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

Adam Orłowski, Tomasz Róg, Sami Paavilainen, Moutusi Manna, Isto Heiskanen, Kaj Backfolk, Jussi Timonen, Ilpo Vattulainen

    Research output: Contribution to journalArticleScientificpeer-review

    14 Citations (Scopus)

    Abstract

    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.

    Original languageEnglish
    Pages (from-to)2911-2925
    Number of pages15
    JournalCellulose
    Volume22
    Issue number5
    Early online date17 Jul 2015
    DOIs
    Publication statusPublished - 2015
    Publication typeA1 Journal article-refereed

    Keywords

    • Cellulose
    • Enzyme
    • Molecular dynamics simulation

    Publication forum classification

    • Publication forum level 2

    ASJC Scopus subject areas

    • Polymers and Plastics

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