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Interaction studies of the tail domain of cellobiohydrolase I and crystalline cellulose using molecular modelling

 

作者: L. Kuutti,   L. Laaksonen,   T. Teeri,  

 

期刊: AIP Conference Proceedings  （AIP Available online 1991）
卷期: Volume 239, issue 1  

页码: 348-348

 

ISSN:0094-243X

 

年代: 1991

 

DOI:10.1063/1.41322

 

出版商: AIP

 

数据来源: AIP

 

摘要:

Cellulose is the most abundant organic compound in the biosphere. In nature, crystalline cellulose is hydrolysed by specific enzymes called cellulases. Understanding the physico‐chemical nature of these enzymatic processes will be essential for developing new energy saving and non polluting methods for cellulose degradation and modification.

 

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