Properties and Transglycosylation Reaction of a Chitinase from Nocardia orientalis(Biological Chemistry)
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概要
- 論文の詳細を見る
The hydrolytic products of a chitinase purified from Nocardia orientalis were examined on reduced (GlcNAc)_n(n=2〜6). The rate of hydrolysis on reduced (GlcNAc)_<4〜6> increased with increasing chain-length of N-acetylglucosamine residues, but the enzyme did not act on reduced (GlcNAc)_2 or reduced (GIcNAc)_3. Based on the analysis of the frequency distribution of bond cleavage on PNP-(GlcNAc)_n(n=2〜5) in the initial hydrolysis, the enzyme was shown to release predominantly (GlcNAc)_2 from the nonreducing end of each substrate. The enzyme, which is essentially a hydrolase, also catalyzed a transglycosylation reaction in an excess of (GlcNAc)_4 as an initial substrate. In this case, the addition of ammonium sulfate to the reaction system resulted in a significant increase in (GlcNAc)_6 production. The yield of the hexasaccharide was about 34% of the chitinase-catalyzed net decrease of (GlcNAc)_4. The rate of the transglycosylation in the presence of ammonium sulfate greatly depended on the salt concentration, the temperature, and the substrate concentration.
- 社団法人日本農芸化学会の論文
- 1989-08-23
著者
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ISOBE Kiyoshi
Department of Material Science, Graduate School of Science, Osaka City University
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Isobe Kiyoshi
静岡赤十字病院
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Isobe Kiyoshi
Department Of Surgery Shizuoka Red Cross Hospital
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Nanjo Fumio
Nfi Laboratories Yaizu Suisan Kagaku Industry Co. Ltd.
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Usui Taichi
Department Of Agricultural Chemistry Faculty Of Agriculture Shizuoka University
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Isobe Kiyoshi
Department Of Agricultural Chemistry Faculty Of Agriculture Shizuoka University
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SAKAI Kazuo
NFI Laboratories, Yaizu Suisan Kagaku Industry Co., Ltd.
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ISHIKAWA Masato
NFI Laboratories, Yaizu Suisan Kagaku Industry Co., Ltd.
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Ishikawa Masato
Nfi Laboratories Yaizu Suisan Kagaku Industry Co. Ltd.
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Sakai Kazuo
Nfi Laboratories Yaizu Suisan Kagaku Industry Co. Ltd.
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