2021
DOI: 10.1039/d0cy01413c
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Laccase aggregates via poly-lysine-supported immobilization onto PEGA resin, with efficient activity and high operational stability and can be used to degrade endocrine-disrupting chemicals

Abstract: Immobilized enzymes possess catalytic activity as well as substrate specificity. Even though enzyme immobilization techniques for industrial applications are well established, the operational stability of immobilized enzymes often needs to...

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Cited by 18 publications
(9 citation statements)
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“…Enzyme immobilization is the most important strategy to address these problems. [14][15][16][17][18] Many efforts have been made to improve the catalysis performance of ADH and AmDH by developing efficient enzyme immobilization technology. 8,19,20 For example, Schmidt-Dannert et al designed a protein scaffold to site-specifically anchor ADH and AmDH with the aid of SpyTag-SpyCatcher for the production of (R)-2aminohexane.…”
Section: Introductionmentioning
confidence: 99%
“…Enzyme immobilization is the most important strategy to address these problems. [14][15][16][17][18] Many efforts have been made to improve the catalysis performance of ADH and AmDH by developing efficient enzyme immobilization technology. 8,19,20 For example, Schmidt-Dannert et al designed a protein scaffold to site-specifically anchor ADH and AmDH with the aid of SpyTag-SpyCatcher for the production of (R)-2aminohexane.…”
Section: Introductionmentioning
confidence: 99%
“…Because immobilized enzymes prepared by adsorptive, ionic, or covalent binding are immobilized at one or several points on the support materials, these immobilized enzymes have a high degree of freedom in their conformational structures and can only be reused a limited number of times, as they are easily desaturated and deactivated. To overcome this, complexes of enzymes and poly-Lys have been cross-linked and conjugated to a support material [46]. This method can immobilize the enzyme at high concentrations, thus improving catalyst efficiency.…”
Section: Cross-linkingmentioning
confidence: 99%
“…Yamaguchi and Miyazaki (2021) studied the removal of the endocrine disruptor bisphenol A (BPA) (100 μM) by laccase immobilized by cross‐linking on polyethylene glycol acrylamide (PEGA) resin in batch and flow reactors. [ 23 ] They found a BPA removal of 144 μM h −1 at 30°C for the batch reactor and of 2880 μM h −1 at 50°C for the flow reactor. However, the volume of the batch reactor was not mentioned and that of the flow reactor was very tiny (a polytetrafluoroethylene tube of 39.25 μL).…”
Section: Immobilized‐laccase Bioreactors For Wastewater Treatmentmentioning
confidence: 99%