Purification and Some Characteristics of β-N-Acetylhlucosaminidase Produced by Vibro sp.

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β-N-Acetylglucosaminidase produced by a Vibrio sp. isolated from soil was purified by ammonium sulfate precipitation, gel filtration on Sephadex G-25 and DEAE-cellulose chromatography. β-N-Acetylglucosaminidase was sepaated from chitinase by these prtocedures, purified to an electrophoretically homogeneous state, and the enzymatic properties of the purified enzyme were examined. The molecular weight of the enzyme measured, by SDS gel electrophoresis was approximately 92,000. The optimum pH and temperature were 6.5 and 50℃, respectively. The enzyme was stable between pH 6.0-7.5 at 40℃ and tolerant to temperatures up to 40℃, but inactivated at 50℃ and more. The enzyme hydrolyzed the chitooligosaccharides such as chitobiose, chitotriose and chitotetraose to N-acetylglucosamine, the monomer of these oligosaccharides. In the course of degradation, oligosaccharides with higher degress of polymerization than that of the substrate appeared during paper chromatography, suggesting that this enzyme has transglycosylation activity.
公益社団法人日本生物工学会の論文
1993-11-25