Physicochemical and Microstructural Characterization of Whey Protein Films Formed with Oxidized Ferulic/Tannic Acids

Protein-based biodegradable packaging films are of environmental significance. The effect of oxidized ferulic acid (OFA)/tannic acid (OTA) on the crosslinking and film-forming properties of whey protein isolate (WPI) was investigated. Both of the oxidized acids induced protein oxidation and promoted WPI crosslinking through the actions of quinone carbonyl and protein sulfhydryl, and amino groups. OTA enhanced the tensile strength (from 4.5 MPa to max 6.7 MPa) and stiffness (from 215 MPa to max 376 MPa) of the WPI film, whereas OFA significantly increased the elongation at break. The water absorption capability and heat resistance of the films were greatly improved by the addition of OTA. Due to the original color of OTA, the incorporation of OTA significantly reduced light transmittance of the WPI film (λ 200–600 nm) as well as the transparency, whereas no significant changes were induced by the OFA treatment. Higher concentrations of OTA reduced the in vitro digestibility of the WPI film, while the addition of OFA had no significant effect. Overall, these two oxidized polyphenols promoted the crosslinking of WPI and modified the film properties, with OTA showing an overall stronger efficacy than OFA due to more functional groups available

Protein Oxidation in Foods: Mechanisms, Consequences, and Antioxidant Solutions

Protein oxidation in foods remains a topic of the utmost scientific interest [...

Animal and Plant Protein Oxidation: Chemical and Functional Property Significance

Protein oxidation, a phenomenon that was not well recognized previously but now better understood, is a complex chemical process occurring ubiquitously in food systems and can be induced by processing treatments as well. While early research concentrated on muscle protein oxidation, later investigations included plant, milk, and egg proteins. The process of protein oxidation involves both radicals and nonradicals, and amino acid side chain groups are usually the site of initial oxidant attack which generates protein carbonyls, disulfide, dityrosine, and protein radicals. The ensuing alteration of protein conformational structures and formation of protein polymers and aggregates can result in significant changes in solubility and functionality, such as gelation, emulsification, foaming, and water-holding. Oxidant dose-dependent effects have been widely reported, i.e., mild-to-moderate oxidation may enhance the functionality while strong oxidation leads to insolubilization and functionality losses. Therefore, controlling the extent of protein oxidation in both animal and plant protein foods through oxidative and antioxidative strategies has been of wide interest in model system as well in in situ studies. This review presents a historical perspective of food protein oxidation research and provides an inclusive discussion of the impact of chemical and enzymatic oxidation on functional properties of meat, legume, cereal, dairy, and egg proteins based on the literature reports published in recent decades

Partial Removal of Phenolics Coupled with Alkaline pH Shift Improves Canola Protein Interfacial Properties and Emulsion in In Vitro Digestibility

The effect of polyphenol removal (“dephenol”) combined with an alkaline pH shift treatment on the O/W interfacial and emulsifying properties of canola seed protein isolate (CPI) was investigated. Canola seed flour was subjected to solvent extraction to remove phenolic compounds, from which prepared CPI was exposed to a pH12 shift to modify the protein structure. Dephenoled CPI had a light color when compared with an intense dark color for the control CPI. Up to 53% of phenolics were removed from the CPI after the extraction with 70% ethanol. Dephenoled CPI showed a partially unfolded structure and increased surface hydrophobicity and solubility. The particle size increased slightly, indicating that soluble protein aggregates formed after the phenol removal. The pH12 shift induced further unfolding and decreased protein particle size. Dephenoled CPI had a reduced β subunit content but an enrichment of disulfide-linked oligopeptides. Dephenol improved the interfacial rheology and emulsifying properties of CPI. Although phenol removal did not promote peptic digestion and lipolysis, it facilitated tryptic disruption of the emulsion particles due to enhanced proteolysis. In summary, dephenol accentuated the effect of the pH shift to improve the overall emulsifying properties of CPI and emulsion in in vitro digestion

The Effect of Batter Characteristics on Protein-Aided Control of Fat Absorption in Deep-Fried Breaded Fish Nuggets

Soy protein (SP), egg white protein (EP), and whey protein (WP) at 6% w/w were individually incorporated into the batter of a wheat starch (WS) and wheat gluten (WG) blend (11:1 w/w ratio). Moisture adsorption isotherms of WS and proteins and the viscosity, rheological behavior, and calorimetric properties of the batters were measured. Batter-breaded fish nuggets (BBFNs) were fried at 170 °C for 40 s followed by 190 °C for 30 s, and pick-up of BBFNs, thermogravimetric properties of crust, and fat absorption were determined. The moisture absorption capacity was the greatest for WS, followed by WG, SP, EP, and WP. The addition of SP significantly increased the viscosity and shear moduli (G″, G′) of batter and pick-up of BBFNs, while EP and WP exerted the opposite effect (p \u3c 0.05). SP, EP, and WP raised WS gelatinization and protein denaturation temperatures and crust thermogravimetry temperature, but decreased enthalpy change (ΔH) and oily characteristics of fried BBFNs. These results indicate that hydrophilicity and hydration activity of the added proteins and their interactions with batter matrix starch and gluten reinforced the batter and the thermal stability of crust, thereby inhibiting fat absorption of the BBFNs during deep-fat frying

