Effect of Different Proteases on the Degree of Hydrolysis and Angiotensin I-Converting Enzyme-Inhibitory Activity in Goat and Cow Milk

Abstract

Angiotensin I-converting enzyme (ACE) peptides are bioactive peptides that have important value in terms of research and application in the prevention and treatment of hypertension. While widespread literature is concentrated on casein or whey protein for production of ACE-inhibitory peptides, relatively little information is available on selecting the proper proteases to hydrolyze the protein. In this study, skimmed cow and goat milk were hydrolyzed by four commercial proteases, including alkaline protease, trypsin, bromelain, and papain. Angiotensin I-converting enzyme-inhibitory peptides and degree of hydrolysis (DH) of hydrolysates were measured. Moreover, we compared the difference in ACE-inhibitory activity between cow and goat milk. The results indicated that the DH increased with the increase in hydrolysis time. The alkaline protease-treated hydrolysates exhibited the highest DH value and ACE-inhibitory activity. Additionally, the ACE-inhibitory activity of hydrolysates from goat milk was higher than that of cow milk-derived hydrolysates. Therefore, goat milk is a good source to obtain bioactive peptides with ACE-inhibitory activity, as compared with cow milk. A proper enzyme to produce ACE-inhibitory peptides is important for the development of functional milk products and will provide the theoretical basis for industrial production.

Hydrolytic degree and antioxidant activity of purified casein characterised by different haplotypes (αs1‐, β‐ and k‐casein) after enzymatic hydrolysis with pepsin and enzymatic extract from Pleurotus eryngii

“…). These findings were in agreement with what reported by other authors (Salami et al , ; Petrat‐Melin et al , ; Shu et al , ) who detected that the antioxidant activity of casein increased during enzymatic digestion. In particular, both EM‐ and EP‐digested caseins showed antioxidant activity and both trends highlighted a direct relationship between the time of hydrolysis and development of antioxidant activity (Fig.…”

High level expression and biochemical characterization of an alkaline serine protease from Geobacillus stearothermophilus to prepare antihypertensive whey protein hydrolysate

“…Due to excellent nutritional and functional properties, whey protein hydrolysates produced by protease hydrolysis, microbial fermentation, and heat treatment have been widely used in food industry [ 42 ]. ACE inhibitory activity of whey protein hydrolysates has been discovered using various proteases (e.g., trypsin, Alcalase, bromelain, papain, and pepsin) [ 43 ]. In this study, whey protein was hydrolyzed by GsProS8 and commercial proteases (e.g., trypsin, Flavourzyme, Protamex, and Alcalase), GsProS8 hydrolysate contained higher peptide content and ACE inhibitory activity (Fig.…”

Green approach towards hydrolysing wheat gluten using waste ingredients from pineapple processing industries

“…The %DH of a protein varies with the enzyme type, its dosage, pH of the reaction media and reaction time (Kong et al ., 2007). The longer the reaction time, the higher the %DH of the protein until it reaches the optimum value (Shu et al ., 2018). In our study, the higher DH of gluten with crude pineapple core extract, compared to buffer alone is attributed to the presence of an active protease, bromelain.…”