Specific Adsorption of Clostridium stercorarium Xylanase to Amorphous Cellulose and Its Desorption by Cellobiose

T Goro; K Shuichi; T Asako; A Md Mainul; K Tetsuya; S Kazuo; O Kunio

doi:10.1271/bbb.60.1183

Specific Adsorption of Clostridium stercorarium Xylanase to Amorphous Cellulose and Its Desorption by Cellobiose

Biosci Biotechnol Biochem. 1996 Jan;60(7):1183-5. doi: 10.1271/bbb.60.1183.

Authors

T Goro¹, K Shuichi^{1

2}, T Asako¹, A Md Mainul¹, K Tetsuya¹, S Kazuo¹, O Kunio¹

Affiliations

¹ a Department of Bioscience, Faculty of Bioresources Mie University , Tsu 514 , Japan.
² b Center for Molecular Biology and Genetics , Mie University , Tsu 514 , Japan.

PMID: 27299720
DOI: 10.1271/bbb.60.1183

Abstract

Clostidium stercorarium xylanase A (XynA) composed of a family 11 catalytic domain of glycosyl hydrolases and family VI CBDs bound to amorphous cellulose, i.e., acid-swollen cellulose (ASC), but not highly crystalline cellulose, and it was released from the cellulose protein complex by wash with a cellobiose solution. The Ka and [PC]max values of ASC were 0.25 liter/μmol and 26μmol/g.

Keywords: Clostridium stercorarium; cellulose-binding domain; xylanase.