Glucoamylase of Caulobacter crescentus CB15: cloning and expression in Escherichia coli and functional identification.

ABSTRACT: The biochemical properties of the maltodextrin-hydrolyzing enzymes of cold-tolerant proteobacterium Caulobacter crescentus CB15 remain to be elucidated, although whose maltodextrin transport systems were well investigated. We cloned the putative glucoamylase of C. crescentus CB15 (CauloGA) gene. The CauloGA gene product that was expressed in E. coli was prone to forming inclusion bodies; however, most of the gene product was expressed in a soluble and active form when it was expressed as a fusion protein with Staphylococcus Protein A. The fusion protein was purified using an IgG Sepharose column and was identified as the active GA. The optimum temperature and pH for the activity of this GA toward maltotriose as a substrate were approximately 40°C and 5.0, respectively, and a differential s

SUBMITTER: Sakaguchi M 

PROVIDER: S-EPMC3917699 | biostudies-literature | 2014 Jan

REPOSITORIES: biostudies-literature