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-methyl-umbelliferyl beta-D-N,N'-diacetylchitobioside [4-MU-(GlcNAc)(2)]. ChiA showed maximum activity at pH 6.0 and its optimum temperature was 45degreesC. ChiA was stable between pH 6.0 and 9.0 and at temperatures up to 40degreesC. The K-m and V-max values of ChiA for 4-MU-(GlcNAc), were estimated to be 6.9 muM and 43 mumol/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.