Protein hydrolysates of seed: Antioxidant and antihyperglycaemic potential as ingredient for the management of type-2 diabetes.

New plant proteins with high nutritional quality and biological properties are actively searched worldwide. seed protein isolate was prepared from defatted flour and hydrolyzed using four proteases namely trypsin, pepsin, Alcalase, and thermolysin. Then, antioxidant activity and cellular glucose uptake properties of the hydrolysates were assessed.

Effect of heat treatment on the structure, functional properties and composition of Moringa oleifera seed proteins.

Knowledge on how food processing conditions and protein composition can modulate individual or food matrix protein functionality is crucial for designing new protein ingredients. In this regard, we investigated how heat treatment and protein composition influence physicochemical and functional properties of Moringa oleifera seed protein isolate. Results showed that changes in processing temperature induced modifications in the conformation affecting the hydrophobic core of proteins.

Influence of pH and temperature on the physicochemical and functional properties of Bambara bean protein isolate.

Bambara bean is a rich low-cost protein source and a functional ingredient in the food industry. We investigated the effects of temperature and different pH on the physicochemical and functional properties of Bambara bean protein isolate. Vicilin was the major protein of Bambara bean as revealed by SDS PAGE analysis.

Investigation on antioxidant, angiotensin converting enzyme and dipeptidyl peptidase IV inhibitory activity of Bambara bean protein hydrolysates.

Protein isolate was hydrolysed by Alcalase, thermolysin and trypsin. BBPH produced by Alcalase showed highest angiotensin-converting enzyme (ACE) inhibitory properties (IC: 52 µg/mL). Hydrolysates produced by Alcalase and thermolysin exhibited similar dipeptidyl peptidase-IV (DPP-IV) inhibitory activity (IC: 1.

Production and characterization of cowpea protein hydrolysate with optimum nitrogen solubility by enzymatic hydrolysis using pepsin.

Background: Cowpea is a source of low-cost and good nutritional quality protein for utilization in food formulations in replacement of animal proteins. Therefore it is necessary that cowpea protein exhibits good functionality, particularly protein solubility which affects the other functional properties. The objective of this study was to produce cowpea protein hydrolysate exhibiting optimum solubility by the adequate combination of hydrolysis parameters, namely time, solid/liquid ratio (SLR) and enzyme/substrate ratio (ESR), and to determine its functional properties and molecular characteristics.

Optimising functional properties during preparation of cowpea protein concentrate.

Response surface methodology (RSM) was used for modelisation and optimisation of protein extraction parameters in order to obtain a protein concentrate with high functional properties. A central composite rotatable design of experiments was used to investigate the effects of two factors, namely pH and NaCl concentration, on six responses: water solubility index (WSI), water absorption capacity (WAC), oil holding capacity (OHC), emulsifying activity (EA), emulsifying stability (ES) and foam ability (FA). The results of analysis of variance (ANOVA) and correlation showed that the second-order polynomial model was appropriate to fit experimental data.

Functional properties of acetylated and succinylated cowpea protein concentrate and effect of enzymatic hydrolysis on solubility.

The present study was undertaken to improve functional properties of cowpea protein concentrate by acylation and partial hydrolysis with pepsin. The acylated concentrate showed significant improvement in protein solubility and water solubility index, at neutral pH. In addition, acylation increased fat absorption capacity compared with the untreated concentrate, and the maximum was obtained at 0.