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Cold plasma treatment is an innovative technology in the food processing and preservation sectors. It is primarily employed to deactivate microorganisms and enzymes without heat and chemical additives; hence, it is often termed a "clean and green" technology. However, food quality and safety challenges may arise during cold plasma processing due to potential chemical interactions between the plasma reactive species and food components. This review aims to consolidate and discuss data on the impact of cold plasma on the chemical constituents and physical and functional properties of major food products, including dairy, meat, nuts, fruits, vegetables, and grains. We emphasize how cold plasma induces chemical modification of key food components, such as water, proteins, lipids, carbohydrates, vitamins, polyphenols, and volatile organic compounds. Additionally, we discuss changes in color, pH, and organoleptic properties induced by cold plasma treatment and their correlation with chemical modification. Current studies demonstrate that reactive oxygen and nitrogen species in cold plasma oxidize proteins, lipids, and bioactive compounds upon direct contact with the food matrix. Reductions in nutrients and bioactive compounds, including polyunsaturated fatty acids, sugars, polyphenols, and vitamins, have been observed in dairy products, vegetables, fruits, and beverages following cold plasma treatment. Furthermore, structural alterations and the generation of volatile and non-volatile oxidation products were observed, impacting the color, flavor, and texture of food products. However, the effects on dry foods, such as seeds and nuts, are comparatively less pronounced. Overall, this review highlights the drawbacks, challenges, and opportunities associated with cold plasma treatment in food processing., (© 2024 The Author(s). Comprehensive Reviews in Food Science and Food Safety published by Wiley Periodicals LLC on behalf of Institute of Food Technologists.)

Quinones, produced by the oxidation of phenolic compounds, covalently bind to nucleophilic groups on amino acids or proteins. In this study, the reactions of 4-methylbenzoquinone (4MBQ) with β-lactoglobulin (β-LG) and amino acids at neutral pH were investigated. LC-MS analysis revealed that Cys121 was likely the most modified residue in β-LG. Identification of reaction products by LC-MS/MS showed that Michael addition occurred in all reactions with amino acids tested. The formation of Schiff base and a di-adduct was found in His and Trp samples. Apparent second-order rate constants (k 2 ) were determined at 25 °C and pH 7.0 by stopped-flow spectrophotometry. The rate of reactions decreased in the order: β-LG > His > Trp > Arg > N α -acetyl His > N α -acetyl Arg > N α -acetyl Trp. The rate constants correlated with the pK a values of the amino acids, showing that the amount of unprotonated amine is the major factor determining the reactivity., 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 © 2023 The Author(s). Published by Elsevier Ltd.. All rights reserved.)

The present study compared the impact of two UV light devices: conventional UV lamp and UV-LED on the colour, pH, lipid and protein oxidation of fresh chicken breast meat aerobically stored at 4 °C for 10 days. Lipid oxidation was the most impacted quality attribute in UV lamp treated meat, unlike UV-LED that showed no effect compared to non-treated meat. Slight changes were observed in colour, pH and protein oxidation of chicken samples subjected to UV lamp and UV-LED. To evaluate these changes from a consumer perspective, the different treatment samples were stored at 4 °C for 3 days and colour likeness, odour likeness and overall appearance were assessed by consumer sensory analysis. However, alterations in quality parameters of chicken meat caused by UV light did not decrease overall acceptance in the sensory analysis. UV-LED was the preferred chicken meat by the participants, even compared to non-treated meat., 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 © 2023 Elsevier Ltd. All rights reserved.)

Formation of Maillard reaction products (MRPs) is increasingly studied by the use of fluorescence spectroscopy, and most often, by measuring single excitation/emission pairs or use of unresolved spectra. However, due to the matrix complexity and potential co-formation of fluorescent oxidation products on tryptophan and tyrosine residues, this practice will often introduce errors in both identification and quantification. The present study investigates the combination of fluorescence excitation emission matrix (EEM) spectroscopy and parallel factor analysis (PARAFAC) to resolve the EEMs into its underlying fluorescent signals, allowing for better identification and quantification of MRPs. EEMs were recorded on a sample system of bovine serum albumin incubated at 40 °C for up to one week with either glucose, methylglyoxal or glyoxal added. Ten unique PARAFAC components were resolved, and assignment was attempted based on similarity with fluorescence of pure standards of MRPs and oxidation products and reported data from literature. Of the ten fluorescent PARAFAC components, tyrosine and buried and exposed tryptophan were resolved and identified, as well as the formation of specific MRPs (argpyrimidine and Nα-acetyl-Nδ-(5-methyl-4-imidazolon-2-yl)ornithine) and tryptophan oxidation products (kynurenine and dioxindolylalanine). The formation of the PARAFAC resolved protein modifications were qualitatively validated by liquid chromatography-mass spectrometry., 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 Authors. Published by Elsevier Ltd.. All rights reserved.)

This study investigated the multiproduct (fucoidans, β-glucans, proteins, carotenoids, fatty acids, amino acids and polyphenols) valorization of the invasive macroalgae Ascophyllum nodosum within a green biorefinery concept using ultrasound (US), microwave (MW) treatment followed by supercritical CO 2 (SC-CO 2 ) with co-solvent and enzymatic extraction. Water and 50% aqueous ethanol were used as green extraction solvents. The extraction methods using 50% ethanol as extraction solvent improved the yields of phenolic compounds and glucan and enhanced in vitro antioxidant activity. The characterization of SC-CO 2 extracts revealed that pretreatment with US and MW improved the 2-fold yield of carotenoids, total phenolics and fatty acids. However, US/MW pretreatment and enzymatic extraction did not improve the yields of proteins and free amino acids. Overall, using concurrent green US/MW-assisted extraction methods enhanced the yields of the bioactive compounds in a short duration and provided extracts with a better antioxidant capacity in the field of food applications., 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 © 2023 Elsevier Ltd. All rights reserved.)

Hemp seeds are currently used mainly for oil extraction, generating waste that could be potentially exploited further as a source of proteins and other bioactives. This study aims to valorise hemp waste ( Cannabis sativa , L.) from previous oil extraction as a source of protein by analysing the effect of high-pressure processing (HPP) pre-treatments (0-600 MPa; 4-8 min) combined with conventional or ultrasound-assisted extraction (UAE) methods on protein recovery/purity, amino acid composition, and protein structure. Overall, maximum protein recovery (≈62%) was achieved with HPP (200 MPa, 8 min) with UAE. The highest protein purity (≈76%) was achieved with HPP (200 MPa, 4 min) with UAE. Overall, UAE improved the extraction of all amino acids compared to conventional extraction independently of HPP pre-treatments. Arg/Lys ratios of the protein isolates ranged between 3.78 and 5.34, higher than other vegetable protein sources. SDS-PAGE did not show visible differences amongst the protein isolates. These results seem to indicate the advantages of the use of UAE for protein recovery in the food industry and the need for further studies to optimise HPP/UAE for an accurate estimation of processing costs and their effects on the composition and structure of proteins to contribute further to the circular economy.

