Successful encapsulation of β-glucosidase during the synthesis of siliceous mesostructured materials

Victoria Gascón, Carlos Márquez-Álvarez, Rosa María Blanco

Research output: Contribution to journalArticlepeer-review

Abstract

BACKGROUND: The biocatalysis field demands ‘universal’ supports able to encapsulate enzymes with a straightforward methodology, and at the same time, capable of retaining their catalytic activity. The employment of siliceous materials for such a purpose is a big challenge because drastic synthesis conditions are required and improved functionalization is needed to increase affinities towards the targeted enzyme. In this work, a compromise between the development of a well-formed mesostructured support and an acceptable enzymatic activity was attempted via the in-situ immobilization approach. RESULTS: The immobilization of β-glucosidase (EC 3.2.1.21) from Aspergillus niger was approached using different strategies. After trying to immobilize β-glucosidase with a post-synthesis approach, nonhigh loadings were achieved both with covalent linkage (using epoxy activated supports; 3.5 mgE g−1) and with noncovalent bonding (using amine-functionalized materials; 7.6 mgE g−1). However, when the in-situ approach was attempted, success in reaching the highest enzyme loading (close to 200 mgE g−1) was achieved. CONCLUSION: In this work, the support cages around the in-situ encapsulated enzyme fully prevented its release through the narrow windows connecting cages, achieving a less than 5% release of the initially desorbed protein, as well as a further total absence of leaching. This enabled the biocatalyst to be reused at least eight times more without any loss in activity.

Original languageEnglish
Pages (from-to)2625-2634
Number of pages10
JournalJournal of Chemical Technology and Biotechnology
Volume93
Issue number9
DOIs
Publication statusPublished - Sep 2018

Keywords

  • enzyme immobilization
  • in-situ
  • ordered mesoporous silica materials
  • post-synthesis
  • β-glucosidase

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