Purification and Some Properties of a Microcrystalline Cellulose-hydrolyzing Enzyme (Avicelase II) from Fungal Strain Y-94(Microbiology & Fermentation Industry)
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概要
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A component of the microcrystalline cellulose (Avicel)-hydrolyzing enzyme porduced by a fungal strain, Y-94, tentatively called Avicelase II, was purifie by several kinds of column chromatography followed by chromatofocusing with Polybuffer anion exchanger (PBE 94), Bio-Gel A0.5m gel filtration, electrophoresis on polyacrylamide gel and disc isoelectric focusing (IEF). The molecular weight of the enzyme was setimated to be 68,000 by the SDS-polyacrylamide gel method and 56,000 by Bio-Gel A0.5m gel filtration, and its isoelectric point was found to be around 4.4 by the chromatofocusing and disc IEF methods. The optimum pH and temperature for Avicel hydrolysis were 5.3 and 62℃, respectively. The enzyme was stable between pH 4.1 and 6.0 at 4℃ for 24hf, and up to 61℃ for 10min. Heavy metal ions such as Cu^<2+> and Hg^<2+> strongly inactivated the enzyme. A highly purified enzyme preparation showed hydrolyzing activities towards Avicel, xylan, carboxylmethyl cellulose (CMC) (activity ratio of 100 : 50 : 20, respectively) and acid-swollen cellulose. By the PAS method, staining glycoprotein with shiff's reagent and periodic acid, the enzyme seemd to be a glycoprotein containing some carbohydrate in its structure. Avicelase II tended to show a higher affinity towards cellooligosaccharides of high molecular weight. The enzyme hydrolyzed Avicel and acid-swollen cellulose, and produced trace amounts of cellotriose and significant quanitities of glucose. In addition, the enzyme is able to act on the internal glycosidic bonds of CMC and xylan. Judging from the results, it appears that Avicelase II should be classified as a member of the specific endoglucanases rather than as an exoglucanase.
- 社団法人日本農芸化学会の論文
- 1988-10-23
著者
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Mitsuishi Yasushi
Fermentation Research Institute Agency Of Industrial Science And Technology Ministry Of Internationa
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YAMANOBE Takasi
Fermentation Research Institute, Agency of Industrial Science and Technology, Ministry of Internatio
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YAGISAWA Mitsuo
Fermentation Research Institute, Agency of Industrial Science and Technology, Ministry of Internatio
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Yagisawa Mitsuo
Fermentation Research Institute Agency Of Industrial Science And Technology Ministry Of Internationa
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Yagisawa Mitsuo
Fermentation Research Institute Agency Of Industrial Science & Technology
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Yamanobe Takasi
Fermentation Research Institute Agency Of Industrial Science And Technology Ministry Of Internationa
関連論文
- Purification and Properties of a β-Glucosidase from Fungal Strain Y-94(Microbiology & Fermentation Industry)
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- Some Enzymatic Properties of Endo-1,4-β-glucanase Components from Fungal Strain Y-94(Microbiology & Fermentation Industry)
- Purification and Some Properties of a Microcrystalline Cellulose-hydrolyzing Enzyme (Avicelase II) from Fungal Strain Y-94(Microbiology & Fermentation Industry)
- The Modes of Action of Three Xylanases from Mesophilic Fungus Strain Y-94 on Xylooligosaccharides(Biological Chemistry)
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