Bioactivity of Hydrolysates Obtained from Chicken Egg Ovalbumin Using Artichoke (Cynara scolymus L.) Proteases

被引：12

作者：

Bueno-Gavila, Estefania ^{[1
]}

Abellan, Adela ^{[1
]}

Giron-Rodriguez, Francisco ^{[1
]}

Cayuela, Jose Maria ^{[1
]}

Tejada, Luis ^{[1
]}

机构：

[1] Univ Catolica Murcia UCAM, Dept Human Nutr & Food Technol, Campus Jeronimos, Guadalupe 30107, Spain

来源：

FOODS | 2021年 / 10卷 / 02期

关键词：

angiotensin-I converting enzyme (ACE) inhibitor; antioxidant; artichoke; bioactive peptide; ovalbumin; ENZYME INHIBITORY PEPTIDE; ANGIOTENSIN-CONVERTING ENZYME; WHITE PROTEIN; ANTIOXIDANT PEPTIDES; ANTIMICROBIAL PEPTIDE; FUNCTIONAL-PROPERTIES; VEGETABLE COAGULANT; IDENTIFICATION; PURIFICATION; DIGESTS;

D O I：

10.3390/foods10020246

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

The aim of this work was to obtain chicken egg ovalbumin hydrolysates using aspartic proteinases present in extracts from the artichoke flower (Cynara scolymus L.) and evaluate their antioxidant, antimicrobial, and angiotensin I-converting enzyme (ACE) inhibitory activity in vitro. Hydrolysis time and molecular weight (<3 kDa) had a significant influence on the hypertensive and antioxidant activity of the hydrolysates. The <3 kDa fraction of the 16 h hydrolysate had an ACE inhibitory activity with an IC50 of 64.06 mu g peptides/mL. The fraction <3 kDa of ovalbumin hydrolysate at 2 h of hydrolysis showed a DPPH radical scavenging activity of 30.27 mu M of Trolox equivalents/mg peptides. The fraction <3 kDa of the hydrolysate of 16 h had an ABTS(+) caption activity of 4.30 mM of Trolox equivalents/mg peptides. The fraction <3 kDa of the hydrolysate of 2 h had an iron (II) chelating activity of 32.18 mu g peptides/mL. From the peptide sequences identified in the hydrolysates, we detected four peptides (from the BIOPEP database) that were already in their bioactive form (IAAEVYEHTEGSTTSY, HLFGPPGKKDPV, PIAAEVYEHTEGSTTSY, and YAEERYPIL), and are reported to display antioxidant and ACE inhibitory activity.

引用

页数：16

共 69 条

[51] The use of high hydrostatic pressure to promote the proteolysis and release of bioactive peptides from ovalbumin [J].