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- W4230753322 abstract "Clostridium paraputrificum chitinase A (ChiA) was purified from a recombinant Escherichia coli. ChiA was active toward chitin from crab shells, colloidal chitin, glycol chitin, and 4-methylumbelliferyl β- d - N,N′ -diacetylchitobioside [4-MU-(GlcNAc) 2 ]. ChiA showed maximum activity at pH 6.0 and its optimum temperature was 45°C. ChiA was stable between pH 6.0 and 9.0 and at temperatures up to 40°C. The K m and V max values of ChiA for 4-MU-(GlcNAc) 2 were estimated to be 6.9 μM and 43 μmol/min/mg, respectively. Thin-layer chromatography indicated that ChiA hydrolyzes chitooligosaccharides to mainly chitobiose. ChiA was found to adsorb not only chitinous polymers but also cellulosic polymers." @default.
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- W4230753322 date "2001-01-01" @default.
- W4230753322 modified "2023-09-25" @default.
- W4230753322 title "Characterization of Clostridium paraputrificum Chitinase A from a Recombinant Escherichia coli." @default.
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- W4230753322 doi "https://doi.org/10.1263/jbb.92.466" @default.
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