Catalytic and thermodynamic properties of [beta]-glucosidases produced by Lichtheimia corymbifera and Byssochlamys spectabilis

The objective of the present study was to optimize parameters for the cultivation of Lichtheimia corymbifera (mesophilic) and Byssochlamys spectabilis (thermophilic) for the production of [beta]-glucosidases and to compare the catalytic and thermodynamic properties of the partially purified enzymes....

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Bibliographic Details
Published in:Preparative biochemistry & biotechnology 2018-01, Vol.48 (9), p.777
Main Authors: Morais, Tobias Pereira de, Barbosa, Paula Mirella Gomes, Garcia, Nayara Fernanda Lisboa, Rosa-Garzon, Nathália Gonsales da, Fonseca, Gustavo Graciano, Paz, Marcelo Fossa da, Cabral, Hamilton, Leite, Rodrigo Simões Ribeiro
Format: Article
Language:English
Subjects:
Byssochlamys spectabilis
Catalysis
Cultivation
Denaturation
Enzymes
Ethanol
Fermentation
Glucosidase
Lichtheimia corymbifera
Optimization
Parameters
pH effects
Saccharification
Substrates
Thermal stability
Thermodynamic properties
Thermophilic fungi
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Summary:The objective of the present study was to optimize parameters for the cultivation of Lichtheimia corymbifera (mesophilic) and Byssochlamys spectabilis (thermophilic) for the production of [beta]-glucosidases and to compare the catalytic and thermodynamic properties of the partially purified enzymes. The maximum amount of [beta]-glucosidase produced by L. corymbifera was 39 U/g dry substrate (or 3.9 U/mL), and that by B. spectabilis was 77 U/g (or 7.7 U/mL). The optimum pH and temperature were 4.5 and 55 °C and 4.0 and 50 °C for the enzyme from L. corymbifera and B. spectabilis, respectively. [beta]-Glucosidase produced by L. corymbifera was stable at pH 4.0-7.5, whereas the enzyme from B. spectabilis was stable at pH 4.0-6.0. Regarding the thermostability, [beta]-glucosidase produced by B. spectabilis remained stable for 1 h at 50 °C, and that from L. corymbifera was active for 1 h at 45 °C. Determination of thermodynamic parameters confirmed the greater thermostability of the enzyme produced by the thermophilic fungus B. spectabilis, which showed higher values of [Delta]H, activation energy for denaturation (Ea), and half-life t(1/2). The enzymes were stable in the presence of ethanol and were competitively inhibited by glucose. These characteristics contribute to their use in the simultaneous saccharification and fermentation of vegetable biomass.
ISSN:1082-6068
1532-2297
DOI:10.1080/10826068.2018.1509083