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Activity losses among T4 lysozyme variants after adsorption to colloidal silica
Author(s) -
Bower C. K.,
Xu Q.,
McGuire J.
Publication year - 1998
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(19980620)58:6<658::aid-bit13>3.0.co;2-3
Subject(s) - lysozyme , thermostability , adsorption , chemistry , colloid , enzyme , enzyme assay , amino acid , biochemistry , organic chemistry
Maintaining a specific molecular conformation is essential for the proper functioning of an enzyme. A substantial loss of catalytic activity can occur from the displacement caused by even a single amino acid substitution. Activity may also be lost as an enzyme undergoes a conformational change during adsorption. In this study, we investigated the effect of thermostability on the activities of three T4 lysozyme variants after adsorption to 9 nm colloidal silica particles. Less‐stable T4 lysozyme variants lost more activity after adsorption than did more stable variants, apparently because they experienced more extensive structural alteration. © 1998 John Wiley & Sons, Inc. Biotechnol Bioeng 58: 658–662, 1998.