Ionic liquid salt-induced inactivation and unfolding of cellulase from Trichoderma reesei

M.B. Turner, S.K. Spear, J.G. Huddleston, John Holbrey, Robin Rogers

Research output: Contribution to journalArticlepeer-review

339 Citations (Scopus)

Abstract

The potential for performing cellulase-catalyzed reactions on cellulose dissolved in 1-butyl-3-methylimidazolium chloride ([bmim] Cl) has been investigated. We have carried out a systematic study on the irreversible solvent and ionic strength-induced inactivation and unfolding of cellulase from Trichoderma reesei ( E.C.#3.2.1.4). Experiments, varying both cellulase and IL solvent concentrations, have indicated that [bmim] Cl, and several other ILs, as well as dimethylacetamide-LiCl (a well-known solvent system for cellulose), inactivate cellulase under these conditions. Despite cellulase inactivity, results obtained from this study led to valuable insights into the requirements necessary for enzyme activity in IL systems. Enzyme stability was determined during urea, NaCl, and [bmim] Cl-induced denaturation observed through fluorescence spectroscopy. Protein stability of a PEG-supported cellulase in [bmim] Cl solution was investigated and increased stability/activity of the PEG-supported cellulase in both the [bmim] Cl and citrate buffer solutions were detected.
Original languageEnglish
Pages (from-to)443-447
Number of pages5
JournalGreen Chemistry
Volume5
Issue number4
DOIs
Publication statusPublished - Aug 2003

ASJC Scopus subject areas

  • Chemistry(all)

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