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

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 co...

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Bibliographic Details
Published in:Journal of chemical technology and biotechnology (1986) 2018-09, Vol.93 (9), p.2625-2634
Main Authors: Gascón, Victoria, Márquez‐Álvarez, Carlos, Blanco, Rosa María
Format: Article
Language:English
Subjects:
Cages
Catalysis
Catalytic activity
Chemical activity
Encapsulation
Enzymatic activity
enzyme immobilization
Enzymes
Glucosidase
Immobilization
in‐situ
Leaching
ordered mesoporous silica materials
Organic chemistry
post‐synthesis
Proteins
Synthesis
β‐glucosidase
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Summary: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. © 2018 Society of Chemical Industry
ISSN:0268-2575
1097-4660
DOI:10.1002/jctb.5616