alexa Reuse of Cyclodextrin Glycosyltransferase through Immob
ISSN: 2329-6674

Enzyme Engineering
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Research Article

Reuse of Cyclodextrin Glycosyltransferase through Immobilization on Magnetic Carriers

Kate Cristina Blanco1, Francisco José dos Santos2, Natalia Sozza Bernardi1, Miguel Jafelicci Júnior3,
Rubens Monti4 and Jonas Contiero1*
1Unesp-Universidade Estadual Paulista, Biological Sciences Institute, Department of Biochemistry and Microbiology, Laboratory of Industrial Microbiology, 24 A Avenue, Bela Vista, Rio Claro, SP, CEP 13506-900, Brazil
2Procell Biologics-Av. Comendador. Alfredo Maffei, 4001-Jardim São Carlos, São Carlos, SP Cep: 13561-270, Brazil
3Unesp-Universidade Estadual Paulista, Chemical Institute, Department of Physical Chemistry, Prof. Francisco Degni Street, Quitandinha, Araraquara, SP. CEP 14800-900, Brazil
4Unesp-Universidade Estadual Paulista, Department of Food and Nutrition, Rodovia Araraquara-Jaú, Km 1, Araraquara, SP, Brazil
Corresponding Author : Jonas Contiero
Unesp-Universidade Estadual Paulista, Biological Sciences Institute
Department of Biochemistry and Microbiology, Laboratory of Industrial Microbiology
24 A Avenue, Bela Vista, Rio Claro, SP, CEP 13506-900, Brazil
Tel: +55 19 35264180
Fax: +55 19 3526 4176
E-mail: [email protected]
Received May 02, 2013; Accepted May 03, 2013; Published May 10, 2013
Citation: Blanco KC, dos Santos FJ, Bernardi NS, Júnior MJ, Monti R, et al. (2013) Reuse of Cyclodextrin Glycosyltransferase through Immobilization on Magnetic Carriers. Enz Eng 2:111. doi:10.4172/2329-6674.1000111
Copyright: © 2013 Blanco KC, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.


CGTase from Bacillus lehensis isolated from wastewater of a cassava flour mill in the state of São Paulo, Brazil was immobilized after being partially purified using precipitation with ammonium sulfate. The partially purified CGTase was immobilized by covalent binding on a magnetite support, which was silanized with 3-aminopropyltrimethoxysilane and activated with glutaraldehyde, resulting in a yield of 16.27% and final activity of 17.54% of the initial activity. The physicochemical properties and kinetics of cyclodextrin glycosyltransferase from Bacillus lehensis were determined. The optimum temperature of the immobilized CGTase was higher than that of the soluble enzyme (70°C and 55°C, respectively). The optimum pH of the immobilized enzyme was the same as that of the soluble enzyme (pH 8.0). In the pH and thermo stability assays, 50% of enzyme activity was maintained after 24 h and 26.22% of the initial activity was retained after 160 min, respectively. The Michaelis-Menten constant was 0.82 and maximum velocity was 45.45−1.min−1. In the reuse study of the immobilized enzyme after four cycles, 16.66% of the initial catalytic activity was maintained, demonstrating the ability to recover and reuse the enzyme immobilized on magnetite.


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