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Surfactant‐Induced Unfolding of Cellulase: Kinetic Studies
Author(s) -
Stoner Michael R.,
Dale Douglas A.,
Gualfetti Peter J.,
Becker Todd,
Randolph Theodore W.
Publication year - 2006
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp0501468
Subject(s) - pulmonary surfactant , chemistry , cellulase , micelle , kinetics , ionic strength , chemical engineering , monomer , critical micelle concentration , ionic bonding , chromatography , enzyme , organic chemistry , biochemistry , aqueous solution , ion , polymer , physics , quantum mechanics , engineering
Surfactant‐induced unfolding is a significant degradation pathway for detergent enzymes. This study examines the kinetics of surfactant‐induced unfolding for endoglucanase III, a detergent cellulase, under conditions of varying pH, temperature, ionic strength, surfactant type, and surfactant concentration. Interactions between protein and surfactant monomer are shown to play a key role in determining the kinetics of the unfolding process. We demonstrate that the unfolding rate can be slowed by (1) modifying protein charge and/or pH conditions to create electrostatic repulsion of ionic surfactants and (2) reducing the amount of monomeric ionic surfactant available for interaction with the enzyme (i.e., by lowering the critical micelle concentration). Additionally, our results illustrate that there is a poor correlation between thermodynamic stability in buffer (Δ G unfolding ) and resistance to surfactant‐induced unfolding.