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An enzymatic membrane reactor for oligodextran production: Effects of enzyme immobilization strategies on dextranase activity.
Su, Ziran; Luo, Jianquan; Sigurdardóttir, Sigyn Björk; Manferrari, Thomas; Jankowska, Katarzyna; Pinelo, Manuel.
Afiliação
  • Su Z; Process and Systems Engineering Centre, Department of Chemical and Biochemical Engineering, Technical University of Denmark, 2800, Kgs, Lyngby, Denmark.
  • Luo J; State Key Laboratory of Biochemical Engineering, Institute of Process Engineering, University of Chinese Academy of Sciences, Chinese Academy of Sciences, Beijing 100190, China. Electronic address: jqluo@ipe.ac.cn.
  • Sigurdardóttir SB; Process and Systems Engineering Centre, Department of Chemical and Biochemical Engineering, Technical University of Denmark, 2800, Kgs, Lyngby, Denmark.
  • Manferrari T; Process and Systems Engineering Centre, Department of Chemical and Biochemical Engineering, Technical University of Denmark, 2800, Kgs, Lyngby, Denmark.
  • Jankowska K; Process and Systems Engineering Centre, Department of Chemical and Biochemical Engineering, Technical University of Denmark, 2800, Kgs, Lyngby, Denmark; Institute of Chemical Technology and Engineering, Faculty of Chemical Technology, Poznan University of Technology, Berdychowo 4, PL-60965, Poznan,
  • Pinelo M; Process and Systems Engineering Centre, Department of Chemical and Biochemical Engineering, Technical University of Denmark, 2800, Kgs, Lyngby, Denmark. Electronic address: mp@kt.dtu.dk.
Carbohydr Polym ; 271: 118430, 2021 Nov 01.
Article em En | MEDLINE | ID: mdl-34364570
An enzymatic membrane reactor (EMR) with immobilized dextranase provides an excellent opportunity for tailoring the molecular weight (Mw) of oligodextran to significantly improve product quality. However, a highly efficient EMR for oligodextran production is still lacking and the effect of enzyme immobilization strategy on dextranase hydrolysis behavior has not been studied yet. In this work, a functional layer of polydopamine (PDA) or nanoparticles made of tannic acid (TA) and hydrolysable 3-amino-propyltriethoxysilane (APTES) was first coated on commercial membranes. Then cross-linked dextranase or non-cross-linked dextranase was loaded onto the modified membranes using incubation mode or fouling-induced mode. The fouling-induced mode was a promising enzyme immobilization strategy on the membrane surface due to its higher enzyme loading and activity. Moreover, unlike the non-cross-linked dextranase that exhibited a normal endo-hydrolysis pattern, we surprisingly found that the cross-linked dextranase loaded on the PDA modified surface exerted an exo-hydrolysis pattern, possibly due to mass transfer limitations. Such alteration of hydrolysis pattern has rarely been reported before. Based on the hydrolysis behavior of the immobilized dextranase in different EMRs, we propose potential applications for the oligodextran products. This study presents a unique perspective on the relation between the enzyme immobilization process and the immobilized enzyme hydrolysis behavior, and thus opens up a variety of possibilities for the design of a high-performance EMR.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Oligossacarídeos / Dextranos / Reatores Biológicos / Dextranase / Enzimas Imobilizadas / Membranas Artificiais Idioma: En Revista: Carbohydr Polym Ano de publicação: 2021 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Oligossacarídeos / Dextranos / Reatores Biológicos / Dextranase / Enzimas Imobilizadas / Membranas Artificiais Idioma: En Revista: Carbohydr Polym Ano de publicação: 2021 Tipo de documento: Article