Isolation, purification and bioactivity of ACE inhibitory peptides from peach kernel protein enzymatic hydrolysate

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 (IC 50 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 kernelderived peptides as an ingredient in functional food to control hypertension.

Isolation and identification of angiotensin‐converting enzyme inhibitory peptides from Tartary buckwheat albumin

“…showed that more hydrophobic peptides had superior ACE inhibition 34 . The reason is that the hydrophobic peptides are more likely to be coordinated at the active center of ACE and bound to zinc ions 35 . Thus, with the help of the peptide property calculator, the hydrophobicity mean was computed, and 42 peptides with hydrophobicity means larger than 0.5 were found within these 84 peptides.…”

“…34 The reason is that the hydrophobic peptides are more likely to be coordinated at the active center of ACE and bound to zinc ions. 35 Thus, with the help of the peptide property calculator, the hydrophobicity mean was computed, and 42 peptides with hydrophobicity means larger than 0.5 were found within these 84 peptides. Chen et al identified the peptide GVVPHN with a hydrophobic amino acid ratio of 0.5 from defatted walnut protein and supported that the higher hydrophobic peptides were more active in ACE inhibition.…”

Plant Protein-Derived Active Peptides: A Comprehensive Review

“…65 Wang et al hydrolyzed peach kernel globulin with Alcalase and identified a peptide with ACE inhibitory activity in vitro, whose IC 50 value was 0.78 mg/mL. 66 The peptide FETISFK with ACE inhibitory activity (IC 50 = 2.12 ± 0.067 μg/mL) in vitro and in vivo was identified from cashew Alcalase hydrolysates, whose ACE inhibition rate was up to 91.04 ± 0.31%, and which could attenuate liver damage by downregulating the ACE-AngII-AT1R axis in the renin-angiotensin system. 67 Gu et al identified two peptides, WH and WS with α-glucosidase inhibitory activity in vitro, from almond protein Prote Ax and Protease M hydrolysates, both of which were relatively stable under simulated digestion conditions.…”

“…Liu et al identified three peptides, YLLK, YLVPH, and YRLD with ACE inhibitory activity in vitro, from pine nut protein Alcalase hydrolysates, however, in combination with the whole gastrointestinal tract simulation environment, the YLLK was suitable for use as an ACE inhibitory peptide while the YLVPH and YRLD were not suitable . Wang et al hydrolyzed peach kernel globulin with Alcalase and identified a peptide with ACE inhibitory activity in vitro, whose IC 50 value was 0.78 mg/mL . The peptide FETISFK with ACE inhibitory activity (IC 50 = 2.12 ± 0.067 μg/mL) in vitro and in vivo was identified from cashew Alcalase hydrolysates, whose ACE inhibition rate was up to 91.04 ± 0.31%, and which could attenuate liver damage by downregulating the ACE-AngII-AT1R axis in the renin-angiotensin system .…”