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Updated: Jul 11, 2026
A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
Published on: November 7, 2012
Fluorinated chloramphenicol acetyltransferase thermostability and activity profile: improved thermostability by a
Natalya Voloshchuk1, Man Xia Lee, Wan Wen Zhu
1Department of Chemical and Biological Sciences, Polytechnic University, 6 Metrotech Center, Brooklyn, NY 11201, USA.
Abstract:
A lysate-based thermostability and activity profile is described for chloramphenicol acetyltransferase (CAT) expressed in trifluoroleucine, T (CAT T). CAT and 13 single-isoleucine CAT mutants were expressed in medium supplemented with T and assayed for thermostability on cell lysates. Although fluorinated mutants, L82I T and L208I T, showed losses in thermostability, the L158I T fluorinated mutant demonstrated an enhanced thermostability relative to CAT T. Further characterization of L158I T suggested that T at position 158 contributed to a portion of the observed loss in thermostability upon global fluorination.
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