Immobilization and characterization of laccase and its use in the biodegradation of paper mill effluent.

Pacheco, S.; Soares, Carlos Henrique Lemos

doi:10.5935/0100-4042.20140036

Cited by 1 publication

(1 citation statement)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Assays were tested at different reaction temperatures (20, 30 or 40 °C). Reactions were performed at pH 4, since previous pH studies using immobilized laccase and syringaldazine as substrate have reported best enzymatic rates at this pH [45]. Individual substrate saturation data was fitted to Equation 2 using STATISTICA 7 Software.…”

Section: Methodsmentioning

confidence: 99%

Substrate Specificity and Enzyme Recycling Using Chitosan Immobilized Laccase

et al. 2014

View full text Add to dashboard Cite

Abstract:The immobilization of laccase (Aspergillus sp.) on chitosan by cross-linking and its application in bioconversion of phenolic compounds in batch reactors were studied. Investigation was performed using laccase immobilized via chemical cross-linking due to the higher enzymatic operational stability of this method as compared to immobilization via physical adsorption. To assess the influence of different substrate functional groups on the enzyme's catalytic efficiency, substrate specificity was investigated using chitosan-immobilized laccase and eighteen different phenol derivatives. It was observed that 4-nitrophenol was not oxidized, while 2,5-xylenol, 2,6-xylenol, 2,3,5-trimethylphenol, syringaldazine, OPEN ACCESSMolecules 2014, 19 16795 2,6-dimetoxyphenol and ethylphenol showed reaction yields up 90% at 40 °C. The kinetic of process, enzyme recyclability and operational stability were studied. In batch reactors, it was not possible to reuse the enzyme when it was applied to syringaldazne bioconversion. However, when the enzyme was applied to bioconversion of 2,6-DMP, the activity was stable for eight reaction batches.

show abstract

Section: Methodsmentioning

confidence: 99%