The production of bioactive peptides from egg white proteins (EWPs) and their separation are emerging areas with many new applications. The objective of this study was to compare antioxidant activity of three distinct EWP hydrolysates and their peptide fractions prepared by membrane ultrafiltration using membranes with 30, 10 and 1 kDa molecular weight cutoff. The hydrolysates were obtained by thermal and ultrasound pretreated EWPs hydrolyzed with a bacterial protease, Alcalase. It appeared that the pretreatment significantly affected peptide profiles and antioxidant activity of the hydrolysates measured by ABTS, DPPH and FRAP methods. The hydrolysate prepared using alcalase and ultrasound pretreatment at 40 kHz-15 min has shown to be the most effective in scavenging both DPPH and ABTS radicals (28.10±1.38 and 79.44±2.31%, respectively). It has been noticed that this hydrolysate had a nutritionally more adequate peptide profile than the other hydrolysates with a much lower amount of peptides <1 kDa (11.19±0.53%) and the greatest content of the peptide fraction in the molecular weight (MW) range of 1-10 kDa (28.80±0.07%). This peptide fraction has shown the highest DPPH and ABTS antioxidant activity compared to all other fractions having a potential to be used as a functional food ingredient.
The problem of environmental pollution becomes more worrisome day by day, primarily due to the large amounts of wastewater contaminated with various harmful organic compounds, discharged untreated or partially clean into the environment. Feasibility of use of horseradish peroxidase (Amoracia rusticana) in the synthetic dyes decolorization was approved by many researchers. Among a number of supports used for the immobilization, it was found that natural clay, kaolin, has excellent features which are a precondition for obtaining biocatalysts with the excellent performances. For this reason, a horseradish peroxidase was immobilized onto kaolin using glutaraldehyde as a cross-linking agent. Obtained biocatalyst was applied in the decolorization of anthraquinone dye C.I. acid violet 109. Under determined optimal conditions (pH 4.0, hydrogen peroxide concentration 0.6 mM, dye concentration 30 mg L-1 , temperature 24 °C) around 76% of dye decolorization was achieved. Reusability study showed that resulting biocatalyst was possible to apply four times in the desired reaction with relatively high decolorization percentage.
Soy protein concentrate (SPC) was hydrolyzed using several commercial food-grade proteases (Alcalase, Neutrase, papain, Everlase, Umamizyme, Flavourzyme) and their combination to obtain promising ingredients in the manufacture of functional bakery products. In all cases, the hydrolysis caused nutritional, sensory, and rheological changes in SPC, as well as protein structural changes like increased surface hydrophobicity and content of exposed SH groups with the magnitude of these changes depending on enzyme specificity. The hydrolysis with the combination of Neutrase and Flavourzyme (NeuFlav) increased essential amino acid content by 9.8% and that of Lys by 32.6% compared to SPC. This hydrolysate showed also significant antioxidant activities including ABTS and superoxide anion scavenging activity and metal-chelating ability. The addition of all hydrolysates in wheat flour decreased water adsorption and increased development time to some extent due to gluten network weakening, but also decreased the rate of starch retrogradation, contributing to the increase of the shelf-life of bakery products. The NeuFlav tasted less bitter than other hydrolysates, while E-nose provided a discrimination index of 93 between control and hydrolysates. It appeared that the addition of the NeuFlav hydrolysate in a cookie formulation improved protein content and nutritional quality and directed to its higher general consumer acceptability than cookies formulated with only wheat flour.
In this study, we assessed the effects of microwave irradiation of wheat gluten proteins as a pretreatment performed in a microwave reactor that could accurately control process parameters as a function of power and temperature, as well as comparing it with conventional heat treatment. The aim was to identify suitable combinations of partial enzymatic hydrolysis and microwave pretreatment parameters to produce gluten hydrolysates with reduced allergenicity and conserved techno-functional features for food application. FTIR analysis, and total and reactive SH group contents confirmed that the microwave-controlled heating can significantly change the secondary structure and conformation of gluten protein. The microwave treatment had the largest effect at 200 W and 100 °C, at which the content of gluten has been reduced by about 2.5-fold. The microwave pretreatment also accelerated the enzymatic hydrolysis of gluten, changing the kinetic profile. The apparent hydrolysis rate constants (k2) were 1.00, 3.68, 3.48, 4.64 and 4.17 min−1 for untreated gluten, and those pretreated with microwave power of 200, 400, 600 and 800 W, respectively. Compared to the heat treatment, it appeared that microwave specific non-thermal effects had a significant influence on the gluten structure and allergenicity and, in combination with the enzymatic hydrolysis, ultimately yielded protein hydrolysates with enhanced antioxidant and functional properties.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.