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Purification and characterization of a chitinase from Cytophaga sp. HJ isolated from sea sand

Title
Purification and characterization of a chitinase from Cytophaga sp. HJ isolated from sea sand
Authors
Lee D.Noh H.-J.Lee K.M.
Ewha Authors
이강만
SCOPUS Author ID
이강만scopus
Issue Date
1999
Journal Title
Journal of Microbiology and Biotechnology
ISSN
1017-7825JCR Link
Citation
vol. 9, no. 6, pp. 839 - 846
Indexed
SCIE; SCOPUS; KCI WOS scopus
Abstract
An extracellular chitinase-producing bacterial strata induced by colloidal chitin was isolated from sea sand and was identified to be a member of the genus Cytophaga. The chitinase was purified successively by 30-60% ammonium sulfate fractionation, and DEAE-BIO gel A column, Octyl-Sepharose CL-4B column, and DEAE-Bio gel A column chromatographies. The enzyme had a molecular mass of 59.75 kDa, and the amino terminal amino acid sequence was ATPNAPVISW MPTDXXLQNXS. The enzyme acted better on colloidal chitin as a substrate than on chitosan. For colloidal chitin and chitosan (Degree of Acetylation, 15-25%), K(cat) values were 0.60 U/mg and 0.08 U/mg, respectively. HPLC analysis of the enzymatic reaction products showed that the chitinase produced mostly N-acetyl-D-glucosamine and di-N- acetylchitobiose. The optimum temperature and pH for the enzyme were 50°C and 4.0, respectively. N-Bromosuccinimide and Hg2+ inhibited the chitinase activity as much as 90%, and Sb3+, diethylpyrocarbonate, and Ag+ inhibited it by 5070%.
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약학대학 > 약학과 > Journal papers
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