Protein-polyphenol interactions affect the structure, stability, and functional properties of proteins and polyphenols. Oxidized polyphenols (o-quinones) react rapidly with the sulfhydryl group of cysteine (Cys) residues, inducing covalent bonding between proteins and polyphenols. However, quantitative data on such reactions remain elusive, despite the importance of depicting the significance of such interactions on food structure and function. This work reports the synthesis, purification, and characterization of caffeic acid-cysteine (CA-Cys) and chlorogenic acid-cysteine (CGA-Cys) adducts and their stable isotope analogs, CA-[ 13 C 3 , 15 N]Cys and CGA-[ 13 C 3 , 15 N]Cys. A sensitive LC-MS/MS isotope dilution method was developed to simultaneously quantify these adducts in foods and beverages. Protein-bound CA-Cys and CGA-Cys were detected in the micro-molar range in milk samples with added CA and CGA, confirming covalent bonding between milk proteins and CA/CGA. These adducts were detected in commercial coffee-containing beverages but not in cocoa-containing drinks. Furthermore, the adducts were found to be partially stable during enzymatic protein hydrolysis., 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 © 2022 The Author(s). Published by Elsevier Ltd.. All rights reserved.)

Caffeic acid (CA) and chlorogenic acid (CGA) are commonly found phenolic acids in plant-derived foods and beverages. Their corresponding adducts with cysteine (Cys) have been detected in coffee-containing beverages. However, despite the well-documented antioxidant and anti-inflammatory activity of CA and CGA, the immunomodulatory activities of the Cys adducts (CA-Cys and CGA-Cys) are unknown. The adducts were therefore synthesized, and their immunomodulatory effects were studied in lipopolysaccharide (LPS)-treated RAW 264.7 cells and compared to the activity of the parent phenolic acids. CA and CGA generally down-regulated the inflammatory responses. However, RNA-sequencing showed that the LPS-induced pathways related to Toll-like receptor signaling, chemokine signaling, and NOD-like receptor signaling, and JAK-STAT/MAPK signaling pathways were upregulated in adduct-treated cells relative to parent phenolic acids, while neurodegenerative disorder-related pathways and metabolic pathways were downregulated. Production of prostaglandin E 2 (PGE 2 ), interleukin-6, tumor necrosis factor-α (TNF-α), and reactive oxygen species (ROS) was all inhibited by CA and CGA ( P < 0.05). PGE 2 and TNF-α were further suppressed in adduct-stimulated cells ( P < 0.05), but ROS production was increased. For example, TNF-α produced by 100 μM CGA-stimulated cells and 100 μM CGA-Cys adduct-stimulated cells were 4.46 ± 0.23 and 1.61 ± 0.18 ng/mL, respectively. Thus, the addition of the Cys moiety drastically alters the anti-inflammatory activity of phenolic compounds.

Quinones are electrophilic compounds that can undergo Michael addition or Schiff base reaction with nucleophilic amines, but the effect of temperature has not been systematically studied. The aim of this study was to characterize how temperature affects the reaction mechanism and kinetics of 4-methylbenzoquinone (4MBQ) with lysine (Lys), N α -acetyl Lys or N ε -acetyl Lys. The products were identified and characterized by LC-MS/MS, which revealed formation of Michael addition products, Schiff base, and a di-adduct in Lys and N α -acetyl Lys-containing reaction mixtures. The product profiles were not affected by temperature in the range of 15-100 °C. NMR analysis proved that Michael addition of N α -acetyl Lys occurred on the C5 position of 4MBQ. Rate constants for the reactions studied by stopped-flow UV-vis spectrophotometry under pseudo-first-order conditions where the amines were present in excess in the range 15 °C to 45 °C showed the α-amino groups of Lys are more reactive than the ε-groups. The kinetics results revealed that the temperature dependence of reaction rates followed the Arrhenius law, with activation energies in the order: Lys < N ε -acetyl Lys < N α -acetyl Lys. Our results provide detailed knowledge about the temperature dependence of the reaction between Lys residues and quinones under conditions relevant for storage of foods., Competing Interests: Declaration of Competing Interest The authors declare the following financial interests/personal relationships which may be considered as potential competing interests: Marianne Nissen Lund reports financial support was provided by Independent Research Fund Denmark. Jingyuan Liu reports financial support was provided by China Scholarship Council., (Copyright © 2022 The Author(s). Published by Elsevier Ltd.. All rights reserved.)

Proteins are important macronutrients for the human body to grow and function throughout life. Although proteins are found in most foods, their very dissimilar digestibility must be taking into consideration when addressing the nutritional composition of a diet. This review presents a comprehensive summary of the in vitro digestibility of proteins from plants, milk, muscle, and egg. It is evident from this work that protein digestibility greatly varies among foods, this variability being dependent not only upon the protein source, but also the food matrix and the molecular interactions between proteins and other food components (food formulation), as well as the conditions during food processing and storage. Different approaches have been applied to assess in vitro protein digestibility (IVPD), varying in both the enzyme assay and quantification method used. In general, animal proteins tend to show higher IVPD. Harsh technological treatments tend to reduce IVPD, except for plant proteins, in which thermal degradation of anti-nutritional compounds results in improved IVPD. However, in order to improve the current knowledge about protein digestibility there is a vital need for understanding dependency on a protein source, molecular interaction, processing and formulation and relationships between. Such knowledge can be used to develop new food products with enhanced protein bioaccessibility.

Protein-polyphenol adducts are formed upon covalent bonding between oxidized polyphenols and proteins. 4-Methylcatechol (4MC) is a polyphenol with origin in coffee and is oxidized to 4-methylbenzoquinone (4MBQ) under conditions used during food processing. The present study characterizes 4MBQ-induced covalent modifications on β-lactoglobulin (β-LG) from bovine milk, (henceforth β-LQ) and the effect on protein digestibility. Significant thiol and amine loss was found in β-LQ compared to β-LG. Site-specific 4MBQ-induced modifications were identified on Cys, Lys, Arg, His and Trp in β-LQ. No significant differences between β-LG and β-LQ on in vitro digestibility were observed by assessment with SDS-PAGE, degree of hydrolysis and LC-MS/MS unmodified peptide intensities. Cys-4MC adduct (1.7 ± 0.1 µmol/g) was released from β-LQ after in vitro digestion. Thus, it is relevant to investigate how released Cys-4MC adducts are absorbed in vivo in future studies., (Copyright © 2022 The Authors. Published by Elsevier Ltd.. All rights reserved.)

