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1.
J Biotechnol ; 344: 57-69, 2022 Jan 20.
Artigo em Inglês | MEDLINE | ID: mdl-34973971

RESUMO

The present work was conducted to investigate the immobilization of lipase from Penicillium sp. onto three modified bentonites by simple adsorption and crosslinking methods. The composites were characterized by FTIR, SEM and BET. The free and bentonite-supported lipase was evaluated in terms of operational and storage stability and pH and thermal activity and stability. The kinetic parameters were also evaluated. The results show that all immobilized enzymes had better thermal and pH stability compared to free enzymes. Among the immobilized enzymes, GDU-bent-lipase had more efficient performance in thermal (38% of its initial activity within 24 h at 65 °C), operational (70% residual activity after 9 cycles), storage stability (70.14% of its initial activities at 4 °C for 21 days), and kinetic properties (effectiveness factor 0.79 relative to free enzyme) than free and other immobilized enzymes. The adsorption isotherm was modeled by Langmuir, Freundlich and Temkin isotherms which Langmuir isotherm indicated a better fit of the experimental adsorption data. To the best of our knowledge, this is the first comparative report about the immobilization of lipase Produced by Penicillium sp., isolated from olive mill wastewater, and the most comprehensive study about the immobilization of lipase onto several supports.


Assuntos
Lipase , Penicillium , Adsorção , Bentonita , Estabilidade Enzimática , Enzimas Imobilizadas/metabolismo , Concentração de Íons de Hidrogênio , Lipase/metabolismo , Temperatura
2.
Prep Biochem Biotechnol ; 51(7): 659-668, 2021.
Artigo em Inglês | MEDLINE | ID: mdl-33269956

RESUMO

Laccases are a group of oxidases that catalyze the oxidation of a wide range of electron rich substrates like phenolic compounds, lignin and aromatic amines. They are of interest because of their potential to be used in environmental and industrial applications. In this research, potent laccase producer fungi were screened and isolated from olive mill wastewater (OMW). One of the 23 isolated fungi was identified as Galactomyces geotrichum based on 18S rDNA sequence analysis that detected good laccase activity. Produced laccase had a molecular weight of 55 kDa that was confirmed by zymogram analysis. This is the first report about the optimization of laccase Production by G. geotrichum under solid-state fermentation. The optimization was made by the Taguchi design of experiments (DOE) methodology. An orthogonal array (L25) was designed using Minitab 19 software to study four effective process factors in five levels for laccase production. The optimum condition derived was; moisture content (80%), fermentation time (14 day), CuSO4⋅5H2O as the inducer (300 µM), glucose as a co-substrate (5 g/L). Maximum laccase activity of 52.86 (U/g of dry substrate) was obtained using optimum fermentation condition. This study aimed to better understand the laccase producing microorganisms in OMW and take them to OMW treatment that is rich in phenolic compounds.


Assuntos
Proteínas Fúngicas , Geotrichum/crescimento & desenvolvimento , Lacase , Proteínas Fúngicas/biossíntese , Proteínas Fúngicas/química , Proteínas Fúngicas/isolamento & purificação , Lacase/biossíntese , Lacase/química , Lacase/isolamento & purificação
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