Articles
Kinetic modeling approach to analyze enzyme activity assays
Article number
1154_13
Pages
99 – 104
Language
English
Abstract
Pome fruit are commonly stored under controlled atmosphere (CA) conditions to extend their storage life and maintain the quality of the fruit.
However, the optimal gas composition is critical, as respiratory metabolism under low oxygen conditions can shift to a fermentative metabolism.
This shift is expected to be regulated by changes in the level of involved enzymes, affecting their overall activity.
In this work, we developed a kinetic modeling approach to estimate in vitro the specific enzyme activity from the spectrophotometric assay data of two main fermentation enzymes extracted from ‘Jonagold’ apple (Malus × domestica Borkh.
‘Jonagold’). This model takes into account the entire progress of the curve to analyze the enzyme activity of pyruvate decarboxylase and alcohol dehydrogenase.
The kinetic model is based on Michaelis-Menten kinetics and first-order kinetics, which describe the conversion of substrate into product by the enzyme.
It can accurately predict the enzyme activity of pyruvate decarboxylase and alcohol dehydrogenase.
In contrast to the law of Lambert Beer, the model is also valid when the assumption of linearity is not fulfilled.
The use of a kinetic model to estimate enzyme activity can be extended to other enzymes as long as the underlying reaction mechanism is known.
However, the optimal gas composition is critical, as respiratory metabolism under low oxygen conditions can shift to a fermentative metabolism.
This shift is expected to be regulated by changes in the level of involved enzymes, affecting their overall activity.
In this work, we developed a kinetic modeling approach to estimate in vitro the specific enzyme activity from the spectrophotometric assay data of two main fermentation enzymes extracted from ‘Jonagold’ apple (Malus × domestica Borkh.
‘Jonagold’). This model takes into account the entire progress of the curve to analyze the enzyme activity of pyruvate decarboxylase and alcohol dehydrogenase.
The kinetic model is based on Michaelis-Menten kinetics and first-order kinetics, which describe the conversion of substrate into product by the enzyme.
It can accurately predict the enzyme activity of pyruvate decarboxylase and alcohol dehydrogenase.
In contrast to the law of Lambert Beer, the model is also valid when the assumption of linearity is not fulfilled.
The use of a kinetic model to estimate enzyme activity can be extended to other enzymes as long as the underlying reaction mechanism is known.
Authors
J. Boeckx, M.L.A.T.M. Hertog, A.H. Geeraerd, B.M. Nicolai
Keywords
kinetic model, enzyme activity, alcohol dehydrogenase, pyruvate decarboxylase
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