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Conflict of Interest: In relation to this article, we declare that there is no conflict of interest.

Publication history: Received March 9, 2012
Accepted July 2, 2012

This is an Open-Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/bync/3.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Improvement of lactulose synthesis through optimization of reaction conditions with immobilized β-galactosidase

Yoon Seok Song Young Joon Suh Chulhwan Park¹ Seung Wook Kim^†

Department of Chemical and Biological Engineering, Korea University, 5Ga, Anam-dong, Sungbuk-gu, Seoul 136-701, Korea ¹Department of Chemical Engineering, Kwangwoon University, 447-1, Wolgye-dong, Nowon-gu, Seoul 139-701, Korea

kimsw@korea.ac.kr

Korean Journal of Chemical Engineering, January 2013, 30(1), 160-165(6), 10.1007/s11814-012-0105-1

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Abstract

Kluyveromyces lactis β-galactosidase was immobilized on silica gels using a covalent bonding method. To improve lactulose synthesis using immobilized β-galactosidase, the optimal reaction conditions, such as lactose and fructose concentrations, pH and ionic strength of the buffer, loading amount of the enzyme and temperature, were determined. Lactulose synthesis using the immobilized β-galactosidase was markedly improved after optimization of the reaction conditions. When the lactulose synthesis was carried out at 47 ℃ using 40% (w/v) lactose, 20% (w/v) fructose and immobilized β-galactosidase of 12 U/ml in 50 mM sodium phosphate buffer at pH 7.5, the lactulose concentration and specific productivity were 15.80 g/l and 1.32 mg/U·h, respectively. In addition, when the immobilized β-galactosidase was reused for lactulose synthesis, its catalytic activity retained 60.5% after 10 reuses.

Keywords

β-Galactosidase Lactulose Optimization Transgalactosylation Immobilization

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