Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
7587066 | Food Chemistry | 2017 | 7 Pages |
Abstract
An aminopeptidase was isolated from the marine Bacillus licheniformis SWJS33 (BLAP) and purified. According to the tandem mass spectrometry, the enzyme displayed 11% amino acid identity with the aminopeptidase from Bacillus (gi|496687392). BLAP exhibited maximum activity at 60 °C and pH 8.0-8.5 and had a molecular mass of 100 kDa. The presence of NaCl enabled 50% improvement of enzyme activity with 10-15% NaCl being the best. The observed inactivation by EDTA and bestatin and activation by Co2+ and Ag+ indicated that the obtained enzyme was a metalloaminopeptidase. Such an aminopeptidase could further improve the hydrolysis degree of soy protein isolate hydrolysates catalyzed by papain, Alcalase 2.4 L or Flavourzyme 500MG from 8.5%, 9.5% or 14.4-18.8%, 18.7% or 20.1%, respectively, while decreasing the bitter intensity score of the SPI hydrolysates catalyzed by Alcalase 2.4 L from 3.6 to 0.4.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Fenfen Lei, Qiangzhong Zhao, Dongxiao Sun-Waterhouse, Mouming Zhao,