Purification of ginger protease and study on its enzymatic properties
Worldwidely,plant chymosin development for substitution of calf rennet has always been the hot topic of dairy science.Ginger protease with milk coagulating activity was isolated from ginger root.Their general enzymatic characteristics and dynamic behavior were studied.This study mainly focused on the following aspects:ginger protease was extracted from ginger rhizome and the crude ginger protease was obtained by ultrafiltration.Two fractions A and B with the same molecular weight were separated by weak anionic exchange resin using a linear gradient of 0-0.3M NaCl.These two fractions were similar in enzymic property and affinity for proteolysis of κ-casein,indicating that ginger protease A and B were isozymes.This work provided theory basis for the industrial application of ginger protease and the development of jiangzhinai.
国家科技期刊平台
NSTL
万方数据
维普
