Xylanase carbohydrate binding module: recent developments / 生物工程学报
Chinese Journal of Biotechnology
;
(12): 290-296, 2010.
Article
in Chinese
| WPRIM
| ID: wpr-336229
ABSTRACT
Besides the catalytic domain, some xylanases contained a non-catalytic domain which is named as carbohydrate binding module (CBM). CBM can be used to improve their binding-ability to insoluble substrates. We illustrated the importance of CBM by reviewing the source of CBMs, type of families, features of binding to insoluble substrates, specific amino acids involved in substrate-binding, linker peptides connecting the catalytic domain, and the effect of CBMs on xylanase thermostability. CBM is important for xylanase to break down complicate carbohydrates. Perspectives on engineering xylanase activity according to the characteristics of CBMs were given.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Substrate Specificity
/
Binding Sites
/
Catalysis
/
Chemistry
/
Endo-1,4-beta Xylanases
/
Carbohydrate Metabolism
/
Metabolism
/
Multienzyme Complexes
Language:
Chinese
Journal:
Chinese Journal of Biotechnology
Year:
2010
Type:
Article
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