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Simultaneous hydrolysis of tri- and tetrasaccharides by industrial mixtures of glucoamylase and α-amylase: kinetics and thermodynamics

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Abstract

The present paper deals with the study of the kinetics and thermodynamics of batch enzymic hydrolysis of multisubstrate media in the presence of more than one glucanase. A kinetic model, similar to the one proposed for competitive inhibition, is presented to describe the competition between two substrates, tri- and tetrasaccharides, for the same enzyme, glucoamylase. A literature research on the most recurrent values of the Michaelis-Menten constant also shows a linear relationship between this parameter and the molecular weight of the sugar substrate for a given glucanase.

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Abbreviations

a dimensionless:

empirical parameter in Eq. (1)

b dimensionless:

empirical parameter in Eq. (1)

B dimensionless:

empirical parameter in Eq. (6)

E kg/m3 :

enzyme concentration

E a kcal/mol:

activation energy

kc kg/m3 :

competition constant

k M kg/m3 :

Michaelis-Menten constant

MW kg·10−3 :

molecular weight

r mol/(min·kg):

specific hydrolysis rate of glucoamylase

R cal/(°K·mol):

ideal gas constant

S kg/m3 :

substrate concentration

T °K:

absolute temperature

v kg/(m3·h):

hydrolysis rate of glucoamylase

1:

values referring to trisaccharides

2:

values referring to tetrasaccharides

0:

starting values

max:

maximum values

References

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Authors and Affiliations

  1. Institute of Chemical Engineering Science and Technology, University of Genoa, Via Opera Pia, 15, I-16145, Genoa, Italy

    A. Converti, G. Fiorito, M. Del Borghi & G. Ferraiolo

Authors
  1. A. Converti
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  2. G. Fiorito
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  3. M. Del Borghi
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  4. G. Ferraiolo
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Converti, A., Fiorito, G., Del Borghi, M. et al. Simultaneous hydrolysis of tri- and tetrasaccharides by industrial mixtures of glucoamylase and α-amylase: kinetics and thermodynamics. Bioprocess Engineering 7, 165–170 (1991). https://doi.org/10.1007/BF00387412

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  • DOI: https://doi.org/10.1007/BF00387412

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