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A kinetic model for the hydrolysis and synthesis of maltose, isomaltose, and maltotriose by glucoamylase
Author(s) -
Beschkov V.,
Marc A.,
Engasser J. M.
Publication year - 1984
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.260260106
Subject(s) - isomaltose , maltotriose , maltose , hydrolysis , chemistry , maltitol , chromatography , autocatalysis , biochemistry , sugar , enzyme , catalysis
Kinetic results on the glucomylase‐catalysed hydrolysis of maltose and maltotriose, and glucose polymerization into maltose and isomaltose up to 450 g/L total sugar concentration are presented. Whereas the enzyme has a faster hydrolytic and synthetic activity on α‐(1→4) than on α‐(1→6) linkages, at equilibrium, on the contrary, the isomaltose level which represents 15% (w/w) of the total sugar concentration at the highest investigated concentrations is much higher than the corresponding maltose level. Under a wide range of initial conditions, experimental results are adequately described by a new kinetic model with simple first‐ and second‐order, or Michaelian‐type, rate expressions for the reversible hydrolysis of maltotriose, maltose, and isomaltose. The model also accounts for the inhibition of hydrolysis by glucose, but does not consider the concentration of water which, under the present conditions, was not found kinetically limiting.