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Immobilization of Aspergillus awamori ß-glucosidase on commercial gelatin: An inexpensive and efficient process.
Nishida, Verônica S; de Oliveira, Roselene F; Brugnari, Tatiane; Correa, Rúbia Carvalho G; Peralta, Rosely A; Castoldi, Rafael; de Souza, Cristina G M; Bracht, Adelar; Peralta, Rosane M.
Afiliação
  • Nishida VS; Department of Biochemistry, Universidade Estadual de Maringá, Maringá, Brazil.
  • de Oliveira RF; Department of Biochemistry, Universidade Estadual de Maringá, Maringá, Brazil; Instituto Federal do Mato Grosso do Sul, Coxim, Brazil.
  • Brugnari T; Department of Biochemistry, Universidade Estadual de Maringá, Maringá, Brazil.
  • Correa RCG; Department of Biochemistry, Universidade Estadual de Maringá, Maringá, Brazil.
  • Peralta RA; Department of Chemistry, Universidade Federal de Santa Catarina, Florianópolis, Brazil.
  • Castoldi R; Department of Biochemistry, Universidade Estadual de Maringá, Maringá, Brazil.
  • de Souza CGM; Department of Biochemistry, Universidade Estadual de Maringá, Maringá, Brazil.
  • Bracht A; Department of Biochemistry, Universidade Estadual de Maringá, Maringá, Brazil.
  • Peralta RM; Department of Biochemistry, Universidade Estadual de Maringá, Maringá, Brazil. Electronic address: rmperalta@uem.br.
Int J Biol Macromol ; 111: 1206-1213, 2018 May.
Article em En | MEDLINE | ID: mdl-29415412
In this work, a ß-glucosidase of Aspergillus awamori with a molecular weight of 180 kDa was produced in solid-state cultures using a mixture of pineapple crown leaves and wheat bran. Maximum production of the enzyme (820 ±â€¯30 U/g substrate) was obtained after 8 days of culture at 28 °C and initial moisture of 80%. The crude enzyme was efficiently immobilized on glutaraldehyde cross-linked commercial gelatin. Immobilization changed the kinetics of the enzyme, whose behavior could no longer be described by a saturation function of the Michaelis-Menten type. Comparative evaluation of the free and immobilized enzyme showed that the immobilized enzyme was more thermostable and less inhibited by glucose than the free form. In consequence of these properties, the immobilized enzyme was able to hydrolyze cellobiose more extensively. In association with Trichoderma reesei cellulase, the free and immobilized ß-glucosidase increased the liberation of glucose from cellulose 3- and 5-fold, respectively. Immobilization of the A. awamori ß-glucosidase on glutaraldehyde cross-linked commercial gelatin is an efficient and cheap method allowing the reuse of the enzyme by at least 10 times.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Aspergillus / Beta-Glucosidase / Enzimas Imobilizadas / Gelatina Idioma: En Revista: Int J Biol Macromol Ano de publicação: 2018 Tipo de documento: Article País de afiliação: Brasil País de publicação: Holanda
Texto completo
Adicionar na Minha BVS
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Aspergillus / Beta-Glucosidase / Enzimas Imobilizadas / Gelatina Idioma: En Revista: Int J Biol Macromol Ano de publicação: 2018 Tipo de documento: Article País de afiliação: Brasil País de publicação: Holanda