Exploring magnetic and imprinted cross-linked enzyme aggregates of rhamnopyranosidase in microbioreactors

Exploring magnetic and imprinted cross-linked enzyme aggregates of rhamnopyranosidase in... •Development of rhamnopyranosidase crosslink enzyme aggregates functionalized with magnetite.•Magnetic rhamnopyranosidase could be separated from reaction mixture by magnetic field.•4′,5,7-trihydroxyflavanone-7-rhamnoglucoside hydrolysis with rhamnopyranosidase was optimized.•Development of a mini-packed bed reactor with magnetic rhamnopyranosidase crosslink aggregates.•Magnetized rhamnopyranosidase crosslink aggregates show enhanced stability and reusability. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Bioresource Technology Elsevier

Exploring magnetic and imprinted cross-linked enzyme aggregates of rhamnopyranosidase in microbioreactors

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Publisher
Elsevier
Copyright
Copyright © 2017 Elsevier Ltd
ISSN
0960-8524
D.O.I.
10.1016/j.biortech.2017.10.078
Publisher site
See Article on Publisher Site

Abstract

•Development of rhamnopyranosidase crosslink enzyme aggregates functionalized with magnetite.•Magnetic rhamnopyranosidase could be separated from reaction mixture by magnetic field.•4′,5,7-trihydroxyflavanone-7-rhamnoglucoside hydrolysis with rhamnopyranosidase was optimized.•Development of a mini-packed bed reactor with magnetic rhamnopyranosidase crosslink aggregates.•Magnetized rhamnopyranosidase crosslink aggregates show enhanced stability and reusability.

Journal

Bioresource TechnologyElsevier

Published: Feb 1, 2018

References

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