Background: Hempseed meal, a by-product of the hempseed oil processing stream, is a potential alternative source for food proteins. Efficient extraction of proteins from hempseed meal is challenging owing to differences in the structure and solubility of various protein fractions present in the seed. In the present study, protein was extracted from hempseed meal using four different solvents, including aqueous NaOH, KOH, NaHCO 3 and NaCl, at four different concentrations with the aim of improving the recovery of protein fractions rich in essential amino acids., Results: Extraction using alkaline solvents provided superior protein recovery (60-78%) compared with NaCl solution and control extractions (20-48% and 21%, respectively). The concentration of alkali or salt (0.25-1 mol L -1 ) had a minor but significant impact on the yield. Amino acid composition analysis revealed that hempseed meal contains 24% (54.5 ± 0.19 mg g -1 ) essential amino acids of total amino acids, and extraction with NaOH, KOH, NaHCO 3 or NaCl did not improve the selective extraction of essential amino acids compared to control experiments. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis allowed the identification of edestin and albumin in the extracts obtained with NaHCO 3 and NaCl solvents, with results further showing that the type of extraction solvent influences protein extraction selectivity., Conclusion: Although alkali solvents provide superior extraction yields, extraction with water resulted in extracts containing the highest proportion of proteins bearing essential amino acids. According to the results of SDS-PAGE, extraction using alkali solvents induced protein crosslinking. © 2022 The Authors. Journal of The Science of Food and Agriculture published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry., (© 2022 The Authors. Journal of The Science of Food and Agriculture published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry.)

Protein is a major nutrient present in foods along with carbohydrates and lipids. Food proteins undergo a wide range of modifications during food production, processing, and storage. In this review, we discuss two major reactions, oxidation and the Maillard reaction, involved in chemical modifications of food proteins. Protein oxidation in foods is initiated by metal-, enzyme-, or light-induced processes. Food protein oxidation results in the loss of thiol groups and the formation of protein carbonyls and specific oxidation products of cysteine, tyrosine, tryptophan, phenylalanine, and methionine residues, such as disulfides, dityrosine, kynurenine, m -tyrosine, and methionine sulfoxide. The Maillard reaction involves the reaction of nucleophilic amino acid residues with reducing sugars, which yields numerous heterogeneous compounds such as α-dicarbonyls, furans, Strecker aldehydes, advanced glycation end-products, and melanoidins. Both protein oxidation and the Maillard reaction result in the loss of essential amino acids but may positively or negatively impact food structure and flavor.

Fermented persimmon juice, Kakishibu, has traditionally been used for wood and paper protection. This protective effect stems at least partially from inhibition of microbial cellulose degrading enzymes. The inhibitory effect of Kakishibu on lytic polysaccharide monooxygenases (LPMOs) and on a cocktail of cellulose hydrolases was studied, using three different cellulosic substrates. Dose dependent inhibition of LPMO activity by a commercial Kakishibu product was assessed for the well-characterized LPMO from Thermoascus aurantiacus TaAA9A, and the inhibitory effect was confirmed on five additional microbial LPMOs. The model tannin compound, tannic acid exhibited a similar inhibitory effect on TaAA9A as Kakishibu. It was further shown that both polyethylene glycol and tannase can alleviate the inhibitory effect of Kakishibu and tannic acid, indicating a likely mechanism of inhibition caused by unspecific tannin-protein interactions.

Lytic polysaccharide monooxygenases (LPMOs) are monocopper enzymes of industrial and biological importance. In particular, LPMOs play important roles in fungal lifestyle. No inhibitors of LPMOs have yet been reported. In this study, a diverse library of 100 plant extracts was screened for LPMO activity-modulating effects. By employing protein crystallography and LC-MS, we successfully identified a natural LPMO inhibitor. Extract screening revealed a significant LPMO inhibition by methanolic extract of Cinnamomum cassia (cinnamon), which inhibited LsAA9A LPMO from Lentinus similis in a concentration-dependent manner. With a notable exception, other microbial LPMOs from families AA9 and AA10 were also inhibited by this cinnamon extract. The polyphenol cinnamtannin B1 was identified as the inhibitory component by crystallography. Cinnamtannin B1 was bound to the surface of LsAA9A at two distinct binding sites: one close to the active site and another at a pocket on the opposite side of the protein. Independent characterization of cinnamon extract by LC-MS and subsequent activity measurements confirmed that the compound inhibiting LsAA9A was cinnamtannin B1. The results of this study show that specific natural LPMO inhibitors of plant origin exist in nature, providing the opportunity for future exploitation of such compounds within various biotechnological contexts., (© 2021 The Authors. New Phytologist © 2021 New Phytologist Foundation.)

A targeted UHPLC-MS/MS isotopic dilution method has been developed for the simultaneous quantification of 18 different free and protein-bound aromatic amino acid oxidation products in food and biological matrices. All analytes, including critical isomeric pairs of Tyr, o-Tyr, m-Tyr, and dioxyindolylalanine diastereomers were chromatographically resolved to obtain high selectivity, without the need for derivatizing or ion pairing agents. The results of method validation showed adequate retention time reproducibility [0.1-0.6% coefficient of variation (CV) for over 224 injections], accuracy (within ±1-20% of the nominal concentration), and precision (1-17% CV) for all target analytes. The lower limit of quantification was calculated in different matrices using both the Hubaux-Vos approach and accuracy and precision data showing values in the range of 0.2-15 ng/mL. Use of stable isotope-labelled internal standards compensated errors due to matrix effects and artefactual degradation of analytes. Both acid and enzymatic hydrolyses were tested to obtain the best possible results for the quantification of protein oxidation products, demonstrating the stability of target analytes under hydrolytic conditions. The method was successfully applied to quantify target analytes in serum, tissue, milk, infant formula, pork liver pâté, chicken meat and fish. The method was also applied to assess the role of Fenton's reagent in oxidizing Trp, Phe and Tyr residues in different proteins, with results showing o-Tyr, dioxyindolylalanine diastereomers, kynurenine, dityrosine being the main oxidation products. The Fenton chemistry favored the formation of o-Tyr over m-Tyr from Phe with 2-36 folds higher yields. 3-Nitrotyrosine, a marker of protein nitration, was also detected in samples treated with Fenton's reagent., (Copyright © 2021 The Authors. Published by Elsevier B.V. All rights reserved.)

