A new mechanism and kinetic model for the enzymatic synthesis of short-chain fructooligosaccharides from sucrose

Roberto Vega; M. E. Zuniga-Hansen

doi:10.1016/j.bej.2013.11.012

A new mechanism and kinetic model for the enzymatic synthesis of short-chain fructooligosaccharides from sucrose

Roberto Vega, M. E. Zuniga-Hansen

Research output: Contribution to journal › Article › peer-review

43 Scopus citations

Abstract

A kinetic model based on a ping-pong mechanism was developed under the steady-state hypothesis to account for the short-chain fructooligosaccharides (sc-FOS) synthesis using the commercial cellulolytic enzyme preparation, Rohapect CM. This new mechanism takes into account the interactions between the enzyme species and potential substrates (sucrose and sc-FOS) as a single complex reaction, allowing a better understanding of the reaction kinetics.The initial reaction rate laws appropriately describe the kinetic profiles of the examined substrates. Whereas sucrose exhibited Michaelis-Menten behavior with substrate inhibition, 1-kestose and nystose followed Michaelis-Menten and sigmoid enzyme kinetics. In addition, the enzyme was competitively inhibited by glucose and exhibited significant hydrolytic activity in the presence of nystose.The overall model was simultaneously fitted to experimental data from three initial sucrose concentrations (0.5, 1.5 and 2.1. M) using a multi-response regression with kinetic parameters that have biochemical relevance and are independent of the enzyme concentration. According to the model, sucrose acts almost exclusively as a fructosyl donor substrate. The mathematical development described herein is expected to be suitable for modeling similar enzymatic reaction systems.

Original language	English
Pages (from-to)	158-165
Number of pages	8
Journal	Biochemical Engineering Journal
Volume	82
DOIs	https://doi.org/10.1016/j.bej.2013.11.012
State	Published - 15 Jan 2014
Externally published	Yes

Bibliographical note

Funding Information:
This research was supported financially by the CREAS . In addition, we acknowledge financial support (scholarship and purchase of software) from the Pontificia Universidad Católica de Valparaiso and CONICYT (scholarship 24100148 ) for R. Vega. We are very grateful to Matias Berndt (Dimerco Comercial Ltda., Chile) for the enzyme sample.

Keywords

Enzyme biocatalysis
Fructooligosaccharides
Kinetic parameters
Modeling
Multi-response regression
Sucrose

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10.1016/j.bej.2013.11.012

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title = "A new mechanism and kinetic model for the enzymatic synthesis of short-chain fructooligosaccharides from sucrose",

abstract = "A kinetic model based on a ping-pong mechanism was developed under the steady-state hypothesis to account for the short-chain fructooligosaccharides (sc-FOS) synthesis using the commercial cellulolytic enzyme preparation, Rohapect CM. This new mechanism takes into account the interactions between the enzyme species and potential substrates (sucrose and sc-FOS) as a single complex reaction, allowing a better understanding of the reaction kinetics.The initial reaction rate laws appropriately describe the kinetic profiles of the examined substrates. Whereas sucrose exhibited Michaelis-Menten behavior with substrate inhibition, 1-kestose and nystose followed Michaelis-Menten and sigmoid enzyme kinetics. In addition, the enzyme was competitively inhibited by glucose and exhibited significant hydrolytic activity in the presence of nystose.The overall model was simultaneously fitted to experimental data from three initial sucrose concentrations (0.5, 1.5 and 2.1. M) using a multi-response regression with kinetic parameters that have biochemical relevance and are independent of the enzyme concentration. According to the model, sucrose acts almost exclusively as a fructosyl donor substrate. The mathematical development described herein is expected to be suitable for modeling similar enzymatic reaction systems.",

keywords = "Enzyme biocatalysis, Fructooligosaccharides, Kinetic parameters, Modeling, Multi-response regression, Sucrose",

author = "Roberto Vega and Zuniga-Hansen, {M. E.}",

note = "Funding Information: This research was supported financially by the CREAS . In addition, we acknowledge financial support (scholarship and purchase of software) from the Pontificia Universidad Cat{\'o}lica de Valparaiso and CONICYT (scholarship 24100148 ) for R. Vega. We are very grateful to Matias Berndt (Dimerco Comercial Ltda., Chile) for the enzyme sample. ",

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AU - Vega, Roberto

AU - Zuniga-Hansen, M. E.

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N2 - A kinetic model based on a ping-pong mechanism was developed under the steady-state hypothesis to account for the short-chain fructooligosaccharides (sc-FOS) synthesis using the commercial cellulolytic enzyme preparation, Rohapect CM. This new mechanism takes into account the interactions between the enzyme species and potential substrates (sucrose and sc-FOS) as a single complex reaction, allowing a better understanding of the reaction kinetics.The initial reaction rate laws appropriately describe the kinetic profiles of the examined substrates. Whereas sucrose exhibited Michaelis-Menten behavior with substrate inhibition, 1-kestose and nystose followed Michaelis-Menten and sigmoid enzyme kinetics. In addition, the enzyme was competitively inhibited by glucose and exhibited significant hydrolytic activity in the presence of nystose.The overall model was simultaneously fitted to experimental data from three initial sucrose concentrations (0.5, 1.5 and 2.1. M) using a multi-response regression with kinetic parameters that have biochemical relevance and are independent of the enzyme concentration. According to the model, sucrose acts almost exclusively as a fructosyl donor substrate. The mathematical development described herein is expected to be suitable for modeling similar enzymatic reaction systems.

AB - A kinetic model based on a ping-pong mechanism was developed under the steady-state hypothesis to account for the short-chain fructooligosaccharides (sc-FOS) synthesis using the commercial cellulolytic enzyme preparation, Rohapect CM. This new mechanism takes into account the interactions between the enzyme species and potential substrates (sucrose and sc-FOS) as a single complex reaction, allowing a better understanding of the reaction kinetics.The initial reaction rate laws appropriately describe the kinetic profiles of the examined substrates. Whereas sucrose exhibited Michaelis-Menten behavior with substrate inhibition, 1-kestose and nystose followed Michaelis-Menten and sigmoid enzyme kinetics. In addition, the enzyme was competitively inhibited by glucose and exhibited significant hydrolytic activity in the presence of nystose.The overall model was simultaneously fitted to experimental data from three initial sucrose concentrations (0.5, 1.5 and 2.1. M) using a multi-response regression with kinetic parameters that have biochemical relevance and are independent of the enzyme concentration. According to the model, sucrose acts almost exclusively as a fructosyl donor substrate. The mathematical development described herein is expected to be suitable for modeling similar enzymatic reaction systems.

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KW - Kinetic parameters

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A new mechanism and kinetic model for the enzymatic synthesis of short-chain fructooligosaccharides from sucrose

Abstract

Bibliographical note

Keywords

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