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Kinetic and enzymatic adsorption model in a recirculation hollow-fibre bioreactor

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Abstract

A general procedure has been developed to model the behaviour of enzymatic reactions in a membrane bioreactor. This procedure unifies the kinetics of the reaction and the adsorption of the enzyme or enzymatic complexes on the membrane, enabling the selection of the most appropriate kinetic model. The general procedure proposed has been particularized and applied to experimental results obtained with two enzymatic reactions carried out in a hollow-fibre reactor, enzymatic hydrolysis of lactose by β-galactosidase and glucose–fructose isomerization by glucose isomerase. The application of the general model has allowed us to determine the mechanism of the reaction for both kinetic reactions, assuming the adsorption of the enzymatic complex EGa for lactose hydrolysis and the adsorption of the free enzyme onto the membrane for glucose–fructose isomerization.

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Abbreviations

C E :

Concentration of total active enzyme (g/L)

E :

Concentration of free enzyme present in the reaction medium (M)

E 1,E 2,...,E e :

Concentration of different enzymatic complexes in the medium reaction (M)

ECS:

Extracapillary space

EGa :

Concentration of the enzyme-galactose complex (M)

EGan :

Concentration of the enzyme-galactose complex adsorbed onto the active centre of the membrane (M)

EL :

Concentration of the enzyme-lactose complex (M)

ELn :

Concentration of the enzyme-lactose complex adsorbed onto the active centre of the membrane (M)

En,E 1 n,E 2 n,...,E e n :

Concentration of the enzymatic species E,E 1,E 2,...,E e adsorbed onto the membrane (M)

e T :

Mols of active enzyme per gram of enzyme (mol/g)

F :

Concentration of fructose (M)

Ga :

Concentration of galactose (M)

Ga 0 :

Initial concentration of galactose (M)

Gl :

Concentration of glucose (M)

Gl 0 :

Initial concentration of glucose (M)

GOD-Perid:

Glucose-oxidase peroxidase

ΔH ad :

Adsorption enthalpy (kJ/mol)

k :

Rate constant of Eq. 2 (molglucose mol −1enzyme  h−1)

k 1,k −1,k 1a ,k −1a ,k 2,k −2,k 3,k −3,...,k e ,k −e :

Individual kinetic constants of the general model proposed

K D0,K D1,K D2,...,K De :

Equilibrium constants of adsorption of the different enzymatic species onto the membrane (dimensionless)

K e :

Equilibrium constant of glucose–fructose isomerization (dimensionless)

k g ,k f :

Kinetic constants of isomerization (L mol−1 h−1)

k −g ,k −f :

Kinetic constants of isomerization (h−1)

K I :

Equilibrium constant of Eq. 3 (M)

K M :

Michaelis-Menten constant (M)

K mf :

Michaelis-Menten constant for fructose–glucose isomerization (M)

K mg :

Michaelis-Menten constant for glucose–fructose isomerization (M)

L :

Concentration of monohydrate lactose (M)

L 0 :

Initial concentration of monohydrate lactose (M)

n :

Concentration of empty active centres on the membrane surface

r :

Reaction rate of glucose–fructose isomerization (mol g−1 h−1)

r fru :

Reaction rate of fructose–glucose isomerization in the RHFB (mol g−1 h−1)

RHFB:

Recirculation hollow-fibre bioreactor

r lac :

Lactose-hydrolysis reaction rate in a RHFB (mol g−1 h−1)

S 0 :

Initial concentration of substrate in the fructose–glucose isomerization and initial concentration of lactose and galactose in lactose hydrolysis (M)

t :

Time (h)

T :

Temperature

V mf :

Maximum rate reaction in fructose–glucose isomerization (mol g−1 h−1)

x :

Conversion (dimensionless)

X :

Concentration of intermediate complex (M)

x e :

Equilibrium conversion (dimensionless)

Xn :

Concentration of the enzymatic species X adsorbed onto the membrane (M)

x 0 :

Initial conversion in fructose–glucose isomerization (dimensionless)

y :

Treatment intensity (g h/L)

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Acknowledgements

We are grateful to Novozymes for providing the enzyme Lactozym and to Genencor International for providing the enzyme Spezyme GI. We also thank Sorin-Biomédica for providing the hollow-fibre modules used in this work.

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Authors and Affiliations

  1. Departamento Ingeniería Química, Facultad Ciencias, Universidad de Granada, Campus Universitario Fuentenueva, Avda. Fuentenueva, s/n, 18071, Granada, Spain

    E. Jurado, F. Camacho, G. Luzón & J. M. Vicaria

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Correspondence to E. Jurado.

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Jurado, E., Camacho, F., Luzón, G. et al. Kinetic and enzymatic adsorption model in a recirculation hollow-fibre bioreactor. Bioprocess Biosyst Eng 28, 27–36 (2005). https://doi.org/10.1007/s00449-005-0007-2

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  • DOI: https://doi.org/10.1007/s00449-005-0007-2

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