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How endoglucanase enzymes act on cellulose nanofibrils: role of amorphous regions revealed by atomistic simulations

Research output: Contribution to journalArticleScientificpeer-review


Original languageEnglish
Pages (from-to)2911-2925
Number of pages15
Issue number5
Early online date17 Jul 2015
Publication statusPublished - 2015
Publication typeA1 Journal article-refereed


Transformation of cellulose into monosaccharides can be achieved in a chemical process performed by a special group of enzymes known as cellulases. We have used atomistic molecular dynamics simulations to study endoglucanase II (Cel5A) that is one of the proteins in this group. Based on the atomistic simulation results, we discuss how the Cel5A enzyme interacts with cellulose fibrils comprised of both crystalline and amorphous regions. We show that the enzyme’s carbohydrate-binding domain prefers to interact with crystalline regions of cellulose, while the catalytic domain has a high affinity to the amorphous regions of fibrils. In particular, through electrostatic interactions the catalytic domain attracts loose glucose chains to its catalytic cleft. The atomistic details of the enzyme–cellulose interaction are presented and the implications for practical applications are briefly discussed.

ASJC Scopus subject areas


  • Cellulose, Enzyme, Molecular dynamics simulation

Publication forum classification

Field of science, Statistics Finland