, while improving their physical and chemical properties. Although incorporating CIN into food packaging films/coatings has been extensively studied, long-term follow-up research on the human safety of active food packaging films/coatings containing CIN needs to be carried out. [ABSTRACT FROM AUTHOR]

Protein lattices that shift the structure and shape anisotropy in response to environmental cues are closely coupled to potential functionality. However, to design and construct shape‐anisotropic protein arrays from the same building blocks in response to different external stimuli remains challenging. Here, by a combination of the multiple, symmetric interaction sites on the outer surface of protein nanocages and the tunable features of phenylalanine‐phenylalanine interactions, a protein engineering approach is reported to construct a variety of superstructures with shape anisotropy, including 3D cubic, 2D hexagonal layered, and 1D rod‐like crystalline protein nanocage arrays by using one single protein building block. Notably, the assembly of these crystalline protein arrays is reversible, which can be tuned by external stimuli (pH and ionic strength). The anisotropic morphologies of the fabricated macroscopic crystals can be correlated with the Å‐to‐nm scale protein arrangement details by crystallographic elucidation. These results enhance the understanding of the freedom offered by an object's symmetry and inter‐object π−π stacking interactions for protein building blocks to assemble into direction‐ and shape‐anisotropic biomaterials. [ABSTRACT FROM AUTHOR]

The structure and assembly properties of ferritin derived from aquatic products remain to be explored. Constructing diverse three-dimensional (3D) protein architectures with the same building blocks has important implications for nutrient delivery, medicine and materials science. Herein, ferritin from Asterias forbesii (AfFer) was prepared, and its crystal structure was resolved at 1.91 Å for the first time. Notably, different from the crystal structure of other reported ferritin, AfFer exhibited a BCT lattice arrangement in its crystals. Bioinspired by the crystal structure of AfFer, we described an effective approach for manufacturing 3D porous, crystalline nanoarchitectures by redesigning the shared protein interface involved in different 3D protein arrays. Based on this strategy, two 3D superlattices of body-centered tetragonal and simple cubicwere constructed with ferritin molecules as the building blocks. This study provided a potentially generalizable strategy for constructing different 3D protein-based crystalline biomaterials with the same building blocks. [ABSTRACT FROM AUTHOR]

Facing extreme pressure from an increasing population and climate degeneration, it is important to explore a green, safe and environmentally sustainable food source, especially for protein-enriched diets. Plant proteins have gained much attention in recent years, ascribing to their high nutritional value and environmental friendliness. In this review, we summarized recent advances in walnut protein with respect to its geographical distribution, structural and physiochemical properties and functional attributes. As a worldwide cultivated and largely consumptive crop, allergies and some physicochemical limitations have also led to a few concerns about walnut protein. Through comprehensive analysis and discussion, some strategies may be useful for future research, extraction and processing of walnut protein. [ABSTRACT FROM AUTHOR]

As the second most abundant trace element in the human body, zinc nutrition is constantly a hot topic. More than one-third population is suffering zinc deficiency, which results in various types of diseases or nutritional deficiencies. Traditional ways of zinc supplementation seem with low absorption rates and significant side effects. Zinc supplements with dietary components are easily accessible and improve zinc utilization rate significantly. Also, mechanisms of maintaining zinc homeostasis are of broad interest. The present review focuses on zinc nutrition in human health in inductive methods. Mainly elaborate on different diseases relating to zinc disorder, highlighting the impact on the immune system and the recent COVID-19. Then raise food-derived zinc-binding compounds, including protein, peptide, polysaccharide, and polyphenol, and also analyze their possibilities to serve as zinc complementary. Finally, illustrate the way to maintain zinc homeostasis and the corresponding mechanisms. The review provides data information for maintaining zinc homeostasis with the food-derived matrix. [ABSTRACT FROM AUTHOR]

Taking inspiration from Nature, we have constructed a two-compartment system based on 3D ferritin nanocage superlattices, the self-assembly behavior of which can be spatiotemporally controlled using two designed switches. One pH switch regulates the assembly of the ferritin subunit into its shell-like structure, whereas the other metal switch is responsible for assembly of the 3D superlattices from ferritin nanocages as building blocks. Consequently, this system holds great promise for the hierarchical encapsulation and release of two different cargo molecules. [ABSTRACT FROM AUTHOR]