UV-B illumination facilitates aggregation of alpha-lactalbumin (α-LA) by intramolecular disulfide bond cleavage followed by intermolecular thiol-disulfide exchange reactions. However, long term exposure to UV-B illumination may induce undesired oxidative modifications of amino acid residues in the protein. The purpose of this study was to examine the effect of UV-induced aggregation of apo-α-LA (a calcium-depleted form of α-LA) under aerobic and anaerobic conditions and by addition of tryptophan (Trp) as a photosensitizer. The addition of Trp to apo-α-LA illuminated under anaerobic conditions facilitated the highest level of free thiol release and disulfide-mediated aggregation as compared to without addition of Trp under both anaerobic and aerobic conditions. Addition of Trp under aerobic condition resulted in the lowest level of free thiols and disulfide-mediated aggregation and the aerobic conditions caused oxidation of the free Trp with formation of kynurenine and 5-hydroxy-Trp. Minor levels of the Trp oxidation product, 3-hydroxy-kynurenine (2% converted from Trp), was formed in apo-α-LA with added Trp under both aerobic and anaerobic conditions after UV-B treatment.

Awareness towards utilizing food-processing by-products are increasing in health as well as environmental purview. Coffee silver skin (CSS), potato peel (PP) and brewer's spent grain (BSG) are voluminous by-products in their respective processing industries. The present study compared these three by-products for their prospective utilization in producing polyphenols-rich aqueous extracts by using ultrasound-assisted extractions (UAE). A probe-type sonicator was used for ultrasound treatments. The total phenolic contents in the extracts were assessed by Folin-Ciocalteu assay, while the phenolic profiles of the extract was characterized by LC-Q-TOF mass spectrometry. The microstructure of the samples after UAE was evaluated by scanning electron microscopy (SEM). Ultrasound treatment enhanced the rate of extraction and recovered 2.79, 2.12 and 0.66 mg gallic acid equivalents/g of TPC from CSS, PP and BSG, respectively in 30 min, which correspond to recoveries of 97.6%, 84.5% and 84.6%, respectively, compared to conventional solid-liquid extractions carried out for 24 h. The extraction yield was dependent on the particle size of the raw materials and the highest yield was obtained from the materials with 100-250 µm particle size. The SEM imaging revealed that ultrasound treatment caused prominent tissue damage. Extracts contained mainly hydroxycinnamic acid derivatives of phenolic acids. PP and CSS had the highest amounts of umami free amino acids (0.13 mg/g in each), while BSG contained the highest amount of essential amino acids (92 mg/g). The present work shows that CSS, PP and BSG are good sources of polyphenols and UAE can be employed to enhance the extraction efficiency as means of a green approach., (© Association of Food Scientists & Technologists (India) 2020.)

Seaweeds are a valuable potential source of protein, as well as free amino acids (FAAs) with umami flavour which are in high demand by the food industry. The most commonly used flavouring agents in the food industry are chemically synthesised and therefore are subject to concerns regarding their safety and associated consumer resistance. This study focuses on the effects of extraction time (1 and 2 h) and solvents (0.1 M HCl, 1% citric acid and deionised water) on the extraction of protein and FAAs including umami FAAs from Irish brown seaweeds ( Ascophyllum nodosum and Fucus vesiculosus ). Extraction yields were influenced by both the extraction solvent and time, and also varied according to the seaweed used. Both seaweeds investigated were found to be good sources of protein, FAAs including umami FAAs, demonstrating potential application as flavouring agents in the food industry. Overall, the use of green solvents (deionised water and citric acid) resulted in higher recoveries of compounds compared to HCl. The results of this study will facilitate the use of more sustainable solvents in industry for the extraction of proteins and flavouring agents from seaweed., Competing Interests: Conflict of interestThe authors declare no competing interests., (© The Author(s) 2021.)

Epigallocatechin gallate (EGCG)-enriched green tea extract (GTE) was added to lactose-reduced UHT-treated milk to evaluate its role in perturbing the Maillard reaction and the formation of advanced glycation endproducts (AGEs) during 1-year storage. The UHT processing caused epimerization of EGCG into gallocatechin gallate (GCG). For milk samples with added 0.1% w/v GTE, a EGCG/GCG loss of 26% was found soon after the UHT treatment and the loss increased to 64% after the 1-year of storage. LC-MS/MS analysis revealed the presence of various EGCG/GCG-α-dicarbonyl adducts and EGCG/GCG-hydroxymethylfurfural adducts in milk samples, while EGCG/GCG-amino acid adducts were not detected. Although EGCG/GCG trapped α-dicarbonyl compounds including glyoxal, methylglyoxal, 3-deoxyglucosone/3-deoxygalactosone, and diacetyl, it did not lower their net steady-state concentrations, except of 3-deoxyglucosone. The addition of GTE reduced the formation of Arg-derived AGEs by 2- to 3-fold, but surprisingly enhanced the accumulation of furosine and lysine-derived AGEs [ N ε-(carboxymethyl)lysine and N ε-(carboxyethyl)lysine)] by 2-4-fold depending on the concentration of the added GTE and storage time. The present study shows that trapping of α-dicarbonyl compounds by EGCG may not be the major pathway for inhibiting the formation of AGEs in milk.

Reaction kinetics for the reactions between four polyphenols (trans-resveratrol, apigenin, kaempferol and fisetin) and methylglyoxal (MGO) were determined at pH 7.4 and 37 °C, and the effect of functional groups of polyphenols on MGO trapping ability was examined. Reaction products of polyphenols with MGO were characterized by HPLC-MS/MS. The apparent second order rate constants for the reaction of MGO with trans-resveratrol, apigenin, kaempferol and fisetin were (2.7 ± 0.2) × 10 -2 M -1 s -1 , (4.4 ± 0.4) × 10 -3 M -1 s -1 , (6.3 ± 0.2) × 10 -2 M -1 s -1 , and (3.6 ± 0.1) × 10 -3 M -1 s -1 , respectively. The rate constants were used to evaluate the possible competition between MGO with nucleophilic sites on proteins and polyphenols at concentrations relevant to UHT milk. Combining this information with solubility and flavour of the polyphenols, it was concluded that kaempferol could effectively trap MGO and hereby inhibit Maillard reactions in UHT milk., 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 © 2020 Elsevier Ltd. All rights reserved.)

