Immobilization of glycoside hydrolase families GH1, GH13, and GH70 : state of the art and perspectives

• Autor(a) principal: Graebin, Natália Guilherme
• Data de Publicação: 2016
• Outros Autores: Schöffer, Jessie da Natividade, Andrades, Diandra de, Hertz, Plinho Francisco, Ayub, Marco Antônio Záchia, Rodrigues, Rafael Costa
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Repositório Institucional da UFRGS
• Texto Completo: http://hdl.handle.net/10183/268401
• topic: Imobilização de enzima; Hidrolase; Ciclodextrina glicosiltransferase; Beta-glucosidase; enzyme immobilization; glycoside hydrolases; β-glucosidase; α-amylase; cyclodextrin glycosyltransferase

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 -glucosidase, -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.