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Co-immobilization of amylases in porous crosslinked gelatin matrices by different reticulations approaches.
Frota, Elionio Galvão; Sartor, Kátia Bitencourt; Biduski, Bárbara; Margarites, Ana Cláudia Freitas; Colla, Luciane Maria; Piccin, Jeferson Steffanello.
Affiliation
  • Frota EG; Post-graduation Program in Food Science and Technology, University of Passo Fundo (UPF), Campus I, km 171, BR 285, P.O. Box 611, 99001-970 Passo Fundo, Rio Grande do Sul, Brazil.
  • Sartor KB; Food Engineering Course, University of Passo Fundo (UPF), Passo Fundo, RS 99052-900, Brazil.
  • Biduski B; Post-graduation Program in Food Science and Technology, University of Passo Fundo (UPF), Campus I, km 171, BR 285, P.O. Box 611, 99001-970 Passo Fundo, Rio Grande do Sul, Brazil.
  • Margarites ACF; Chemical Engineering Course, University of Passo Fundo (UPF), Passo Fundo, RS 99052-900, Brazil.
  • Colla LM; Post-graduation Program in Food Science and Technology, University of Passo Fundo (UPF), Campus I, km 171, BR 285, P.O. Box 611, 99001-970 Passo Fundo, Rio Grande do Sul, Brazil.
  • Piccin JS; Post-graduation Program in Food Science and Technology, University of Passo Fundo (UPF), Campus I, km 171, BR 285, P.O. Box 611, 99001-970 Passo Fundo, Rio Grande do Sul, Brazil. Electronic address: jefersonpiccin@upf.br.
Int J Biol Macromol ; 165(Pt A): 1002-1009, 2020 Dec 15.
Article in En | MEDLINE | ID: mdl-33011269
ABSTRACT
The aim of this study was to carry out the co-immobilization of α-amylase and glucoamylase in crosslinked gelatin porous supports. For this, two methods of co-immobilization were proposed based on the crosslinking with glutaraldehyde (Ggta) or CaCl2 in presence of alginate (Gcal). The supports characterization revealed a porous microstructure with good interaction between its components according to the FTIR analysis and thermal properties. Optimal pH and temperature of the Gcal co-immobilized enzymes were determined at 60 °C and pH 6.0, present an enzymatic activity of 120 µmol·mL·min-1. Moreover, both supports were reused for up to 8 hydrolysis cycles. In addition, co-immobilized enzymes were more efficient than free enzymes in starch saccharification of starch in the long term. These results reveal that the co-immobilization of amylases in gelatinous supports is a promising approach in enzymatic chain reactions.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Starch / Enzymes, Immobilized / Alpha-Amylases / Gelatin Language: En Journal: Int J Biol Macromol Year: 2020 Document type: Article Affiliation country: Brazil

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Starch / Enzymes, Immobilized / Alpha-Amylases / Gelatin Language: En Journal: Int J Biol Macromol Year: 2020 Document type: Article Affiliation country: Brazil