The kinetics of the reaction between epicatechin and various carbonyl compounds typically formed in cooked and stored foods were evaluated in model systems at pH 7.4 and 37 °C, and the corresponding reaction products in stored ultrahigh temperature (UHT) milk-added epicatechin were identified by high-performance liquid chromatography-tandem mass spectrometry (HPLC-MS/MS). The rate constants for the reactions of carbonyl compounds with epicatechin decreased in the following the order: methylglyoxal; 1.6 ± 0.2 M -1 s -1 > glyoxal; (5.9 ± 0.3) × 10 -2 M -1 s -1 ≥ 5-(hydroxymethyl)furfural; (4.0 ± 0.2) × 10 -2 M -1 s -1 ≥ acetaldehyde; (2.6 ± 0.3) × 10 -2 M -1 s -1 ≥ phenylacetaldehyde; (2.1 ± 0.2) × 10 -2 M -1 s -1 ≥ furfural; (4.3 ± 0.1) × 10 -3 M -1 s -1 > 2-methylbutanal and 3-methylbutanal; ∼0 M -1 s -1 . Reaction products generated by epicatechin and methylglyoxal, glyoxal, 5-(hydroxymethyl)furfural, and acetaldehyde were detected in UHT milk samples by incubating milk samples with epicatechin at 37 °C for 24 h. The lack of reaction between epicatechin and phenylacetaldehyde, furfural, 2-methylbutanal, and 3-methylbutanal in stored UHT milk may be due to their slow reaction rates or low concentration in stored UHT milk. It is demonstrated that epicatechin traps 5-(hydroxymethyl)furfural, acetaldehyde, glyoxal, and methylglyoxal and may thereby reduce off-flavor formation in UHT milk during storage both by trapping of precursors (methylglyoxal and glyoxal) for off-flavor formation and by direct trapping of off-flavors.

Photolytic cleavage of disulfide bonds in proteins by UV light will influence their structure and functionality. The present study aimed to investigate the efficiency of disulfide cleavage by UV-B light in a system without a protein backbone consisting of combinations of cystine (a disulfide) and tryptophan (Trp) or tyrosine (Tyr) under anaerobic and aerobic conditions and to identify oxidation products formed by UV-B light. Cystine was reduced to cysteine (Cys) almost with a 1:1 stoichiometry by photoexcited Trp for anaerobic equimolar aqueous solutions (each 200 μM; pH 7.0), while photoexcited Tyr provided lower concentrations of Cys. The calculation of apparent quantum yields allowed for a comparison between the efficiency of reactions and showed that formation of Cys from disulfide cleavage of cystine was more efficient by photoexcited Trp than by photoexcited Tyr and of cystine alone and that Trp was more sensitive to photodegradation than Tyr and cystine under both aerobic and anaerobic conditions. Increasing the ratio between cystine and Trp to a 1:2 ratio did not increase the efficiency of free thiol formation but caused a more efficient photodegradation of Trp. The free thiol formed from disulfide cleavage of cystine was further oxidized to other unidentified compounds. Trp oxidation products (3-hydroxykynurenine (3-OH-Kyn) and tryptamine) were only identified in minor concentrations following light exposure of cystine and Trp in 1:1 and 1:2 ratios under both aerobic and anaerobic conditions, indicating further photodegradation to unidentified compounds. 3,4-Dihydroxyphenylalanine (DOPA) was formed from the oxidation of Tyr in the illuminated samples of cystine and Tyr in a 1:1 ratio under both aerobic and anaerobic conditions.

Whey proteins are widely used as ingredients in the form of aggregates to obtain certain functionalities in food applications. The aim of this study was to understand how UV illumination generates aggregates of α-lactalbumin (α-LA) as an alternative to heat treatments traditionally used for industrial production of protein aggregates. Absorption of UV light by α-LA caused cleavage of disulfide bonds and release of thiol groups, which resulted in primarily disulfide-mediated aggregation. This process mediated efficient aggregation with up to 98% monomer conversion into aggregates through formation of intermolecular disulfide bonds, while only minor levels of nonreducible cross-links were observed. SDS-PAGE analysis revealed that illumination led to formation of dimeric, trimeric, and oligomeric forms of α-LA. LC-MS/MS analysis showed that all of the four native disulfide bonds in α-LA were cleaved by UV illumination but to different extents, and the extent of cleavage was found to be higher in the absence of calcium. Seventeen different non-native disulfides were formed after 24 h of UV illumination. Two dityrosine bonds were identified (Tyr103-Tyr103 and Tyr36-Tyr103) alongside ditryptophan (Trp118-Trp118) and tyrosine-tryptophan (Tyr50-Trp60) cross-links. In addition, Trp60, Trp118, Cys73, Cys91, Cys120, Phe80, Met90, His68, and His107 were found to be oxidized up to 12% as compared to a nonilluminated control. Our work illustrates that light exposure can be used for generation of α-LA aggregates, but optimization of the illumination conditions is required to reduce oxidative damage to Trp, Cys, Phe, Met, and His residues.

Advanced glycation end products (AGEs) and protein cross-links have been extensively investigated in both food and biomedical fields over the past years. Although there are a few chromatographic and immunological methods for the analysis of selected AGEs, there is no method available for comprehensive simultaneous analysis of major AGEs found in processed foods and biological samples. In the present study, we have reported a validated UHPLC-MS/MS method for simultaneous identification and quantification of 15 different AGEs, furosine (an indicator of Amadori products), 2 protein-derived cross-links (lanthionine and lysinoalanine) and 2 amino acids (Lys and Arg). The analytes were separated on a reversed phase C-18 column and quantified accurately based on the isotope dilution method, where 9 stable isotope-labelled internal standards were used to quantify 20 different analytes using an Orbitrap mass analyzer. The method showed acceptable linearity, accuracy and precision. The LOD and LOQ values in plasma were in the range of 0.30-19.02 and 0.87-57.06 ng/mL, respectively. The recovery values at the three spiked levels were in the range of 71-110%, with some exceptions. The intraday and interday precision were in the range of 1.5-13.2%, however, quantification of N-ɛ-(carboxymethyl)lysine accompanied slightly higher interday precision (30.7%). The applicability of the method was successfully assessed by analyzing AGEs and protein cross-links in six different complex matrices including Ultra-High Temperature (UHT) processed milk, roasted chicken breast meat, roasted chicken skin, roasted pork liver, bovine plasma and perfusion liquid., 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 © 2019 Elsevier B.V. All rights reserved.)

