Specific Adsorption ofClostridium stercorariumXylanase to Amorphous Cellulose and Its Desorption by Cellobiose
Author(s) -
Goro Takada,
Shuichi Karita,
Asako Takeuchi,
Ahsan Md. Mainul,
Tetsuya Kimura,
Sakka Kazuo,
Kunio Ohmiya
Publication year - 1996
Publication title -
bioscience biotechnology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.509
H-Index - 116
eISSN - 1347-6947
pISSN - 0916-8451
DOI - 10.1271/bbb.60.1183
Subject(s) - cellobiose , cellulose , chemistry , adsorption , xylanase , amorphous solid , cellulase , crystallinity , desorption , glycosyl , polymer chemistry , organic chemistry , chromatography , enzyme , crystallography
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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom