ACE-Inhibitory and Radical-Scavenging Activity of Peptides Derived from -Lactoglobulin f(19-25). Interactions with As
详细信息    查看全文
文摘
In this work, the angiotensin-converting enzyme (ACE)-inhibitory and radical-scavenging activities ofthe -lactoglobulin (-Lg)-derived peptides WY f(19-20), WYS f(19-21), WYSL f(19-22), WYSLAf(19-23), WYSLAM f(19-24), and WYSLAMA f(19-25) have been determined. The ACE-inhibitoryactivity (IC50) varied from 38.3 to 90.4 M, with the exception of WYS (>500 M). All -Lg-derivedpeptides also exhibited radical-scavenging activity (oxygen radical absorbance capacity (ORAC) valuesranged from 4.45 to 7.67 mol Trolox equivalents/mol of peptide). The presence and position ofamino acids Trp, Tyr, and Met were proposed to be responsible for the antioxidant activity. Theequimolar amino acid mixtures of all the peptides showed ORAC values lower than those of thecorresponding peptides, indicating that the peptidic bond or the structural conformation had a positiveinfluence on this activity. Finally, positive antioxidant effects of WYS, WYSL, and WYLA with ascorbicacid were observed, whereas WY and WYSLAM showed negative effects, both cases for differentmolar ratio mixtures. These results should be taken into account in the development of new foodingredients on the basis of peptides from -Lg.

© 2004-2018 中国地质图书馆版权所有 京ICP备05064691号 京公网安备11010802017129号

地址:北京市海淀区学院路29号 邮编:100083

电话:办公室:(+86 10)66554848;文献借阅、咨询服务、科技查新:66554700