Lactose-hydrolyzed (LH) ultrahigh temperature (UHT) processed milk is more prone to Maillard reactions and formation of advanced glycation end products (AGEs) during processing and storage than conventional (CON) UHT milk because of the presence of free galactose and glucose. Commercially available β-d-galactosidases with transgalactosylating activity can incorporate galactose into galactooligosaccharides (GOSs) and potentially limit Maillard reactions in this lactose-reduced GOS-containing milk. The aim of this study was to examine the extent of Maillard reactions in a lactose-reduced GOS milk compared to LH and CON milk after UHT processing. The GOS milk had significant lower levels of lysine- and arginine-derived AGEs compared to LH milk, while their concentrations were similar to those found in CON milk. The total concentration of measured Arg-derived AGEs was similar to the total concentration of Lys-derived AGEs in the three types of milk, indicating that Arg is an important source of AGEs in milks. Interestingly, the GOS milk generated threefold higher concentrations (up to 330 ± 6 μM) of 3-deoxyglucosone (3-DG, a C6 α-dicarbonyl). These results demonstrate that GOS milk could be a potential alternative for LH milk for lactose-intolerant individuals, although further studies are needed to understand the increased formation of 3-DG in GOS-containing milk.

Protein oxidation of beef patties stored in high oxygen modified atmosphere packaging for 9 days was investigated. Meat was either stored in the dark, under light, or in the dark with addition of FeCl 2 /H 2 O 2 /myoglobin (forced oxidation). SDS-PAGE analysis showed high degree of protein polymerization for meat exposed to light, compared to the other samples. Light exposure induced reducible (disulfide) and non-reducible cross-links, while mainly disulfides were formed in meat stored in the dark. Light exposure was responsible for 58% loss of free thiols (Cys residues). No significant loss of other amino acid residues was observed and none of the most common oxidation products of tryptophan, tyrosine, and phenylalanine were detected. Intrinsic fluorescence measurements of tryptophan showed 27% loss in samples exposed to light, which was ascribed to loss of protein solubility via protein polymerization rather than tryptophan oxidation. Protein carbonyls were mainly detected in forced oxidized samples at Day 0., (Copyright © 2019 Elsevier Ltd. All rights reserved.)

A comprehensive quantitative characterization of Maillard reaction products was carried out for conventional (CON) and lactose-hydrolyzed (LH) ultrahigh temperature (UHT) milk during storage at 20, 30, and 40 °C for 1 year. The accumulation of 3-deoxyglucosone (3-DG) and 3-deoxygalactosone (3-DGal) in LH-UHT milk ranged from 20-fold (at 20 °C) to 44-fold (at 40 °C) higher than that in CON-UHT milk. High temperature storage (40 °C) significantly accelerated the accumulation of 3-DG, 3-DGal, and 5-hydroxymethyl furfural but not the majority of the analyzed advanced glycation endproducts (AGEs). The concentrations of major AGEs including N -ε-carboxymethyllysine (CML), N -ε-carboxyethyllysine (CEL), methylglyoxal-hydroimidazolone isomers (MG-H1/H3), glyoxal-hydroimidazolone isomers (G-H1/H3), and G-H2 detected in CON milk during storage were in the range 12-700, 1-14, 8-45, 4-13, and 1-30 μM, respectively, while they were 30-570, 2-88, 17-150, 9-20, and 5-34 μM, respectively, in LH milk. Pyrraline, S -(carboxymethyl)cysteine (CMC), and glyoxal-lysine dimer were detected in lower levels, while MG-H2, methylglyoxal-lysine dimer, argpyrimidine, glyoxal-lysine-amide, glycolic acid-lysine-amide, and pentosidine were not detected in any of the milk samples. This work demonstrates for the first time that five of the analyzed AGEs (CML, CEL, MG-H1/H3, G-H1/H3, and G-H2) could be selected as markers for evaluation of the extent of the Maillard reaction in UHT milk. These results contribute to a better understanding of how Maillard reactions progress during storage of UHT milk and can be used to develop strategies to inhibit Maillard reactions in LH milk.

Methylglyoxal (MGO) is a highly reactive ɑ-dicarbonyl compound that may adversely impact food quality and human health by modifying proteins. The kinetics of the reaction of naringenin with MGO was studied at pH 6-8 and 37 °C by UV-Vis spectrophotometry and reaction products were characterized by liquid chromatography-mass spectrometry (LC-MS/MS). The apparent second order rate constant (k 2 ) increased at pH above the lowest pKa value of naringenin, indicating deprotonated naringenin as the main reactant. A Lederer-Manasse type reaction mechanism is suggested, with dehydration of the MGO-dihydrate as a rate determining step. The quantitative data obtained in the present study was used to simulate the competitive reaction between MGO and nucleophilic amino acid residues (Lys, Arg and Cys) and naringenin in milk. It is predicted that naringenin will be able to efficiently trap MGO during storage of milk, although the reversible trapping of MGO by Cys residues is initially kinetically favourable., (Copyright © 2019 Elsevier Ltd. All rights reserved.)

α-Dicarbonyls are reactive intermediates formed during Maillard reactions and carbohydrate degradation. The formation of seven α-dicarbonyls was characterized in solutions containing dairy related carbohydrates (galactose, glucose, lactose, and galacto-oligosaccharides (GOS)) during incubations at 40 and 50 °C with and without Nα-acetyl-l-lysine at pH 6.8 for up to 2 months. The concentrations of α-dicarbonyls in samples of monosaccharides with Nα-acetyl-l-lysine were found to be 3-deoxyglucosone (3-DG) > 3-deoxygalactosone (3-DGal) > glyoxal > glucosone, galactosone > methylglyoxal > diacetyl. The presence of Nα-acetyl-l-lysine resulted in up to 100-fold higher concentrations of C6 α-dicarbonyls but lesser formation of glyoxal in the monosaccharide-containing models compared to what was observed in the absence of Nα-acetyl-l-lysine. Galactose incubated with Nα-acetyl-l-lysine generated the highest concentrations of 3-DGal (up to 130 μM), glyoxal (up to 100 μM), and methylglyoxal (up to 9 μM) compared to the other carbohydrates during incubation. Surprisingly, 3-DG (1500 μM) and 3-DGal (80 μM) were formed at levels of 2 orders of magnitude higher in solutions of GOS in the absence of Nα-acetyl-l-lysine as compared to the other carbohydrates at 40 °C, while GOS generated the lowest levels of glyoxal. GOS are widely used as an ingredient in various types of foods products, and it is therefore of importance to consider the risk of generating high levels of the reactive C6 α-dicarbonyl, 3-DG, in these types of products. This study contributes to the understanding of major α-dicarbonyl formation as affected by the presence of primary amines in GOS-, lactose-, and galactose-containing solutions under moderate heating in liquid foods.

