Stability of immobilized laccase on Luffa Cylindrica fibers and assessment of synthetic hormone degradation

In this work were studied the pH, thermal, and storage stability of free and immobilized laccases. Enzymes were produced by Pleurotus ostreatus on potato dextrose (PD) broth and potato dextrose modified (PDM) broth, and immobilized using Luffa cylindrica fibers as support. Both free and immobilized...

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Published in:Preparative biochemistry & biotechnology 2019, Vol.49 (1), p.58-63
Main Authors: Lacerda, Monike Fabiane Alves Ribeiro, Lopes, Flávio Marques, Sartoratto, Adilson, Ponezi, Alexandre Nunes, Thomaz, Douglas Vieira, Schimidt, Fernando, Santiago, Mariângela Fontes
Format: Article
Language:English
Subjects:
Bioremediation
Degradation
Dextrose
Enzymatic activity
Enzymes
Ethinylestradiol
Fibers
Immobilization
Immobilized enzymes
Laccase
lignocellulosic natural fiber
lignolitic enzyme
Luffa cylindrica
Optimization
pH effects
Pleurotus ostreatus
Potatoes
Shelf life
Stability analysis
Storage
Storage stability
Temperature
Thermal stability
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Summary:In this work were studied the pH, thermal, and storage stability of free and immobilized laccases. Enzymes were produced by Pleurotus ostreatus on potato dextrose (PD) broth and potato dextrose modified (PDM) broth, and immobilized using Luffa cylindrica fibers as support. Both free and immobilized enzymes were assessed on their respective enzymatic activities and for 17α-ethinylestradiol (EE2) degradation. The optimum pH conditions concerning laccase activity ranged from 3.6 to 4.6, while temperature ranged between 30 °C and 50 °C for both free and immobilized enzyme. Laccase produced using PD broth presented greater storage stability and thermal stability than that of PDM. Best EE2 removals were of 79.22% and 75.00% for the free and immobilized enzymes, respectively. Removal rates were assessed during 8 h at pH 5. The removal of 17α-ethinylestradiol was stabilized in the fourth cycle of use. Results imply that immobilization promoted stability towards pH and temperature variations, although media played a decisive role in the enzymatic activity. Both free and immobilized laccases of P. ostreatus were able to degrade EE2, whereas immobilized laccase in PDM medium presented possible reuse applicability, albeit removal was not optimal when compared to other reports.
ISSN:1082-6068
1532-2297
DOI:10.1080/10826068.2018.1525568