Cloning of the 52-kDa chitinase gene from Serratia marcescens KCTC2172 and its proteolytic cleavage into an active 35-kDa enzyme.

@article{Gal1998CloningOT,
  title={Cloning of the 52-kDa chitinase gene from Serratia marcescens KCTC2172 and its proteolytic cleavage into an active 35-kDa enzyme.},
  author={Sang Wan Gal and J Y Choi and Chang Yub Kim and Yong Hwa Cheong and Young Jun Choi and Si Young Lee and Jeong Dong Bahk and Moo Je Cho},
  journal={FEMS microbiology letters},
  year={1998},
  volume={160 1},
  pages={151-8}
}
A chitinase gene (pCHI52) encoding the 52-kDa chitinase was isolated from a Serratia marcescens KCTC2172 cosmid library. This chitinase gene consists of 2526 bp with an open reading frame that encodes 485 amino acids. Escherichia coli harboring the pCHI52 gene secreted not only a 52-kDa but also a 35-kDa chitinase into the culture supernatant. We purified both 52-kDa and 35-kDa chitinases using a chitin affinity column and Sephacryl-S-300 gel filtration chromatography. We determined that the 17… CONTINUE READING
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