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Highly stable novel silica/chitosan support for ß-galactosidase immobilization for application in dairy technology.
Ricardi, Natália Carminatti; de Menezes, Eliana Weber; Valmir Benvenutti, Edilson; da Natividade Schöffer, Jéssie; Hackenhaar, Camila Regina; Hertz, Plinho Francisco; Costa, Tania Maria Haas.
Afiliação
  • Ricardi NC; Instituto de Química (IQ), Universidade Federal do Rio Grande do Sul (UFRGS), Porto Alegre, RS, Brazil.
  • de Menezes EW; Instituto de Química (IQ), Universidade Federal do Rio Grande do Sul (UFRGS), Porto Alegre, RS, Brazil.
  • Valmir Benvenutti E; Instituto de Química (IQ), Universidade Federal do Rio Grande do Sul (UFRGS), Porto Alegre, RS, Brazil.
  • da Natividade Schöffer J; Instituto de Ciência e Tecnologia de Alimentos (ICTA), Universidade Federal do Rio Grande do Sul (UFRGS), Porto Alegre, RS, Brazil.
  • Hackenhaar CR; Instituto de Ciência e Tecnologia de Alimentos (ICTA), Universidade Federal do Rio Grande do Sul (UFRGS), Porto Alegre, RS, Brazil.
  • Hertz PF; Instituto de Ciência e Tecnologia de Alimentos (ICTA), Universidade Federal do Rio Grande do Sul (UFRGS), Porto Alegre, RS, Brazil.
  • Costa TMH; Instituto de Química (IQ), Universidade Federal do Rio Grande do Sul (UFRGS), Porto Alegre, RS, Brazil. Electronic address: taniaha@iq.ufrgs.br.
Food Chem ; 246: 343-350, 2018 Apr 25.
Article em En | MEDLINE | ID: mdl-29291859
ß-d-Galactosidase is an important enzyme in the dairy industry, and the enzyme from the yeast Kluyveromyces lactis is most widely used. Here, we report immobilization of the enzyme on a silica/chitosan composite support, devised to have 10% and 20% chitosan (SiQT10 and SiQT20, respectively). Morphological and textural characterizations showed that chitosan is dispersed in micrometric regions in silica. For comparison, a silica organofunctionalized with 3-aminopropyltrimethoxysilane (SiO2aptms) was prepared. Performance of the biocatalysts was tested for lactose hydrolysis, and the enzyme immobilized in SiQT10 and SiQT20 composites showed higher efficiency (62% and 47%, respectively) compared with the enzyme in SiO2aptms. Operational stability in this system was evaluated for the first time. After 200 h of continuous use in a fixed-bed reactor, SiQT10 remained with approximately 90% activity. Thus, in addition to demonstrating compatibility for food processing, these results align the enzyme stabilization properties of chitosan with the mechanical resistance of silica.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Beta-Galactosidase / Dióxido de Silício / Quitosana / Enzimas Imobilizadas Idioma: En Ano de publicação: 2018 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Beta-Galactosidase / Dióxido de Silício / Quitosana / Enzimas Imobilizadas Idioma: En Ano de publicação: 2018 Tipo de documento: Article