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Deactivation of free and stabilized acid phosphatase by urea
Author(s) -
Gianfreda Liliana,
Marrucci Giuseppe,
Greco Guido
Publication year - 1986
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.260281108
Subject(s) - urea , chemistry , ultrafiltration (renal) , membrane , kinetics , enzyme , concentration polarization , phosphatase , polymer , chromatography , chemical engineering , inorganic chemistry , organic chemistry , biochemistry , physics , quantum mechanics , engineering
Abstract Tests on acid phosphatase (E.G. 3.1.3.2) deactivation by urea have been performed at two pH values. Two conditions have been used: native enzyme operating batch‐wise in dilute solution and stabilized enzyme in continuous flow ultrafiltration membrane reactor. Stabilization is achieved by confining the enzyme within a concentrated solution of a linear chain polymer that forms a polarization layer over the membrane. The results provide significant information on the kinetics and thermodynamics of the complex phenomena taking place during deactivation. Deactivation by urea is also compared with thermal deactivation.