Ferritin is an important iron storage protein, which is widely existed in all forms of life. Ferritin can regulate iron homeostasis when iron ions are lacking or enriched in the body, so as to avoid iron deficiency diseases and iron poisoning. Ferritin presents a hollow nanocage, which can store ions or other small molecular substances in the cavity. Therefore, ferritin shows its potential as a functional nanomaterial that can deliver nutrients or drugs in a targeted manner to improve bioavailability. Due to the special structure, the research on ferritin has attracted more and more attention in recent years. In this paper, the structural characteristics of ferritin were introduced, and the natural purification and prokaryotic expression methods of ferritin from different sources were described. At the same time, ferritin can bind to small molecules, so that it has the activity of small molecules, to construct a new type of ferritin. As a result, ferritin plays an important role as a nutrient substance, in targeted transport, and disease monitoring, etc. In conclusion, the yield of ferritin can be improved by means of molecular biology. Meanwhile, molecular modification can be used to make ferritin have unique activity and function, which lays a foundation for subsequent research. The molecular and structural properties of ferritins were clearly described. Isolation and purification technologies of ferritin were compared. Characterization, functions and molecular modifications mechanism of ferritin were reviewed. The applications of ferritin in pharmaceutical and food industry were prospected. [ABSTRACT FROM AUTHOR]

Heme-containing proteins, commonly abundant in red meat and blood, are considered promising dietary sources for iron supplementation and fortification with higher bioavailability and less side effects. As the precise structures and accurate bioactivity mechanism of various heme-containing proteins (hemoglobin, myoglobin, cytochrome, etc.) are determined, many methods have been explored for iron fortification. Based on their physicochemical and biological functions, heme-containing proteins and the hydrolyzed peptides have been also widely utilized as food ingredients and antibacterial agents in recent years. In this review, we summarized the structural characterization of hemoglobin, myoglobin, and other heme proteins in detail, and highlighted recent advances in applications of naturally occurring heme-containing proteins as dietary iron sources in the field of food science and nutrition. The regulation of absorption rate, auto-oxidation process, and dietary consumption of heme-containing proteins are then discussed. Future outlooks are also highlighted with the aim to suggest a research line to follow for further studies. [ABSTRACT FROM AUTHOR]

As a natural phenolic compound, carvacrol has attracted much attention due to its excellent antibacterial and antioxidant activities. However, its application is limited due to its instability, such as easy volatilization, easy oxidation, etc. Protein-polysaccharide interactions provide strategies for improving their stability issues. In this study, the plant-based carvacrol microcapsules via complex coacervation between walnut meal protein isolate (WMPI) and gum Arabic (GA) has been fabricated and characterized. The formation conditions of WMPI-GA coacervates were determined by some parameters, such as pH, zeta-potential, and turbidity. The optimum preparation conditions were achieved at pH 4.0 with a WMPI-to-GA ratio of 6:1 (w/w). The mean particle size, loading capacity (LC), and encapsulation efficiency (EE) of the microcapsules were 43.21 μm, 26.37%, and 89.87%, respectively. Fourier transform infrared spectroscopy (FT-IR) and fluorescence microscopy further confirmed the successful microencapsulation of carvacrol. The microencapsulation of carvacrol improved the thermal stability of the free carvacrol. The swelling capacity results indicated that it could resist gastric acid, and facilitate its intestinal absorption. Meanwhile, the carvacrol molecules trapped within the microcapsules could be continuously released in a concentration-dependent manner. Furthermore, the microcapsules presented good antioxidant activity and antibacterial activity against the Gram-negative (E. coli) and the Gram-positive (S. aureus) bacteria. These results indicated that the obtained carvacrol microcapsules have a potential application value as a food preservative in the food industry. [ABSTRACT FROM AUTHOR]

Constructing different protein nanostructures by using identical building blocks, while realizing their structural transformation in response to external stimuli, remains a challenge. Here, we fabricated protein nanocages and nanorods by using dimeric TmFtn as a building block and reacting with Mg2+/(α, L -lysine) with polymerization degrees of 9 (PLL9) and 15 (PLL15), respectively. Notably, the reversible shape transformation of these two supramolecular protein architectures with different dimensions can be achievable in response to external stimuli. [ABSTRACT FROM AUTHOR]

The low stability of trans‐astaxanthin (AX) not only limits its applications as a functional factor in food systems, but also affects the sensor quality of most shrimp products. Therefore, it is important to find an easy, effective way to improve the physical and chemical stability of AX. In this study, by taking advantage of the co‐existence of AX and shrimp ferritin (Marsupenaeus japonicus ferritin, MjF), we investigated the interaction of AX with MjF. Results showed that AX molecules are able to bind on the outer surface of MjF to form complexes, and quantitative analyses demonstrated that one ferritin molecule is bound to ∼48 AX molecules. Consequently, such binding not only greatly enhances the water solubility, thermal stability, and photo stability of AX, but also protects AX from Fe2+‐induced oxidative damage, as compared to free AX. Thus, MjF could be used as a protective molecule to improve the physical and chemical stability of AX. Practical Application: Our study opens up a new avenue for improving the physicochemical properties of bioactive molecules by interacting with protein, and shrimp ferritin could be explored as a protective system for the bioactive molecules. [ABSTRACT FROM AUTHOR]

