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

Lauri Kuutti, Leif Laaksonen, Tuula Teeri

Research output: Chapter in Book/Report/Conference proceedingConference abstract in proceedingsScientific

Abstract

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.
Original languageEnglish
Title of host publicationCellulose '91
EditorsHelena L. Chum
PublisherAmerican Chemical Society ACS
DOIs
Publication statusPublished - 1991
MoE publication typeNot Eligible
EventCellulose '91 - New Orleans, United States
Duration: 2 Dec 19916 Dec 1991

Conference

ConferenceCellulose '91
CountryUnited States
CityNew Orleans
Period2/12/916/12/91

Keywords

  • molecular modelling
  • chemical modelling

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  • Cite this

    Kuutti, L., Laaksonen, L., & Teeri, T. (1991). Interaction studies of the tail domain of cellobiohydrolase I and crystalline cellulose using molecular modelling. In H. L. Chum (Ed.), Cellulose '91 [28] American Chemical Society ACS. https://doi.org/10.1063/1.41322