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摘要
ACE inhibitory activity was investigated for protein hydrolysates derived from protein isolates of three Phaseolus vulgaris varieties, namely, navy bean, black bean and small red bean. Hydrolysis was performed using sequential digestion of Alcalase/Flavourzyme (AF) or Alcalase/papain (AP). Samples of the protein isolates were heated prior to hydrolysis and the results (i.e., degree of hydrolysis (DH), electrophoresis profiles, and ACE inhibitory activities) were compared to unheated samples. For all varieties, significantly higher DH values (P<0.05) were obtained for the AF hydrolysates compared to the AP hydrolysates. Heat treatments improved the DH values of navy bean and small red bean, however, lower values were observed for the heated black bean samples. For all unheated samples, phaseolins were degraded slowly to fragments with an estimated molecular mass around 20-24 kDa which were resistant to further AF or AP digestions. Extensive degradations were observed for heat-treated samples and phaseolins were hydrolyzed into smaller peptides at the initial stage of digestions. AP hydrolysates for all investigated varieties presented higher ACE inhibitory activity than the AF hydrolysates. The highest ACE inhibitory activities were obtained after 100 min of AP digestion for heated samples from navy bean, and 95 min of AP digestion for heated samples from both black and small red beans, which yielded an IC50 of 68 +/- 5 mu g protein/ml, 83 +/- 13 mu g protein/ml and 78 +/- 7 mu g protein/ml, respectively. Stabilities of these hydrolysates were tested by simulated in vitro gastrointestinal digestion followed by ACE inhibition studies, and lower IC50 values were determined for all three hydrolysates.
- 出版日期2012-12
