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Nanoparticle‐Mediated Enzyme Immobilization on Cellulose Fibers: Reusable Biocatalytic Systems for Cascade Reactions
Author(s) -
Goldhahn Christian,
Burgert Ingo,
Chanana Munish
Publication year - 2019
Publication title -
advanced materials interfaces
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.671
H-Index - 65
ISSN - 2196-7350
DOI - 10.1002/admi.201900437
Subject(s) - biocatalysis , laccase , immobilized enzyme , reusability , glucose oxidase , horseradish peroxidase , catalysis , cellulose , materials science , nanoparticle , chemical engineering , chemistry , combinatorial chemistry , organic chemistry , nanotechnology , enzyme , biosensor , reaction mechanism , computer science , software , engineering , programming language
Enzymatic biocatalysis has the potential to enable greener and more efficient synthesis routes for the chemical industry. However, enzymes are hard to remove and recover from the reaction solution due to the homogeneous nature of biocatalysis. Hence, enzymes are often limited to single‐use applications. This work shows the immobilization of enzymes based on nanoparticle‐mediated robust physisorption on natural cellulose fibers. The resulting hybrid material is able to perform heterogeneous biocatalysis. The catalytic activity and the multifold reusability of immobilized enzyme are exemplarily investigated for the enzyme laccase. The kinetic parameters of immobilized laccase are determined and compared to the ones of free laccase. Furthermore, relative activities are evaluated in dependence of pH and temperature, and compared to the ones of free enzyme. The heterogeneous biocatalyst is easy to handle and can be quickly and completely removed from the reaction solution due to its macroscopic nature. The potential of multifold reusability of the catalyst is shown for 20 cycles with remaining activities of 45% after 10 and 24% after 20 reaction cycles. The approach may allow for sophisticated enzymatic cascade reaction systems in a simple flow‐through device as exemplarily shown for the immobilized enzymes glucose oxidase and horseradish peroxidase.