Radical Scavenging Activity of Black Currant (\u3ci\u3eRibes nigrum\u3c/i\u3e L.) Extract and Its Inhibitory Effect on Gastric Cancer Cell Proliferation via Induction of Apoptosis

A black currant extract (BCE) was prepared and its antiproliferative activity against gastric cancer SGC-7901 cells was investigated. Strong 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical and 2,2′-azinobis(3-ethylbenzothiazoline-6-sulphonic acid) diammonium salt (ABTS) radical scavenging activities and a high reducing power were confirmed with BCE. BCE inhibited the proliferation of SGC-7901 cells in a dose- and time-dependent manner, and the IC50 were 12.7, 10.2 and 9.0 mg/mL for 12, 24 and 48 h, respectively. Morphologic observations with inverted and fluorescence microscopes yielded vivid evidence of cell shrinkage, formation of cytoplasmic filaments, condensation of nuclear chromatin, and cell apoptosis in the presence of BCE. Flow cytometric analysis also showed that BCE treatment at concentrations of 10–20 mg/mL resulted in marked reductions of viable cells. The high concentration of phenolic compounds present in the BCE (12.2 mg/mL), including six prominent anthocyanins identified by HPLC–ESI-MS2, appeared to be responsible for BCE’s antiradical activity and anticancer effects. These findings of inhibition of SGC-7901 cells and induction of apoptosis suggest that black currant may contribute to the reduction in gastric cancer risk

Effects of Supplementation of Microalgae (\u3cem\u3eAurantiochytrium\u3c/em\u3e sp.) to Laying Hen Diets on Fatty Acid Content, Health Lipid Indices, Oxidative Stability, and Quality Attributes of Meat

The present study is conducted to investigate the effects of dietary docosahexaenoic acid (DHA)-rich microalgae (MA, Aurantiochytrium sp.) on health lipid indices, stability, and quality properties of meat from laying hens. A total of 450 healthy 50-wk-old Hy-Line Brown layers were randomly allotted to 5 groups (6 replicates of 15 birds each), which received diets supplemented with 0, 0.5, 1.0, 1.5, and 2.0% MA for 15 weeks. Fatty acid contents and quality properties of breast and thigh muscles from two randomly selected birds per replicate (n = 12) were measured. The oxidative stability of fresh, refrigerated, frozen, and cooked meat was also determined. Results indicated that supplemental MA produced dose-dependent enrichments of long-chain n-3 polyunsaturated fatty acids (n-3 LC-PUFA), predominantly DHA, in breast and thigh muscles, with more health-promoting n-6/n-3 ratios (1.87-5.27) and favorable lipid health indices (p \u3c 0.05). MA supplementation did not affect tenderness (shear force) and color (L*, a*, and b* values) of hen meat nor muscle endogenous antioxidant enzymes and fresh meat oxidation (p \u3e 0.05). However, the n-3 LC-PUFA deposition slightly increased lipid oxidation in cooked and stored (4 °C) meat (p \u3c 0.05). In conclusion, MA supplementation improves the nutritional quality of hen meat in terms of lipid profile without compromising meat quality attributes. Appropriate antioxidants are required to mitigate oxidation when such DHA-enriched meat is subjected to cooking and storage

Food Frontiers : An academically sponsored new journal

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Meat and meat alternatives: where is the gap in scientific knowledge and technology?

The unprecedented surge of developing meat analogues and other alternative protein products in the past few years has occurred amidst numerous technological challenges. The creation of fibril structure and flavour from non-muscle proteinaceous sources to mimic fresh and processed meat requires a clear understanding of the fundamental differences between muscle and alternative proteins. Currently, plant-based meat alternatives are dominating the alternative market; mycoprotein-based products have also gained a market share, while algae and insects are other emerging sources of alternative proteins. Both traditional and novel processing technologies and innovative ingredient formulations are being developed to transform nonmuscle proteins into fibrous or particle structures that microscopically resemble muscle. However, the production of meat analogues generally entails ultra-processing and ultra-formulation, which could compromise nutritional value and safety. Therefore, to sustain the alternative protein market, scientists and entrepreneurs must methodically examine and understand inherent differences that separate alternative proteins from muscle proteins. An intuitive knowledge base is essential to designing new approaches to overcome technical challenges. In doing so, food scientists and entrepreneurs must be keenly cognisant that animal meat products are unique; the quality and sensorial attributes of meat can only be simulated but not replicated