Reaction Kinetics and Modeling of the Enzyme-catalyzed Production of Lactosucrose using .BETA.-Fructofuranosidase from Arthrobacter sp. K-1.
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- PILGRIM Axel
- Department of Chemical Engineering, Faculty of Engineering, Kyoto University
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- KAWASE Motoaki
- Department of Chemical Engineering, Faculty of Engineering, Kyoto University
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- OHASHI Masayasu
- Department of Chemical Engineering, Faculty of Engineering, Kyoto University
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- FUJITA Koki
- Bio Research Corporation of Yokohama
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- MURAKAMI Kazufumi
- Bio Research Corporation of Yokohama
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- HASHIMOTO Kenji
- Department of Chemical Engineering, Faculty of Engineering, Kyoto University Present affiliation: Department of Applied Physics and Chemistry, Fukui University of Technology
Bibliographic Information
- Other Title
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- Reaction Kinetics and Modeling of the Enzyme-catalyzed Production of Lactosucrose using β-Fructofuranosidase from Arthrobacter sp. K-1
- Reaction Kinetics and Modeling of the Enzyme catalyzed Production of Lactosucrose using ベータ Fructofuranosidase from Arthrobacter sp K 1
- Reaction kinetics and modeling of the enzyme-catalyzed production of lactosucrose using β -fructofuranosidase from Athrobacter sp. K-1
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Description
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.
Journal
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 65 (4), 758-765, 2001
Japan Society for Bioscience, Biotechnology, and Agrochemistry
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Details 詳細情報について
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- CRID
- 1390001206475864064
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- NII Article ID
- 110002680342
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- NII Book ID
- AA10824164
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- COI
- 1:CAS:528:DC%2BD3MXjsVags7k%3D
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- ISSN
- 13476947
- 09168451
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- NDL BIB ID
- 5768775
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- PubMed
- 11388450
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- Abstract License Flag
- Disallowed