Purification and Characterization of One Alkaline Protease from Actinomucor elegans AS3.2778
10.3969/j.issn.1671-8135.2008.09.018
- VernacularTitle:雅致放射毛霉AS3.2778碱性蛋白酶的纯化及性质研究
- Author:
Jin-Quan PAN
1
;
Xiao-Chun LUO
;
Ming-Quan XIE
Author Information
1. 华南理工大学
- Keywords:
Actinomucor elegans Protease Purification Characterization
- From:
China Biotechnology
2008;28(9):111-118
- CountryChina
- Language:Chinese
-
Abstract:
One alkaline protease from Actinomucor elegans AS3.2778 was purified protein. The enzyme was purified using ammonium sulfate precipitation, ion exchange chromatography, hydrophobic chromatography and size exclusion chromatography method, and its properties were also investigated. The molecular weight of this enzyme is 32 kDa with SDS-PAGE method, optimum temperature is 60℃, optimum pH is 8.5 to 10.5, it is stable in the pH range of 6.0 to 9.0 at < 40℃ temperature, and being completely inhibited by the serine protease inhibitor, PMSF, indicated that it belongs to the serine protease family. Specificity test indicated this protease has extensive selectivity to peptide bones, especially to peptide bones composed of Leucine residue.
