Premium
Induction of catalytic activity in proteins by lyophilization in the presence of a transition state analogue
Author(s) -
Slade Christopher J.,
Vulfson Evgeny N.
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(19980120)57:2<211::aid-bit9>3.0.co;2-q
Subject(s) - catalysis , chemistry , isopropyl , bovine serum albumin , substrate (aquarium) , amine gas treating , serum albumin , imprinting (psychology) , polymer , transition (genetics) , combinatorial chemistry , chromatography , biochemistry , organic chemistry , biology , ecology , gene
The induction of catalytic activity in proteins by lyophilization in the presence of a transition state analogue (biomolecular imprinting) has been attempted. It was shown that proteins which were freeze‐dried with n‐isopropyl‐4‐nitrobenzyl‐amine (a transition state analogue for the reaction of dehydrofluorination of 4‐fluoro‐4‐[p‐nitrophenyl] butan‐2‐one) displayed higher β‐elimination activity as compared to their‐non‐imprinted counterparts. It was also found that native bovine serum albumin has a high dehydrofluorination activity towards the above substrate with kinetic parameters rather similar to those of a catalytic antibody prepared by Shokat et al. (1989). A comparison of the kinetic parameters determined in this study with those obtained for analogous catalytic antibodies and imprinted polymers was made. © 1998 John Wiley & Sons, Inc. Biotechnol. Bioeng. 57: 211–215, 1998.