Premium
Angiotensin‐converting enzyme ( ACE )‐inhibitory activity of boza, a traditional fermented beverage
Author(s) -
Kancabaş Aslı,
Karakaya Sibel
Publication year - 2013
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.5883
Subject(s) - hydrolysate , in vitro , angiotensin converting enzyme , inhibitory postsynaptic potential , enzyme , food science , digestion (alchemy) , renin–angiotensin system , chemistry , biochemistry , fermentation , biology , chromatography , endocrinology , hydrolysis , blood pressure
Background In this study the angiotensin‐converting enzyme ( ACE )‐inhibitory activity of boza and protein fractions of boza separated according to molecular weight was determined. In addition, the effect of in vitro digestion on ACE ‐inhibitory activity was investigated.Results The protein content, ACE ‐inhibitory activity and IC 50 value of boza were 1.0896 ± 0.08%, 76.76 ± 14.93% and 7.2 ± 0.28 µg protein mL −1 respectively. The protein hydrolysate was separated into three fractions according to molecular weight ( MW ), i.e. MW < 5000 Da, 5000 < MW < 10 000 Da and 10 000 < MW < 20 000 Da. The lowest IC 50 value (0.268 ± 0.07 µg protein mL −1 ) was found for the fraction with 5000 < MW < 10 000 Da ( P < 0.05). After in vitro digestion the ACE ‐inhibitory activities of stomach and intestine dialysates were almost the same ( P > 0.05). The IC 50 value of stomach digest was determined as 2.06 ± 0.32 (µg protein mL −1 ). However, the IC 50 value of intestine digest could not be determined, because all dialysates with different protein concentrations displayed ACE ‐inhibitory activity greater than 50%.Conclusion The findings indicate that boza, protein hydrolysate, fractionated hydrolysates and dialysates obtained after in vitro digestion contain bioactive compounds with different ACE ‐inhibitory activities. Based on these results, boza can be considered as a good source of ACE ‐inhibitory peptides.