Purification and Some Properties of β-1,3-Glucanase from Streptomyces sp.(Biological Chemistry)

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概要

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• β-1,3-Glucanase was purified from the culture filtrate of a Streptomyces sp. by ammonium sulfate fractionation, hydroxylapatite and DE-52 column chromatographies, gel filtration on Biogel P-100 and isoelectric focusing. The purified β-1,3-glucanase was homogeneous on polyacrylamide disc-gel electrophoresis. The isoelectric point was pH 3.7, and the molecular weight was 36,000. The optimum pH and temperature for the activity of the enzyme were 5.5 and 55℃, respectively. The enzyme was stabilized by Ca^<2+>, but inactivated by Hg^<2+>, and was inhibited by N-bromo-succinimide. The glucanase did not hydrolyze laminaribiose or sophorose, cellobiose, or gentiobiose. The enzyme ultimately hydrolyzed laminari-oligosaccharides (laminaritriose to laminarihexaose) to glucose and laminaribiose, and their sugar alcohols (laminaritriitol to laminarihexaitol) mainly to laminaribiose and laminaribiitol via a disproportionation reaction.

• 社団法人日本農芸化学会の論文
• 1986-05-23

著者

• Kusakabe Isao

  Institute of Applied Biochemistry, University of Tsukuba

• Murakami Kazuo

  Institute of Applied Biochemistry, University of Tsukuba

• KUSAMA Satoru

  Institute of Applied Biochemistry, University of Tsukuba

• Kusakabe I

  Univ. Tsukuba Tsukuba Jpn

• Kusakabe Isao

  Institute Of Applied Biochemistry University Of Tsukuba

• Kusama Satoru

  Institute Of Applied Biochemistry University Of Tsukuba

• Murakami K

  Tokai University School Of Medicine

• Murakami Kazuo

  Institute Of Applied Biochemistry University Of Tsukuba

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