Synergistic Effects of Cellobiose Dehydrogenase, Cellulases, and .BETA.-Glucosidase from Irpex lacteus in the Degradation of Various Types of Cellulose.

• Hai Pham Quy

  Department of Chemistry and Material Engineering, Faculty of Engineering,Shinshu University

• Nozaki Kouichi

  Department of Chemistry and Material Engineering, Faculty of Engineering,Shinshu University

• Amano Yoshihiko

  Department of Chemistry and Material Engineering, Faculty of Engineering,Shinshu University

• Kanda Takahisa

  Department of Chemistry and Material Engineering, Faculty of Engineering,Shinshu University

Bibliographic Information

Other Title

• 結晶化度の異なるセルロースに対するセロビオース脱水素酵素,セルラーゼおよびβ-グルコシダーゼの相乗効果
• Synergistic Effects of Cellobiose Dehydrogenase, Cellulases, and β-Glucosidase from Irpex lacteus in the Degradation of Various Types of Cellulose
• Synergistic Effects of Cellobiose Dehydrogenase Cellulases and ベータ Glucosidase from Irpex lacteus in the Degradation of Various Types of Cellulose
• Synergistic effects of cellulobiose dehydrogenase, cellulases and β-glucosidase from Irpex lacteus in the degradation of various types of cellulose

Abstract

Synergistic effects in the degradation of bacterial cellulose (BC), Avicel and H3PO4-swollen Avicel (HA) by cellobiose dehydrogenase (CDH) and ?A-1, 4-glucanases from Irpex lacteus including exo-cellulase (Ex-1), endo-cellulase (En-1) and ?A-glucosidase were investigated. CDH effectively promoted both the degradation of celluloses by Ex-1 and synergism of Ex-1 and En-1 but moderately the degradation by En-1. Kinetic studies indicated that CDH enhances cellulose degradation by Ex-1 more effectively than ?A-glucosidase does by preventing product inhibition. The enhancement in the cellulose-degrading capability of cellulases by synergistically acting with CDH was significant and independent of the crystallinity of substrate while the synergistic effect of Ex-1 and En-1 by themselves was limited when substrates were at low crystallinity. Despite the large amount of cellobiose consumed by CDH in the presence of electron acceptors, the cellulolytic enzyme system from 1. lacteus effectively degraded different cellulose sources and continued producing sufficient glucose for the cell.

Journal

• Journal of Applied Glycoscience

  Journal of Applied Glycoscience 49 (1), 9-17, 2002

  The Japanese Society of Applied Glycoscience

Details

• CRID: 1390282681267957888
• NII Article ID: 10008253212
• NII Book ID: AN10453916
• DOI: 10.5458/jag.49.9
• COI: 1:CAS:528:DC%2BD38Xhs1ertbg%3D
• ISSN: 18807291
• ISSN: 13447882
• NDL BIB ID: 6053739
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I6053739
• Web Site: http://www.jstage.jst.go.jp/article/jag1999/49/1/49_1_9/_pdf
• Text Lang: en
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
• Abstract License Flag: Disallowed