Single Step Purification of Novel Thermostable and Chelator Resistant Amylase from BacillusLicheniformis RM44 by Affinity Chromatography.

ABSTRACT: Bacillus licheniformis RM44 was isolated from hot spring near Karachi and screened for the production of extracellular amylase Amy RM44. Amy RM44 was purified to homogeneity on a single step by affinity chromatography using insoluble corn starch. The molecular weight of Amy RM44 was estimated to be 66 kDa by SDS-PAGE and zymographic analysis. Nine fold purification was achieved with the specific activity of 870 U/mg that provides the total yield of the enzyme up to 31%. Studies on purified AmyRM44 characterization revealed that the optimum temperature of enzyme was 100 ºC. Amy RM44 was proved to be highly thermostable as it retained 50% activity after 2 h at 100 ºC. Amy RM44 was stable over wide range of pH with optimum activity at pH 5. Enzyme activity was not significantly inhibited by S

SUBMITTER: Siddiqui A 

PROVIDER: S-EPMC5610767 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature