Functional properties and Angiotensin-I converting enzyme inhibitory activity of soy-whey proteins and fractions

Food Research International
Tajudini Akande LassissiMichael Davis

Abstract

Soy proteins when prepared to high purity can confer good functional properties and the whey by-product is a potential source for bioactivity. In this study, we determined the protein, moisture, fiber, solubility, foaming, emulsion properties, as well as Angiotensin-I converting enzyme (ACE-I) inhibitory activity of prepared soy-whey proteins and its fractions. The soy-whey proteins were fractionated into <5, >5, >10, and >50kDa using ultrafiltration. The expanded AACC methods were used to determine protein, moisture, and fiber analyses of the whey and its fractions. Solubility method was conducted to determine the protein solubility profile of the soy-whey and its fractions at varying pHs. Turbidimetric method was used to evaluate emulsifying activity (EA) and emulsion stability (ES). There were significant differences observed in moisture, protein and salt contents between unfractionated, >50kDa and smaller sized fractions. No significant differences were observed with phytic acid and total dietary fiber contents among all samples. The unfractionated whey protein and >50kDa fraction showed better solubility than other fractions. Unfractionated whey protein had the highest foam capacity (42.7mL) while the fraction >5kDa showed...Continue Reading

Citations

Jan 17, 2019·Annual Review of Food Science and Technology·Simon M Loveday
Feb 15, 2018·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Cheng-Mei LiuFang Wang

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