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Activity losses among T4 lysozyme charge variants after adsorption to colloidal silica
Author(s) -
Bower C. K.,
Sananikone S.,
Bothwell M. K.,
McGuire J.
Publication year - 1999
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/(sici)1097-0290(19990805)64:3<373::aid-bit14>3.0.co;2-j
Subject(s) - lysozyme , adsorption , enzyme , chemistry , colloid , charge (physics) , enzyme assay , substrate (aquarium) , surface charge , catalysis , chemical engineering , biophysics , organic chemistry , biochemistry , biology , ecology , physics , quantum mechanics , engineering
Enzyme structure and function depend to some extent on enzyme net charge and charge location. Altering the charge of even a single residue may affect the interaction between enzyme and substrate such that all catalytic activity is lost. In this study we investigated the effect of net charge and charge location on the enzymatic activity of synthetic mutants of bacteriophage T4 lysozyme in the presence of colloidal silica. Enzymatic activity decreased upon adsorption, and these changes were variant‐specific. Results were interpreted with reference to differences in adsorbed enzyme structure and orientation, and electrostatic effects. By exploring the effects of enzyme charge on adsorption, it may be possible to gain a better understanding of how enzyme structure influences adsorption and function at an interface. © 1999 John Wiley & Sons, Inc. Biotechnol Bioeng 64: 373–376, 1999.