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Rosemond Godbless Dadzie,Haile Ma,Ernest Ekow Abano,Wenjuan Qu,Shuyun Mao 한국식품과학회 2013 Food Science and Biotechnology Vol.22 No.6
The degree of hydrolysis (DH) and angiotensinI-converting enzyme (ACE)-inhibitory activity of vitalwheat gluten (VWG) hydrolyzed using Alcalase wereinvestigated using Box-Behnken response surfacemethodology (RSM). The mean responses were fitted to asecond order polynomial to obtain regression equations. The enzyme-substrate ratio and the hydrolysis time increasedthe DH significantly (p<0.05). The substrate concentrationwas the only significant linear term leading to an increasein ACE-inhibitory activity. The optimized conditions of asubstrate concentration of 5.04%, an enzyme-substrateratio 5.94%, and a hydrolysis time 30.79 min gave a pointprediction of a 12.74% DH and 82.28% ACE-inhibitoryactivity. Analytical results from confirmatory experimentwere a 12.22%±0.5 DH and a 78.93%±1.07 ACEinhibitoryactivity. The optimized conditions of the studyprovide useful information to the functional food andbeverage industries to enhance the anti-hypertensiveactivities of peptides from VWG.