Purification and Characterization of an Endo-cellulase from Acremonium cellulolyticus.
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- Kansarn Supannee
- The Graduate School of Electronic Science and Technology, Shizuoka University
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- Matsushita Naoyoshi
- Department of Biology, Faculty of Education, 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起源のエンドセルラーゼの精製と基本性質
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Abstract
An endo-cellulase from a commercial cellulase preparation of a filamentous fungus Acremonium cellulolyticus was separated and extensively purified to essential homogeneity by using consecutive column chromatographies of QAE-Toyopearl 550C, DEAE-Toyopearl 650S, Butyl-Toyopearl 650M and Bio-Gel P-100, and was designated as cellulase IV The purified enzyme was homoge-neous on both Native- and SDS-PAGE, and was completely free from β-glucosidase. The enzyme showed high specific activity for CMC and an extremely low specific activity for Avicel (a mi-crocrystalline cellulose powder), 106 and 0.08 U/mg of protein, respectively. The molecular mass of the enzyme was estimated to be about 38 kDa by SDS-PAGE. The enzyme was an acidic protein with a pI value of≤3.4. The N-terminal amino acid sequence from the 2nd up to the 27th residue of the purified cellulase was Gln-Ala-Ser-(Cys)-Phe-Glu-Trp-Phe-Gly-Ser-Asn-Glu-Ser-Gly-Ala-Glu-Phe-Gly-Ser-Gly-Asn-Ile-Pro-Gly-Val-Glu-. The optimum pH and temperature were 4.0 and 60-C, respectively. The enzyme was completely stable over the range of pH 5.0-12.0 at 4-C for 24 h and at temperatures below 50-C. Cellulase IV was characterized as a medium endo -type cellulase on the basis of its action on CMC and cellooligosaccharides. The enzyme was completely inhibited by 5 mM Hg2+, Fe3+ and KMnO4. Cellulase IV split various cellulosic substrates to pro-duce 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 (2), 177-185, 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
- 1390282681269120768
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- NII Article ID
- 10008251762
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- NII Book ID
- AN10453916
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- ISSN
- 18807291
- 13447882
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- NDL BIB ID
- 5436037
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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