Comparative study on structural, biological and functional activities of hydrolysates from Adzuki bean (Vigna angularis) and mung bean (Vigna radiata) protein concentrates using Alcalase and Flavourzyme.

The physicochemical features of mung bean protein (MBP) and adzuki bean protein (ABP) hydrolysates derived from Alcalase (MBPHA, ABPHA) and Flavourzyme (MBPHF, ABPHF) were assessed using FTIR, hydrophobicity, emulsion activity, zeta potential, and health-promoting activities. The results proved that the choice of peptidase and substrate both have a significant effect on the hydrolysates in different physicochemical, structural and functional properties. Size exclusion-HPLC was used to fractionate the MBP and ABP hydrolysates. The results demonstrated that Alcalase hydrolysates included smaller peptides than Flavourzyme hydrolysates, and the chromatogram patterns of the two peptidases were similar. The peptides with the most potent antioxidant and ACE-inhibitory properties were identified using MALDI-TOF-MS. The fraction (F4) of MBPHA exhibited the highest levels of metal chelating activity. The Flavourzyme hydrolysates fraction (F2) and the ABPHA fraction (F2) showed the highest ABTS radical scavenging activity and ACE-inhibitory activity, respectively. Pro-Pro was identified in peptide sequences with ABTS radical scavenging activity as an active component while Pro-Gln was identified in peptide sequences with ACE-inhibitory activity. As a result, Pro-Pro and Pro-Gln, respectively, are likely-one of the characteristics of antioxidant and ACE-inhibitory peptides from MBP and ABP. Compared to mung bean and adzuki bean protein as substrate, Alcalase and Flavourzyme as peptidases significant impacted the development of distinct functionalities and biological activities.

Fractionation of foam-mat dried rice bean hydrolysates using membrane filtration and solid phase extraction: Peptide- and phenolic-based fractions with bioactive potential.

Flavourzyme was used to hydrolyze the germinated rice bean, and the hydrolysates were separated using membrane ultrafiltration with a molecular weight (MW) cut-off of 3 kDa. The ultrafiltration permeate fraction (UFP), non-fractionated hydrolysate (RH), and ultrafiltration retentate fraction (UFR) were foam-mat dried at two temperatures, 60 and 70 °C. The content of each phenolic composition in dried RH samples decreased with increasing drying temperature particularly gallic acid, p-coumaric acid, vanillin, rutin, and, quercetin dropped by 27, 24, 21, 35 and 33%, however the kind of phenolic compositions identified in dried samples was unaffected by drying temperature. Dried UFR and dried UFP had different chromatograms. When the dried UFP and dried UFR chromatograms were examined, it was discovered that the intensity of the peaks in the dried UFR chromatogram was much lower. The majority of phenolics can pass through ultrafiltration membranes with a molecular weight cut-off of 3 kDa, according to this finding. Individual phenolic compound levels in dried UFP samples were similar to RH, implying that the majority of phenolic components in dried rice bean protein hydrolysate were smaller than 3 kDa. With increasing drying temperature, gallic acid, p-coumaric acid, catechol, epicatechin and naringenin levels in dried UFP samples were decreased. The antioxidant capacity of dried rice bean hydrolysate was discovered to be due to phenolic components (gallic acid, epicatechin, catechol, ferulic acid, and rutin), which were found to be more prevalent than peptide fractions. As a result, rice bean hydrolysates could bring novel health advantages, which could lead to the development of nutraceuticals and food products.

A Review on Health-Promoting, Biological, and Functional Aspects of Bioactive Peptides in Food Applications.

Food-derived bioactive peptides are being used as important functional ingredients for health-promoting foods and nutraceuticals in recent times in order to prevent and manage several diseases thanks to their biological activities. Bioactive peptides are specific protein fractions, which show broad applications in cosmetics, food additives, nutraceuticals, and pharmaceuticals as antimicrobial, antioxidant, antithrombotic, and angiotensin-I-converting enzyme (ACE)-inhibitory ingredients. These peptides can preserve consumer health by retarding chronic diseases owing to modulation or improvement of the physiological functions of human body. They can also affect functional characteristics of different foods such as dairy products, fermented beverages, and plant and marine proteins. This manuscript reviews different aspects of bioactive peptides concerning their biological (antihypertensive, antioxidative, antiobesity, and hypocholesterolemic) and functional (water holding capacity, solubility, emulsifying, and foaming) properties. Moreover, the properties of several bioactive peptides extracted from different foods as potential ingredients to formulate health promoting foods are described. Thus, multifunctional properties of bioactive peptides provide the possibility to formulate or develop novel healthy food products.

Identification and synthesis of multifunctional peptides from wheat germ hydrolysate fractions obtained by proteinase K digestion.

Wheat germ protein hydrolysate (WGPH) was obtained by proteinase K digestion, in order to produce bioactive antioxidant and antihypertensive peptides. Response surface methodology (RSM) was used to optimize hydrolysis conditions (enzyme-to-substrate ratio, time, and temperature) for antioxidant activity of hydrolysates. The crude WGPH produced in this way significantly inhibited angiotensin-I converting enzyme (ACE) in a concentration-dependent manner. It was next fractionated by reversed-phase semi-preparative High Performance Liquid Chromatography (HPLC) into 12 fractions that were examined for antioxidant and antihypertensive activities. Fractions with antioxidant and ACE-inhibitory activities were then submitted to further analysis by nano-LC-ESI-MS-MS. Among the various peptides identified, MDATALHYENQK (IC50 : 293.3 ± 6.5 µg/ml) and SGGSYADELVSTAK (IC50 : 265.5 ± 8.3 µg/ml) displayed antioxidant activity and VALTGDNGHSDHVVHF (IC50 : 189.3 ± 4.05 µg/ml), VDSLLTAAK (IC50 : 159.7 ± 0.33 µg/ml), MDATALHYENQK (IC50 : 303.6 ± 2.47 µg/ml), IGGIGTVPVGR (IC50 : 125.7 ± 2.3 µg/ml) and SGGSYADELVSTAK (IC50 : 128.2 ± 1.17 µg/ml) showed good ACE-inhibitory activity. PRACTICAL APPLICATIONS: Wheat milling industries produce massive amounts of wheat germ as by-product that can be converted into valuable compounds. The present research indicates that proteinase K is useful to hydrolyze wheat germ proteins in a search for bioactive peptides with antioxidant and ACE-inhibitory properties. The identified peptides can be regarded as functional food additives, or nutraceuticals to improve human health.