Reaction kinetics and modeling of the enzyme-catalyzed production of lactosucrose using β-fructofuranosidase from Arthrobacter sp. K-1

Article abstract of DOI:10.1271/bbb.65.758

Lactosucrose synthesis from sucrose and lactose was carried out by using β-fructofuranosidase from Arthrobacter sp. K-1. The transfructosylation mechanism was found to be of an ordered bi-bi type in which sucrose was bound first to the enzyme and lactosucrose was released last. Hydrolysis side-reaction experiments indicated that the reactions were uncompetitively inhibited by glucose and lactose, while no inhibition by fructose was apparent. The overall reaction rates were formulated. The reaction rate constants, equilibrium constant, and dissociation and Michaelis constants were determined at 35°C and 50°C by fitting the experimental concentration changes with the calculated values by a nonlinear least-square method. The average relative derivation for the concentrations was 9.67%. The kinetic parameters were also calculated for 43°C and 60°C by assuming the Arrhenius law, and the course of reaction was predicted. The obtained reaction rate equations well represented the concentration changes during the experiment at all temperatures.

Full text of DOI:10.1271/bbb.65.758

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Reaction Kinetics and Modeling of the Enzyme-
catalyzed Production of Lactosucrose using β-
Fructofuranosidase from Arthrobacter sp. K-1
a
a
a
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Axel PILGRIM , Motoaki KAWASE , Masayasu OHASHI , Koki FUJITA , Kazufumi MURAKAMI
ac
&
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Kenji HASHIMOTO
Department of Chemical Engineering, Faculty of Engineering, Kyoto University
Bio Research Corporation of Yokohama
b
c
Present affiliation: Department of Applied Physics and Chemistry, Fukui University of
Technology
Published online: 22 May 2014.
To cite this article: Axel PILGRIM, Motoaki KAWASE, Masayasu OHASHI, Koki FUJITA, Kazufumi MURAKAMI & Kenji
HASHIMOTO (2001) Reaction Kinetics and Modeling of the Enzyme-catalyzed Production of Lactosucrose using β-
Fructofuranosidase from Arthrobacter sp. K-1, Bioscience, Biotechnology, and Biochemistry, 65:4, 758-765, DOI: 10.1271/
bbb.65.758
To link to this article: http://dx.doi.org/10.1271/bbb.65.758
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