Unveiling differential impact of heat and microwave extraction treatments on the structure, functionality, and digestibility of jack bean proteins extracted under varying extraction pH.

The poor extractability and digestibility of jack beans restrict their application in food systems. Thermal treatment could be a processing tool to disrupt the compact conformation of the plant matrix and inactivate inherent antinutrients. Therefore, this research investigated the impact of conventional heat-aided (HA-) and microwave-aided (MA-) extraction treatments on the structure, functional properties, and digestibility of jack bean protein concentrate (JBPC) under varying extraction pH. The novelty brought by the present study is establishing the thermal treatment/extraction pH combinations for improving techno-functionalities and digestibility of JBPC. Heat (50 °C for 1 h) and sequential microwave power (400 W, 600 W, and 800 W for 5 min) at three extraction pH (9.0, 10.0, and 11.0) were studied. Upon increasing extraction pH, a significant decrease in the protein content, and ß-Sheet structure was observed, in the order of pH 11.0 > 10.0 > 9.0. JBPC extracted using HA treatments displayed the highest contents of surface hydrophobicity (90.02) and sulfhydryl groups. In functional properties, MA-extracted JBPC under 400 W showed significantly improved solubility (93.45 %), emulsifying activity index (45.23 m2/g), and foaming capacity (141.70 %) when compared to other thermal treatments. The degree of hydrolysis result revealed that MA treatment improved the JBPC in vitro digestibility at a low power level of 400 W. These findings suggest that MA extraction treatment can improve the functional and nutritional properties of JBPC regardless of the extraction pH, and thus, expand the potential application in food systems.

Metabolomics approach for the identification of bioactive compounds released from young and mature soybean upon in vitro gastrointestinal digestion and their effect on health-related bioactive properties.

The aim of the present study was to comparatively investigate the relative phytochemical profiles (phenolic content, organic and amino acids, free sugars, and other metabolites using metabolomics approach), and bioactive potentials of young (YS) and mature soybean (MS) upon in vitro simulated gastrointestinal digestion (SGID). Cumulatively, a total of 198 metabolites were identified in MS and YS, 119 metabolites in undigested YS, and a total of 136 metabolites in undigested MS, which further increased to 156 and 152 in YS and MS upon SGID, respectively. Gastric digesta of both YS and MS exhibited higher inhibitory properties towards α-amylase and DPP-IV enzymes than their intestinal digesta. Furthermore, the intestinal digesta of MS showed higher antioxidant and anti-inflammatory activities compared to the YS intestinal digesta. Overall, the results suggested that the gastrointestinal digestion of YS and MS displayed distinctive metabolic profiles together with varied bioactive potentials.

Novel Plant-Protein (Quinoa) Derived Bioactive Peptides with Potential Anti-Hypercholesterolemic Activities: Identification, Characterization and Molecular Docking of Bioactive Peptides.

Hypercholesterolemia remains a serious global public health concern. Previously, synthetic anti-hypercholesterolemic drugs were used for ameliorating this condition; however, long-term usage presented several side-effects. In this regard, natural products as an adjunct therapy has emerged in recent times. This study aimed to produce novel bioactive peptides with anti-hypercholesterolemic activity (cholesterol esterase (CEase) and pancreatic lipase (PL)) from quinoa protein hydrolysates (QPHs) using three enzymatic hydrolysis methods (chymotrypsin, protease and bromelain) at 2-h hydrolysis intervals (2, 4, and 6 h). Chymotrypsin-generated hydrolysates showed higher CEase (IC50: 0.51 mg/mL at 2 h) and PL (IC50: 0.78 mg/mL at 6 h) inhibitory potential in comparison to other derived hydrolysates and intact quinoa proteins. Peptide profiling by LC-MS QTOF and in silico interaction with target enzymes showed that only four derived bioactive peptides from QPHs could bind in the active site of CEase, whereas twelve peptides could bind in the active site of PL. Peptides QHPHGLGALCAAPPST, HVQGHPALPGVPAHW, and ASNLDNPSPEGTVM were identified to be potential CEase inhibitors, and FSAGGLP, QHPHGLGALCAAPPST, KIVLDSDDPLFGGF, MFVPVPH, and HVQGHPALPGVPAHW were identified as potential PL inhibitors on the basis of the maximum number of reactive residues in these bioactive peptides. In conclusion, QPHs can be considered as an alternative therapy for the treatment of hypercholesterolemia.

Plant-derived proteins as a sustainable source of bioactive peptides: recent research updates on emerging production methods, bioactivities, and potential application.

The development of novel protein sources to compensate for the expected future shortage of traditional animal proteins due to their high carbon footprint is a major contemporary challenge in the agri-food industry currently. Therefore, both industry and consumers are placing a greater emphasis on plant proteins as a sustainable source of protein to meet the growing nutritional demand of ever increasing population. In addition to being key alternatives, many plant-based foods have biological properties that make them potentially functional or health-promoting foods, particularly physiologically active peptides and proteins accounting for most of these properties. This review discusses the importance of plant-based protein as a viable and sustainable alternative to animal proteins. The current advances in plant protein isolation and production and characterization of bioactive hydrolysates and peptides from plant proteins are described comprehensively. Furthermore, the recent research on bioactivities and bioavailability of plant protein-derived bioactive peptides is reviewed briefly. The limitations of using bioactive peptides, regulatory criteria, and the possible future applications of plant protein-derived bioactive peptides are highlighted. This review may help understand plant proteins and their bioactive peptides and provide valuable suggestions for future research and applications in the food industry.