학술논문

Isolation, purification and bioactivity of ACE inhibitory peptides from peach kernel protein enzymatic hydrolysate
Document Type
article
Source
Food Science and Technology. January 2022 42
Subject
peach kernel protein enzymatic hydrolysate
ACE inhibitory peptides
isolation and purification
bioactivity
Language
English
ISSN
0101-2061
Abstract
Peaches mainly produced in China are a source of food-derived proteins, but much of it is wasted. To make full use of the peaches and peaches related resources, we extracted proteins, including albumin, globulin, gliadin, and glutelin, from defatted Tibet wild peach kernels using Osborne method to study their angiotensin I-converting enzyme (ACE) inhibiting activity, which is an active ingredient for hypertension treatment. The different enzymatic products of these extracts were further separated by ultrafiltration membranes and reversed phase high-performance liquid chromatography (RP-HPLC). The component K2 originated from globulin hydrolysate by alcalase treatment showed the highest ACE inhibiting activity (IC50 0.78 mg/mL). Through further analyzing the Mass spectrometry results of K2 and searching the BIOEP database, the specific dipeptide AH (consisted of Ala and His) has been identified as the ACE inhibitory peptide, providing a potential for using Tibet peach kernel-derived peptides as an ingredient in functional food to control hypertension.