Functional Properties of Protein Isolate from Cowpea (Vigna unguiculata L. Walp.)

Abstract

: Functional properties of protein isolates prepared from 3 cowpea varieties and 2 soybean varieties in each of 2 y were determined. Both cowpea protein isolate (CPI) and soy protein isolate (SPI) showed a u‐shaped curve for solubility with the minimum solubility occurring at pH 4.5. The CPI had lower emulsifying activity than SPI but was similar in stability. Foaming capacity and foaming stability ranged from 58.6 to 60.2 mL and 63.7 to 64.4 min for CPI and from 31.9 to 33.0 mL and 43.4 to 45.0 min for SPI, respectively. Gels were formed at 70 °C for 40 min and 30 min for CPI (12%) and SPI (10%), respectively. The CPI needs modification to enhance functional properties for potential application in food products.

Nutrients and antinutrients in cowpea and horse gram flours in comparison to chickpea flour: Evaluation of their flour functionality

“…Better foaming capacity of chickpea flour implies greater incorporation of air bubbles into the product. Although, a lower value of FC (20.8%) for cowpea flour was reported previously (Akubor, Adamolekun, Oba, Obari, & Abudu, 2003), the observed FC was lower than the 60.2% reported for cowpea protein isolate (Horax, Hettiarachchy, Chen, & Jalaluddin, 2004). This may be due to differences in the proteins and the concentrations employed.…”

Optimisation of extraction conditions and thermal properties of protein from the Andean pseudocereal cañihua (Chenopodium pallidicaule Aellen)

“…In the DSC spectrum, the denaturation temperature (T p ) represents the thermal stability of the protein, and the enthalpy change of the endotherm (Dh) indicates the hydrophilic/hydrophobic characteristics of the protein, which could lead to protein aggregation (Wang et al, 2014). The value obtained is close to the values reported for soya protein and isolated globulin from amaranth (96 and 97°C, respectively) (Mart ınez &Añon, 1996 andHorax et al, 2004). A single peak generally suggests that the protein isolate consisted either of one protein species, or of several species with similar thermostability ( Avila Ruiz et al, 2016).…”

Pulse proteins: Processing, characterization, functional properties and applications in food and feed

“…LGCs of 12% for cow pea protein isolate and 10% for SPI (Horax, Hettiarachchy, Chen, & Jalaluddin, 2004) and 10% for mung bean protein isolate (Coffman & Garcia, 1977) have been reported. As indicated for the other functional properties, differences in reported LGCs of pulse protein could be due to pulse type, variety, conditions used for protein extraction and drying, protein purity and composition of the extracts, as well as storage conditions.…”