Hydrolization Of Salvianolic Acid B By Enzyme

In this paper, the enzyme which could hydrolyze Salvianolic acid B was isolated, purified and characterized. The reaction conditions of producing enzymatic hydrolysate were optimized. And enzymatic hydrolysate was separated by macroporous resin.In order to purify crude Salvianolic acid B which content was10%, SP207macroporous resin was eluted by60%ethanol for four times bed volume. After that the purity of Salvianolic acid B reached to78%.The Absidia sp.D38s strain was incubated with malt extract and40%salvia miltiorrhiza extract for96h to produce enzyme which had the Salvianolic acid B-hydrolyase activity.The enzyme was purified by DEAE-cellulose DE52column. SDS-polyacrylamide gel electrophoresis was used to estimate the molecular weight of Salvianolic acid B-hydrolyase from Absidia sp.D38s strain, and the purified enzyme was almost one band on SDS-polyacrylamide gel electrophoresis, which molecular weight was about65kDa.The properties of the Salvianolic acid B-hydrolyase were studied. The enzyme optimal substrate concentration was1.6%, pH was5.0, temperature was35℃, and the optimal reaction time was14h.The Salvianolic acid B-hydrolysates mainly contain danshensu and hydrolysate Ⅱ.6g Salvianolic acid B hydrolysates were purified by Sepabeads SP207macroporous resin,1.05g danshensu monomer which eluted by water and2.46g hydrolysate Ⅱ which eluted by ethanol were obtained. Their yields were17.6%and41.0%, purity were99%and91%in the HPLC method respectively. The structure, property, pharmacology functions of Hydrolysate Ⅱ needs further investigated.