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Acid phosphatase deactivation by a series mechanism
Author(s) -
Gianfreda Liliana,
Marrucci Giuseppe,
Grizzuti Nino,
Greco Guido
Publication year - 1984
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/bit.260260518
Subject(s) - chemistry , hydrolysis , phosphate , acid phosphatase , enzyme , phosphatase , kinetics , stereochemistry , organic chemistry , physics , quantum mechanics
Acid phosphatase (E.C.3.1.3.2.) thermal deactivation at pH 3.77 has been investigated by monitoring the enzyme activity as a function of time in the hydrolysis of p ‐nitrophenyl phosphate. The experimental curves obtained show a two‐slope behavior in a log (activity)versus‐time plot, which indicates that deactivation occurs via a complex mechanism. From the dependence of the kinetic parameters on both deactivation and hydrolysis temperatures, it is inferred that the deactivation mechanism involves intermediate, temperature‐dependent, less‐active forms of the enzyme. This interpretation is confirmed by the results of additional tests in which the temperature was suddenly changed during the deactivation process.