Affordable Access

deepdyve-link
Publisher Website

Carbohydrate-binding modules influence substrate specificity of an endoglucanase from Clostridium thermocellum.

Authors
  • Ichikawa, Shunsuke1
  • Yoshida, Mitsuki1
  • Karita, Shuichi1, 2
  • Kondo, Makoto2
  • Goto, Masakazu2
  • 1 a Graduate School of Regional Innovation Studies , Mie University , Tsu , Japan. , (Japan)
  • 2 b Graduate School of Bioresources , Mie University , Tsu , Japan. , (Japan)
Type
Published Article
Journal
Bioscience Biotechnology and Biochemistry
Publisher
Informa UK (Taylor & Francis)
Publication Date
Jan 01, 2015
Volume
80
Issue
1
Pages
188–192
Identifiers
DOI: 10.1080/09168451.2015.1069696
PMID: 26223555
Source
Medline
Keywords
License
Unknown

Abstract

Most cellulases contain carbohydrate-binding modules (CBMs) that largely contribute to their activity for insoluble substrates. Clostridium thermocellum Cel5E is an endoglucanase having xylanolytic activity. The Cel5E originally has a family 11 CBM preferentially binding to β-1,4- and β-1,3-1,4-mixed linkage glucans. In this study, we replaced the CBM with a different type of CBM, either a family 3 microcrystalline cellulose-directed CBM from Clostridium josui scaffoldin, or a family 6 xylan-directed CBM from Clostridium stercorarium xylanase 11A. Chimeric endoglucanases showed enhanced activity that was affected by CBM binding specificity. These chimeric enzymes could efficiently degrade milled lignocellulosic materials, such as corn hulls, because of heterologous components in the plant cell wall, indicating that diverse CBMs play roles in degradation of lignocellulosic materials.

Report this publication

Statistics

Seen <100 times