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Identification of Diol Dehydratase and Its Reactivating Factor of Lactobacillus Collinoides

Author: LiangTian
Tutor: HuangRiBo
School: Guangxi University
Course: Microbiology
Keywords: 1， 3-propanediol diol dehydratase glycerol dehydratase reactivating factor Lactobacillus collinoides
CLC: Q78
Type: Master's thesis
Year: 2007
Downloads: 1
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Abstract


Glycerol dehydratase （EC4.2.1.30） has turned out to be a research hotspot for being the rate-limited enzyme in biosynthesis of 1,3-propanediol, which is a useful material in chemical industry, Diol dehydratase（EC4.2.1.28） and glycerol dehydrates are isofunctional enzymes ,so diol dehydratase was widely attended.The genes encoding diol dehydratase （pduCDE） and its reactivating factor （pduGH） were amplified from genomic DNA of Lactobacillus collinoides by PCR, then cloned in vector pSE380 and pET30a（+） respectively forming recombinant plasmids pSE-pduCDE and pET-pduGH. These genes are expressed by induction of IPTG in E. coli JM109 and E. coli rosseta（DE3） carrying these recombinant plasmids respectively. After SDS-PAGE, three bands were present as pduCDE expression product with molecular masses of 63, 28 and 22kDa, corresponding to the prediction and then pduGH expression product with molecular masses of 64.5 and 14.4kDa, corresponding to the prediction. In the function identification, pduCDE expression product in didn’t performed the activity of dehydratase, which was in the case of the recombinant expression of diol dehydratase genes of Lactobacillus diovorans in E. coli BL21; the high expression of pduGH in E.coli rosseta（DE3） was insoluble inclusion body. By the protein soluble and Refolding, some soluble protein was obtained. In the presence of free adenosylcobalamn, ATP, and Mg2+ (or Mn2+) , the glycerol dehyadrtase from Clostridium pasteurianum , Which had been inactivated to be enzyme-cyanocobalamin complex, was reactivated the reactivating factor PduGH

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