Study on isolation,purification and characterization of porcine amylopsin
MIN Yu-tao1,SONG Yan-xian1,XU Feng-cai2,MA Qing-yi2(1.Zhongzhou University,Zhengzhou 450044,China;2.Zhengzhou University of Light Industry,Zhengzhou 450002,China)
The amylopin was extracted from porcine pancreas,partially purified and characterized by using a combination of precipitation with isopropanol,solving-precipitating with ammonium sulfate,dialysis and reverse osmosis. The results showed that the specific activity of amylopin from porcine pancreas was 856U/mg protein,almost 6 times as that of crude enzyme(146U/mg). The amylopin can be a substitution of commercially available enzyme and used in our experiments. The optimum temperature and pH value were 37℃ and 6.9 respectively.
【CateGory Index】： TS201.25