Establishing artificial photosynthesis systems in a simple but effective manner to mitigate the greenhouse effect and address the energy crisis remains challenging. The combination of photocatalysis technology with bioengineering is an emerging field with great potential to construct such artificial photosynthesis systems, but so far, it has barely been explored in this area. Herein, an artificial photocatalysis platform is constructed with high CO2 conversion and H2O splitting capability by integration of CdS QDs into the intra‐subunit interface of H‐type ferritin (Marsupenaeus japonicus), a natural ferroxidase through protein interface redesign. The crystal structure of the synthesized CdS QDs with engineered ferritin molecules as bio‐templates confirmed the design at an atomic level. Notably, upon absorbing desirable visible light (≈420 nm), such a single CdS‐ferritin hybrid molecule is able to selectively catalyze the reduction of CO2 into HCOOH (≈90%), meanwhile catalyzing the oxidation of H2O into O2 in an aqueous environment. The O2 production rate reached to 180 µmol g−1 h−1, and the HCOOH output hit almost 800 µmol g−1 h−1. This work advances the utilization of the four‐helix bundle structure for crafting artificial photosynthesis systems, facilitating the seamless integration of bioengineering and photocatalysis technology. [ABSTRACT FROM AUTHOR]

Compartmentalization is a hallmark of living systems. Through compartmentalization, ubiquitous protein nanocages such as viral capsids, ferritin, small heat shock proteins, and DNA-binding proteins from starved cells fulfill a variety of functions, while their shell-like structures hold great promise for various applications in the field of nanomedicine and nanotechnology. However, the number and structure of natural protein nanocages are limited, and these natural protein nanocages may not be suited for a given application, which might impede their further application as nanovehicles, biotemplates or building blocks. To overcome these shortcomings, different strategies have been developed by scientists to construct artificial protein nanocages, and 1D, 2D and 3D protein arrays with protein nanocages as building blocks through genetic and chemical modification to rival the size and functionality of natural protein nanocages. This review outlines the recent advances in the field of the design and construction of artificial protein nanocages and their assemblies with higher order, summarizes the strategies for creating the assembly of protein nanocages from zero-dimension to three dimensions, and introduces their corresponding applications in the preparation of nanomaterials, electrochemistry, and drug delivery. The review will highlight the roles of both the inter-subunit/intermolecular interactions at the key interface and the protein symmetry in constructing and controlling protein nanocage assemblies with different dimensions. [ABSTRACT FROM AUTHOR]

Protein nanocages have recently received considerable attention in the fields of nanoscience and nanomedicine and have been used as either biotemplates for the preparation of a variety of nanomaterials or vehicles for drugs or imaging agents. However, their utilization for detection of heavy metal ions has yet to be explored. In this study, by grafting a mercury binding peptide (MBP) on the exterior surface of a recombinant human H-chain ferritin (rHuHF) nanocage, we successfully prepared a new protein nanocage (HuHF-MBP) which exhibits high binding capacity and affinity for Hg2+. The fluorescence of HuHF-MBP labeled with a green fluorescent dye fluorescein isothiocyanate (FITC) can be quenched by graphene oxide (GO), while addition of Hg2+ to the above solution recovered the quenched fluorescence in a dose-dependent manner. Thus, this system consisting of FITC-labeled HuHF-MBP and GO, where FITC and graphene oxide were used as fluorescent reporter probes, has great potential to be explored as a sensor for Hg2+ detection. Indeed, this newly constructed protein sensor exhibited high sensitivity and selectivity for Hg2+, and the limit of detection was 1.0 nM. The construction of this system provides an alternative strategy for the preparation of heavy metal ion sensors by using protein nanocages as biotemplates. [ABSTRACT FROM AUTHOR]

Ferritin, a ubiquitous iron storage protein, has a crucial role in innate immunity in arthropods, which have no adaptive immune system. Arthropods are thought to have two types of ferritin molecules: the secreted type and the cytosolic type. Here, we present the first crystal structure of ferritin from crustacean, kuruma prawn (Marsupenaeus japonicus), at 1.16 Å resolution. This shrimp ferritin (MjFer) is the cytosolic type, and its structure shows well‐conserved ferritin fold composed of a 4‐helix bundle that assembles into a cage‐like 24‐mer. The structure of MjFer was more similar to those of human and vertebrate ferritins than to that of the secreted‐type arthropod ferritin from an insect. MjFer possesses both a ferroxidase site and a nucleation site, which are the main characteristics of vertebrate H and L chain ferritins, respectively. The first crystal structure of crustacean ferritin, MjFer, has exceptionally high quality that provides the detailed structural information of metal moving pathway in ferritin. PDB Code(s): 6A4U [ABSTRACT FROM AUTHOR]