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Molecules 2016, 21(8), 1074; doi:10.3390/molecules21081074

Immobilization of Glycoside Hydrolase Families GH1, GH13, and GH70: State of the Art and Perspectives

Biotechnology, Bioprocess, and Biocatalysis Group, Food Science and Technology Institute, Federal University of Rio Grande do Sul, Av. Bento Gonçalves 9500, P.O. Box 15090, ZC 91501-970 Porto Alegre, RS, Brazil
These authors contributed equally to this manuscript.
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Author to whom correspondence should be addressed.
Academic Editor: Roberto Fernandez-Lafuente
Received: 27 July 2016 / Revised: 11 August 2016 / Accepted: 12 August 2016 / Published: 17 August 2016
(This article belongs to the Special Issue Enzyme Immobilization 2016)
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Abstract

Glycoside hydrolases (GH) are enzymes capable to hydrolyze the glycosidic bond between two carbohydrates or even between a carbohydrate and a non-carbohydrate moiety. Because of the increasing interest for industrial applications of these enzymes, the immobilization of GH has become an important development in order to improve its activity, stability, as well as the possibility of its reuse in batch reactions and in continuous processes. In this review, we focus on the broad aspects of immobilization of enzymes from the specific GH families. A brief introduction on methods of enzyme immobilization is presented, discussing some advantages and drawbacks of this technology. We then review the state of the art of enzyme immobilization of families GH1, GH13, and GH70, with special attention on the enzymes β-glucosidase, α-amylase, cyclodextrin glycosyltransferase, and dextransucrase. In each case, the immobilization protocols are evaluated considering their positive and negative aspects. Finally, the perspectives on new immobilization methods are briefly presented. View Full-Text
Keywords: enzyme immobilization; glycoside hydrolases; β-glucosidase; α-amylase; cyclodextrin glycosyltransferase; dextransucrase enzyme immobilization; glycoside hydrolases; β-glucosidase; α-amylase; cyclodextrin glycosyltransferase; dextransucrase
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Graebin, N.G.; Schöffer, J.N.; Andrades, D.D.; Hertz, P.F.; Ayub, M.A.Z.; Rodrigues, R.C. Immobilization of Glycoside Hydrolase Families GH1, GH13, and GH70: State of the Art and Perspectives. Molecules 2016, 21, 1074.

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