Lactose reduced dairy products are more prone to Maillard reactions due to the presence of reactive monosaccharides. Conventional β-galactosidases, which are used for lactose hydrolysis in lactose-reduced dairy products, will lead to conversion of lactose into glucose and galactose, where especially galactose is very reactive during Maillard reactions. Some β-galactosidases have transgalactosylating activity and will thus convert lactose into galacto-oligosaccharides (GOS) and hereby limit the release of galactose. The aim of this study was to investigate the extent of participation of GOS in Maillard reactions in comparison to lactose, a 50:50 mixture of glucose and galactose, and galactose exclusively in sodium caseinate-based milk-like model systems heated at 130 and 75 °C at pH 6.8. The GOS system exhibited reduced loss of free amino groups; accumulated less furosine and less of the following advanced glycation end products (AGEs): N ε -carboxyethyl lysine, methylglyoxal-derived hydroimidazolone isomers, glyoxal-derived lysine dimer, and methylglyoxal-derived lysine dimer; and also developed less browning compared to monosaccharide models. However, the GOS-caseinate system accumulated more 3-deoxyglucosone and 3-deoxygalactosone, which resulted in higher concentrations of 5-(hydroxymethyl)furfural and pyrraline. The results indicated that GOS overall participate less readily in Maillard reactions than the monosaccharides investigated but were more prone to degradation to C6 α-dicarbonyls species. Finally, relationship analysis indicated that C6 α-dicarbonyls seemed to primarily increase concentrations of 5-(hydroxymethyl)furfural instead of AGEs. Our results suggest that conversion of lactose into GOS instead of monosaccharides in milk by transgalactosylating β-galactosidases could be a useful strategy for production of lactose-free milk for people with lactose intolerance.

Background: Metabolomics aims to identify the changes in endogenous metabolites of biological systems in response to intrinsic and extrinsic factors. This is accomplished through untargeted, semi-targeted and targeted based approaches. Untargeted and semi-targeted methods are typically applied in hypothesis-generating investigations (aimed at measuring as many metabolites as possible), while targeted approaches analyze a relatively smaller subset of biochemically important and relevant metabolites. Regardless of approach, it is well recognized amongst the metabolomics community that gas chromatography-mass spectrometry (GC-MS) is one of the most efficient, reproducible and well used analytical platforms for metabolomics research. This is due to the robust, reproducible and selective nature of the technique, as well as the large number of well-established libraries of both commercial and 'in house' metabolite databases available., Aim of Review: This review provides an overview of developments in GC-MS based metabolomics applications, with a focus on sample preparation and preservation techniques. A number of chemical derivatization (in-time, in-liner, offline and microwave assisted) techniques are also discussed. Electron impact ionization and a summary of alternate mass analyzers are highlighted, along with a number of recently reported new GC columns suited for metabolomics. Lastly, multidimensional GC-MS and its application in environmental and biomedical research is presented, along with the importance of bioinformatics., Key Scientific Concepts of Review: The purpose of this review is to both highlight and provide an update on GC-MS analytical techniques that are common in metabolomics studies. Specific emphasis is given to the key steps within the GC-MS workflow that those new to this field need to be aware of and the common pitfalls that should be looked out for when starting in this area.

"Horchata de chufa" is a traditional Spanish beverage produced from tiger nuts (Cyperus esculentus L.). Due to its richness in nutritional compounds, it is highly perishable and its conservation by pasteurization and/or adding preservatives is required. Although efficient, conventional thermal treatment for pasteurization induces changes in the nutritional and sensory properties. Replacing conventional pasteurization by non-thermal technologies such as pulsed electric fields, ultraviolet, and high pressure, combined with moderate temperatures (<40°C) allows a reduction of energy consumption, along with the preservation of the most thermo-sensitive molecules. Accordingly, this review deals with the description of the most relevant non-thermal technologies applied to preserve "horchata" beverage in order to extend the shelf life and inactivate pathogenic microorganisms as well as to preserve the nutritional and quality properties of this food beverage., (Copyright © 2017 Elsevier Ltd. All rights reserved.)

The effect of epigallocatechin gallate enriched green tea extract (GTE) on flavor, Maillard reactions and protein modifications in lactose-hydrolyzed (LH) ultrahigh temperature (UHT) processed milk was examined during storage at 40 °C for up to 42 days. Addition of GTE inhibited the formation of Strecker aldehydes by up to 95% compared to control milk, and the effect was similar when GTE was added either before or after UHT treatment. Release of free amino acids, caused by proteolysis, during storage was also decreased in GTE-added milk either before or after UHT treatment compared to control milk. Binding of polyphenols to milk proteins was observed in both fresh and stored milk samples. The inhibition of Strecker aldehyde formation by GTE may be explained by two different mechanisms; inhibition of proteolysis during storage by GTE or binding of amino acids and proteins to the GTE polyphenols.

In this study, enzyme-assisted extraction was performed to extract umami taste and total free amino acids (FAAs) from the six different mushrooms including shiitake (Lentinus edodes), oyster (Pleurotus ostreatus), tea tree (Agrocybe aegerita) and, white, brown and portobello champignons (Agaricus bisporus). β-Glucanase and Flavourzyme® were used as the enzymes for cell wall and proteins hydrolysis, respectively. It was found that β-glucanase treatment alone did not enhance the extraction efficiency, however in combination, β-glucanase and Flavourzyme® enhanced the extraction efficiency significantly up to 20-fold compared to conventional HCl mediated extraction, depending on the mushroom species. The optimal conditions for the enzyme treatment were: water as extraction solvent (initial pH = 7), enzyme concentration of 5% v/w each of β-glucanase and Flavourzyme®, temperature 50°C and an incubation time of 1h. White and brown champignons were found to be the richest source of umami taste FAAs (26.75±1.07 and 25.6±0.9mg/g DM, respectively)., (Copyright © 2017 Elsevier Ltd. All rights reserved.)

