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Stability and activity modulation of chymotrypsins in AOT reversed micelles by protein–interface interaction: Interaction of α‐chymotrypsin with a negative interface leads to a cooperative breakage of a salt bridge that keeps the catalytic active conformation (Ile 16 –Asp 194 )
Author(s) -
Almeida Fábio C. L.,
Valente Ana Paula,
Chaimovich Hernan
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(19980805)59:3<360::aid-bit12>3.0.co;2-i
Subject(s) - salt bridge , interface (matter) , chymotrypsin , modulation (music) , breakage , salt (chemistry) , chemistry , micelle , materials science , biophysics , trypsin , physics , enzyme , biochemistry , pulmonary surfactant , biology , aqueous solution , mutant , gene , gibbs isotherm , acoustics , composite material
The stability of α‐chymotrypsin and δ‐chymotrypsin was studied in reversed micelles of sodium bis(2‐ethylhexyl)sulfosuccinate (AOT) in isooctane. α‐Chymotrypsin is inactivated at the interface and at the water pool, while δ‐chymotrypsin is inactivated only at the water pool. The mechanism of inactivation at the interface is related to the interaction of N‐terminal group alanine 149 (absent in δ‐chymotrypsin) with the negative interface. The dependence of enzyme activity on water content of these two enzymes in reversed micelles of AOT is also related with the interface interaction, since δ‐chymotrypsin does not have a bell‐shaped curve as observed for α‐chymotrypsin. © 1998 John Wiley & Sons, Inc. Biotechnol Bioeng 59:360–363, 1998.