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Glucose Isomerase and Its Behaviour under Hydrogenation Conditions
Author(s) -
Makkee M.,
Kieboom A. P. G.,
van Bekkum H.
Publication year - 1985
Publication title -
starch ‐ stärke
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.62
H-Index - 82
eISSN - 1521-379X
pISSN - 0038-9056
DOI - 10.1002/star.19850370706
Subject(s) - chemistry , fructose , glucose 6 phosphate isomerase , isomerase , isomerization , sugar , mannitol , enzyme , biochemistry , catalysis
A survey is given of glucose isomerase, its sources, its mechanism of isomerization and its data and properties in three different immobilized forms. In addition, the effect of a number of parameters on the activity of immobilized glucose isomerase has been investigated, e. g. hydrogen pressure, Mg(II) and Ca(II), transition metal ions, borate and sugar alcohols. Immobilized glucose isomerase remains sufficiently active under hydrogenation conditions to maintain D ‐glucose and D ‐fructose in equilibrium. D ‐Glucitol, in contrast to D ‐mannitol, has some inhibiting effect on the enzyme action. The D ‐glucose/ D ‐fructose equilibrium constant is independent of the total sugar concentration (between 0.2 – 2.2‐M).