Over the last several decades, γ-aminobutyric acid (GABA) has attracted much attention due to its diverse physiological implications in plants, animals, and microorganisms. GABA naturally occurs in plant materials and its concentrations may vary considerably, from traces up to μmol/g (dry basis) depending on plant matrix, germination stage, and processing conditions, among other factors. However, due to its important biological activities, considerable interest has been shown by both food and pharmaceutical industries to improve its concentration in plants. Natural and conventional treatments such as mechanical and cold stimulation, anoxia, germination, enzyme treatment, adding exogenous glutamic acid (Glu) or gibberellins, and bacterial fermentation have been shown effective to increase the GABA concentration in several plant materials. However, some of these treatments can modify the nutritional, organoleptic, and/or functional properties of plants. Recent consumer demand for food products which are "healthy," safe and, having added benefits (nutraceuticals/functional components) has led to explore new ways to improve the content of bioactive compounds while maintaining desirable organoleptic and physicochemical properties. Along this line, nonthermal processing technologies (such as high-pressure processing, pulsed electric fields, and ultrasound, among others) have been shown as means to induce the biosynthesis and accumulation of GABA in plant foods; and the main findings so far reported are presented in this review. Moreover, the most novel tools for the identification of metabolic response in plant materials based on GABA analysis will be also described., (© 2017 Institute of Food Technologists®.)

This paper reports on improved conventional thermal silylation (CTS) and microwave-assisted silylation (MAS) methods for simultaneous determination of tocopherols and sterols by gas chromatography. Reaction parameters in each of the methods developed were systematically optimized using a full factorial design followed by a central composite design. Initially, experimental conditions for CTS were optimized using a block heater. Further, a rapid MAS was developed and optimized. To understand microwave heating mechanisms, MAS was optimized by two distinct modes of microwave heating: temperature-controlled MAS and power-controlled MAS, using dedicated instruments where reaction temperature and microwave power level were controlled and monitored online. Developed methods: were compared with routine overnight derivatization. On a comprehensive level, while both CTS and MAS were found to be efficient derivatization techniques, MAS significantly reduced the reaction time. The optimal derivatization temperature and time for CTS found to be 55°C and 54min, while it was 87°C and 1.2min for temperature-controlled MAS. Further, a microwave power of 300W and a derivatization time 0.5min found to be optimal for power-controlled MAS. The use of an appropriate derivatization solvent, such as pyridine, was found to be critical for the successful determination. Catalysts, like potassium acetate and 4-dimethylaminopyridine, enhanced the efficiency slightly. The developed methods showed excellent analytical performance in terms of linearity, accuracy and precision., (Copyright © 2016 Elsevier B.V. All rights reserved.)

Marine microalgae and seaweeds (microalgae) represent a sustainable source of various bioactive natural carotenoids, including β-carotene, lutein, astaxanthin, zeaxanthin, violaxanthin and fucoxanthin. Recently, the large-scale production of carotenoids from algal sources has gained significant interest with respect to commercial and industrial applications for health, nutrition, and cosmetic applications. Although conventional processing technologies, based on solvent extraction, offer a simple approach to isolating carotenoids, they suffer several, inherent limitations, including low efficiency (extraction yield), selectivity (purity), high solvent consumption, and long treatment times, which have led to advancements in the search for innovative extraction technologies. This comprehensive review summarizes the recent trends in the extraction of carotenoids from microalgae and seaweeds through the assistance of different innovative techniques, such as pulsed electric fields, liquid pressurization, supercritical fluids, subcritical fluids, microwaves, ultrasounds, and high-pressure homogenization. In particular, the review critically analyzes technologies, characteristics, advantages, and shortcomings of the different innovative processes, highlighting the differences in terms of yield, selectivity, and economic and environmental sustainability., Competing Interests: The authors declare no conflict of interest.

The aim of this work was to optimize the extraction of pure all-trans-lycopene from the pulp fractions of tomato processing waste. A full factorial design (FFD) consisting of four independent variables including extraction temperature (30-50 °C), time (1-60 min), percentage of acetone in n-hexane (25-75%, v/v) and solvent volume (10-30 ml) was used to investigate the effects of process variables on the extraction. The absolute amount of lycopene present in the pulp waste was found to be 0.038 mg/g. The optimal conditions for extraction were as follows: extraction temperature 20 °C, time 40 min, a solvent composition of 25% acetone in n-hexane (v/v) and solvent volume 40 ml. Under these conditions, the maximal recovery of lycopene was 94.7%. The HPLC-DAD analysis demonstrated that, lycopene was obtained in the all-trans-configuration at a very high purity grade of 98.3% while the amount of cis-isomers and other carotenoids were limited., (Copyright © 2015 Elsevier Ltd. All rights reserved.)

The present work involves extraction of phytochemicals from the root bark of a well-known Indian traditional medicinal plant, viz. Mammea suriga , with various solvents and evaluation of their in vitro antimicrobial and antioxidant activities using standard methods. The phytochemical analysis indicates the presence of some interesting secondary metabolites like flavonoids, cardiac glycosides, alkaloids, saponins and tannins in the extracts. Also, the solvent extracts displayed promising antimicrobial activity against Staphylococcus aureus , Bacillus subtilis and Cryptococcus neoformans with inhibition zone in a range of 20-33 mm. Further, results of their antioxidant screening revealed that aqueous extract (with IC 50 values of 111.51±1.03 and 31.05±0.92 μg/mL in total reducing power assay and DPHH radical scavenging assay, respectively) and ethanolic extract (with IC 50 values of 128.00±1.01 and 33.25±0.89 μg/mL in total reducing power assay and DPHH radical scavenging assay, respectively) were better antioxidants than standard ascorbic acid. Interestingly, FT-IR analysis of each extract established the presence of various biologically active functional groups in it.

Lycopene, a nutraceutical compound, was extracted from tomato processing waste, an abundantly available food industry by-product in Italy. The extraction kinetics was mathematically described using the first order kinetic model, the mass transfer model and Peleg's model to understand the physicochemical behaviour of the extraction. Samples were extracted using acetone/n-hexane mixtures at different ratios (1:3, 2:2 and 3:1, v/v) and at different temperatures (30, 40 and 50 °C) and simultaneously analysed using UV-VIS spectrophotometry. The lycopene yield was in the range 3.47-4.03 mg/100g, which corresponds to a percentage recovery of 65.22-75.75. All kinetic models gave a good fit to the experimental data, but the best one was Peleg's model, having the highest RAdj(2) and the lowest RMSE, MBE and χ(2) values. All the models confirmed that a temperature of 30 °C and solvent mixture of acetone/n-hexane 1:3 (v/v) provided optimal conditions for extraction of lycopene., (Copyright © 2014 Elsevier Ltd. All rights reserved.)