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Kinetic study on thermal stability of immobilized invertase
Author(s) -
Ooshima Hiroshi,
Sakimoto Masuo,
Harano Yoshio
Publication year - 1980
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.260221013
Subject(s) - invertase , covalent bond , hydrolysis , thermal stability , chemistry , ionic strength , kinetics , immobilized enzyme , ionic bonding , substrate (aquarium) , chromatography , sucrose , enzyme , kinetic energy , ion exchange , chemical engineering , porous glass , organic chemistry , ion , porosity , aqueous solution , physics , oceanography , quantum mechanics , engineering , geology
The kinetic study of the thermal stability of three kinds of invertases: native, immobilized on porous glass covalently, and on ion‐exchange resin ionically, has been carried out, measuring their enzymatic activity for sucrose hydrolysis. Thermal deactivations of all invertases obeyed first‐order kinetics, being independent of substrate concentration, with k d and Δ E d , Δ S d * as shown in Tables I and II, respectively. Based on these parameter values, the effects of immobilization and pH at deactivation on the stability have been considered, and it was suggested that the ionic bond gives a more loosely deformed enzyme than the covalent bond.