Measurement of antioxidant activity

Purification and identification of novel antioxidant peptides from enzymatic hydrolysates of sardinelle (Sardinella aurita) by-products proteins.

Novel protein sources (like insects, algae, duckweed, and rapeseed) are expected to enter the European feed and food market as replacers for animal-derived proteins. However, food safety aspects of these novel protein sources are not well-known. The aim of this article is to review the state of the art on the safety of major novel protein sources for feed and food production, in particular insects, algae (microalgae and seaweed), duckweed, and rapeseed. Potential hazards for these protein sources are described and EU legislative requirements as regard to food and feed safety are explained. Potential hazards may include a range of contaminants, like heavy metals, mycotoxins, pesticide residues, as well as pathogens. Some safety aspects of novel protein sources are intrinsic to the product, but many potential hazards can also be due to production methods and processing conditions. These aspects should be considered in advance during product development. European law is unclear on several issues regarding the use of novel protein sources in food and feed products. For food product applications, the most important question for food producers is whether or not the product is considered a novel food. One of the major unclarities for feed applications is whether or not products with insects are considered animal-derived products or not. Due to the unclarities in European law, it is not always clear which Regulation and maximum levels for contaminants apply. For market introduction, European legislation should be adjusted and clarified.

https://onlinelibrary.wiley.com/doi/pdf/10.1111/1541-4337.12032

Safety of Novel Protein Sources (Insects, Microalgae, Seaweed, Duckweed, and Rapeseed) and Legislative Aspects for Their Application in Food and Feed Production

Antioxidant activity and functional properties of porcine plasma protein hydrolysate as influenced by the degree of hydrolysis

Autoxidation in food and biological systems is responsible for a multitude of adverse effects and implications in human health as well as in food stability and preservation. Antioxidants play a major role in preventing or delaying autoxidation and have attracted much attention as food stabilizers, dietary supplements and natural health products. Both synthetic and natural antioxidants are widely used in food products and an ever increasing number of research papers have appeared in the recent literature on the discovery and application of natural antioxidants and their therapeutic use in inhibiting a myriad of diseases. However, some common synthetic antioxidants have also become controversial due to their potential adverse effects on health. This overview provides the latest developments about novel antioxidants, particularly phenolic derivatives, peptides/protein hydrolysates, phospholipids and polysaccharides, and their role in food quality preservation and human health promotion.

Novel antioxidants in food quality preservation and health promotion.

Antioxidant activity and water-holding capacity of canola protein hydrolysates

Topologically, platelet factor-4 kinocidins consist of distinct N-terminal extended, C-terminal helical, and interposing gamma-core structural domains. The C-terminal alpha-helices autonomously confer direct microbicidal activity, and the synthetic antimicrobial peptide RP-1 is modeled upon these domains. In this study, the structure of RP-1 was assessed using several complementary techniques. The high-resolution structure of RP-1 was determined by NMR in anionic sodium dodecyl sulfate (SDS) and zwitterionic dodecylphosphocholine (DPC) micelles, which approximate prokaryotic and eukaryotic membranes, respectively. NMR data indicate the peptide assumes an amphipathic alpha-helical backbone conformation in both micelle environments. However, small differences were observed in the side-chain orientations of lysine, tyrosine, and phenylalanine residues in SDS versus DPC environments. NMR experiments with a paramagnetic probe indicated differences in positioning of the peptide within the two micelle types. Molecular dynamics (MD) simulations of the peptide in both micelle types were also performed to add insight into the peptide/micelle interactions and to assess the validity of this technique to predict the structure of peptides in complex with micelles. MD independently predicted RP-1 to interact only peripherally with the DPC micelle, leaving its spherical shape intact. In contrast, RP-1 entered deeply into and significantly distorted the SDS micelle. Overall, the experimental and MD results support a preferential specificity of RP-1 for anionic membranes over zwitterionic membranes. This specificity likely derives from differences in RP-1 interaction with distinct lipid systems, including subtle differences in side chain orientations, rather than gross changes in RP-1 structure in the two lipid environments.

https://onlinelibrary.wiley.com/doi/pdf/10.1002/bip.21071

Nichole Cumby

Papers

Antioxidant activity and water-holding capacity of canola protein hydrolysates

Antimicrobial peptide RP-1 structure and interactions with anionic versus zwitterionic micelles.