Purification and Properties of Two Endo-cellulases from Acremonium cellulolyticus.
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- Kansarn Supannee
- The Graduate School of Electronic Science and Technology, Shizuoka University
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- Nihira Takanori
- The Graduate School of Electronic Science and Technology, Shizuoka University
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- Hashimoto Emiko
- Department of Biology, Faculty of Education, Shizuoka University
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- Suzuki Masayuki
- The Graduate School of Electronic Science and Technology, Shizuoka University
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- Kono Toshiaki
- Bio Science Laboratories, Meiji Seika Kaisha, Ltd.
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- Okada Gentaro
- The Graduate School of Electronic Science and Technology, Shizuoka University Department of Biology, Faculty of Education, Shizuoka University
Bibliographic Information
- Other Title
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- 糸状菌Acremonium cellulolyticus起源の2種エンドセルラーゼの精製と基本性質
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Abstract
Two distinct endo-cellulase components derived from Acremonium cellulase, a commercial cellulase preparation from Acremonium cellulolyticus, were extensively purified by consecutive column chromatography and designated as cellulase III-A and cellulase III-B. Cellulases III-A and III-B were each homogeneous on both Native- and SDS-PAGE, and were completely free from β-glucosidase. The molecular mass (SDS-PAGE) and pI Tvalues of cellulases IIIV-A and III-B were 58 kDa and 4.6, and 49 kDa and 4.2, respectively. Both enzymes contained 14-16% carbohydrates (as glucose). The N-terminal amino acid sequences from the 2nd up to the 20th residue of bothenzymes were determined by Edman degradation. Some enzymatic properties of the purified cellulases were investigated. The optimum pH and temperature for cellulases III-A and III-B were pH 5.5 and 55°C, and pH 5.5 and 65°C, respectively. Cellulases III-A and III-B were completely stable over the range of pH 4.2-8.0 at 4°C for 24 h and at temperatures below 55°C, and pH 3.3-7.8 and below 60°C, respectively. Cellulases III-A and III-B retained 25 and 88% of the original CMC-saccharification activities, respectively, after heating at 70°C for 10 min. The hydrolysis of CMC by cellulase III-B was more endo-lytic than that by cellulase III-A. Both enzymes splitvarious soluble and insoluble substrates to produce predominant cellobiose and a small amount of glucose as the final hydrolysis products.
Journal
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- Journal of Applied Glycoscience
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Journal of Applied Glycoscience 47 (3/4), 293-302, 2000
The Japanese Society of Applied Glycoscience
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Details 詳細情報について
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- CRID
- 1390282681269272448
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- NII Article ID
- 10008252079
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- NII Book ID
- AN10453916
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- ISSN
- 18807291
- 13447882
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- NDL BIB ID
- 5521380
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed