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KMID : 0545119990090060839
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Journal of Microbiology and Biotechnology
1999 Volume.9 No. 6 p.839 ~ p.846
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Purification and Characterization of a Chitinace from Cytophaga sp.HJ Isolated from Sea Sand
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Lee, Dong Mi
Noh, Hee Jung/Lee, Kang Man
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Abstract
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An extracellular chitinase-producing bacterial strain 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, OctylSepharose 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 0.60U/㎎ and 0.08U/㎎, 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℃ and 4.0, respectively. N-Bromosuccinimide and Hg^2+ inhibited the chitinase activity as much as 90%, and Sb^3+, diethylpyrocarbonate, and Ag^+ inhibited it by 50-70%.
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