Purification and Properties of the Endo-1,4-β-Glucanase III from Ruminococcus albus
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概要
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Endoglucanase III (EGIII) was purified from Ruminococcus albus culture supernatant. An enzyme having a molecular weight of 53,000 was stabilized by mercaptoethanol and inhibited by sulfhydryl group-blocking reagents, and exhibited its highest CMC-degrading activity at pH 5.7 and 55℃. The enzyme hydrolyzed cellobiose (G2) and cellotriose (G3) only negligibly, but significantly hydrolyzed cellotetraose (G4), cellopentaose (G5) and cellohexaose (G6). The major hydrolysis reactions conducted by the enzyme were G4→2G2,G5→G2+G3,G6→G2+G4 and G6→2G3. The V_<max> values of these reactions increased remarkably while the K_m values decreased significantly with an increase in degree of polymerization of the substrate.
- 社団法人日本生物工学会の論文
- 1992-01-25
著者
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Ohmiya Kunio
Faculty Of Bioresources Mie University
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Shimizu Shoichi
Laboraotory Of Bioreaction Engineering Department Of Food Science And Technology Faculty Of Agricult
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Shimizu S
Professor Emeritus Nagoya University
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Shiimizu Susumu
Department Of Food Science And Technology Faculty Of Agriculture Nagoya University
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Matsuda T
Department Of Applied Molecular Biosciences School Of Bioagricultural Sciences Nagoya University
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Matsuda T
Department Of Applied Molecular Biosciences Graduate School Of Bioagricultural Sciences Nagoya Unive
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Matsuda Tsukasa
School Of Agriculture Nagoya University
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WATANABE YUICHI
Niigata Research Laboratories, Mitsubishi Gas Chemical Company Inc.
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MORIYAMA RYOUICHI
School of Agriculture, Nagoya University
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SHIMIZU SHOICHI
Professor Emeritus, Nagoya University
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Matsuda Tsukasa
Department Of Applied Biological Sciences School Of Agricultural Sciences Nagoya University
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Shimizu Shoichi
Daiichi Pharmaceutical Co. Ltd.
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WATANABE Yuichi
Laboratory of Bioreaction Engineering, School of Agriculture, Nagoya University
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Moriyama Ryouichi
School Of Agriculture Nagoya University
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Watanabe Yuichi
Laboratory Of Bioreaction Engineering School Of Agriculture Nagoya University
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