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Solid‐state enzyme deactivation in air and in organic solvents
Author(s) -
Toscano Giuseppe,
Pirozzi Domenico,
Maremonti Michele,
Greco Guido
Publication year - 1994
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.260440604
Subject(s) - chemistry , kinetics , enzyme , thermal stability , salt (chemistry) , thermal , organic chemistry , chemical engineering , inorganic chemistry , stereochemistry , thermodynamics , physics , quantum mechanics , engineering
Thermal deactivation of solid‐state acid phosphates (E.C. 3.1.3.2, from potato) is analyzed, both in the presence and in the absence of organic solvents. The thermal deactivation profile departs from first order kinetics and shows an unusual activity. The process is described by a phenomenological equation, whose theoretical implications are also discussed. The total amount of buffer salts in the enzyme powder dramatically affects enzyme stability in the range 70×C to 105×C. The higher salt/protein ratio increases the rate of thermal deactivation. The deactivation rate is virtually unaffected by the presence of organic solvents, independent of their hydrophilicity. © 1994 John Wiley & Sons, Inc.