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Characteristics 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.260221012
Subject(s) - invertase , chemistry , biochemistry , chromatography , biochemical engineering , enzyme , engineering
Abstract Five kinds of immobilized invertases (IMI)—covalently of porous glass and ion‐exchange resins and ionically on ion‐exchange resins—have been prepared and their kinetic characteristics for sucrose hydrolysis, such as K m , K , pH profile, and thermal stability were studied. Comparing the values of K m and activation energy and the entropy of IMI with those of native invertase, it was concluded that the immobilization influences not binding but kinetic specificity. The effects of the immobilization method on thermal stability were also discussed.