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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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Published in: | Preparative biochemistry & biotechnology 2018-01, Vol.48 (9), p.777 |
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creator | 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 |
description | 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. |
doi_str_mv | 10.1080/10826068.2018.1509083 |
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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. 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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.</description><subject>Byssochlamys spectabilis</subject><subject>Catalysis</subject><subject>Cultivation</subject><subject>Denaturation</subject><subject>Enzymes</subject><subject>Ethanol</subject><subject>Fermentation</subject><subject>Glucosidase</subject><subject>Lichtheimia corymbifera</subject><subject>Optimization</subject><subject>Parameters</subject><subject>pH effects</subject><subject>Saccharification</subject><subject>Substrates</subject><subject>Thermal stability</subject><subject>Thermodynamic properties</subject><subject>Thermophilic fungi</subject><issn>1082-6068</issn><issn>1532-2297</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><recordid>eNqNj81OwzAQhC1EJcrPIyBZ4pzgddXGuVKBOHDkhlC1sZ3GVRwHr3PwhWfHRTwAl53V7DcjLWP3IGoQSjyWIXdip2opQNWwFa1Qmwu2hu1GVlK2zWXZC1OdoSt2TXQSAtoG1Jp97zHhmJPTHCfD02CjDyZP6IszxzDbmJwlHnr-0dmEn9VxXHQgZ5CKXQizaGt4l_mb00PJO--Q6xCz71xvI_72PmWioIcRfSZOs9UJOzc6umWrHkeyd396wx5ent_3r1Up_lospcMpLHEqp4OEBgCa82__o34A6_hYww</recordid><startdate>20180101</startdate><enddate>20180101</enddate><creator>Morais, Tobias Pereira de</creator><creator>Barbosa, Paula Mirella Gomes</creator><creator>Garcia, Nayara Fernanda Lisboa</creator><creator>Rosa-Garzon, Nathália Gonsales da</creator><creator>Fonseca, Gustavo Graciano</creator><creator>Paz, Marcelo Fossa da</creator><creator>Cabral, Hamilton</creator><creator>Leite, Rodrigo Simões Ribeiro</creator><general>Taylor & Francis Ltd</general><scope>7QL</scope><scope>7QO</scope><scope>7QR</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope></search><sort><creationdate>20180101</creationdate><title>Catalytic and thermodynamic properties of [beta]-glucosidases produced by Lichtheimia corymbifera and Byssochlamys spectabilis</title><author>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</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-proquest_journals_21711179083</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Byssochlamys spectabilis</topic><topic>Catalysis</topic><topic>Cultivation</topic><topic>Denaturation</topic><topic>Enzymes</topic><topic>Ethanol</topic><topic>Fermentation</topic><topic>Glucosidase</topic><topic>Lichtheimia corymbifera</topic><topic>Optimization</topic><topic>Parameters</topic><topic>pH effects</topic><topic>Saccharification</topic><topic>Substrates</topic><topic>Thermal stability</topic><topic>Thermodynamic properties</topic><topic>Thermophilic fungi</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Morais, Tobias Pereira de</creatorcontrib><creatorcontrib>Barbosa, Paula Mirella Gomes</creatorcontrib><creatorcontrib>Garcia, Nayara Fernanda Lisboa</creatorcontrib><creatorcontrib>Rosa-Garzon, Nathália Gonsales da</creatorcontrib><creatorcontrib>Fonseca, Gustavo Graciano</creatorcontrib><creatorcontrib>Paz, Marcelo Fossa da</creatorcontrib><creatorcontrib>Cabral, Hamilton</creatorcontrib><creatorcontrib>Leite, Rodrigo Simões Ribeiro</creatorcontrib><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Preparative biochemistry & biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Morais, Tobias Pereira de</au><au>Barbosa, Paula Mirella Gomes</au><au>Garcia, Nayara Fernanda Lisboa</au><au>Rosa-Garzon, Nathália Gonsales da</au><au>Fonseca, Gustavo Graciano</au><au>Paz, Marcelo Fossa da</au><au>Cabral, Hamilton</au><au>Leite, Rodrigo Simões Ribeiro</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Catalytic and thermodynamic properties of [beta]-glucosidases produced by Lichtheimia corymbifera and Byssochlamys spectabilis</atitle><jtitle>Preparative biochemistry & biotechnology</jtitle><date>2018-01-01</date><risdate>2018</risdate><volume>48</volume><issue>9</issue><spage>777</spage><pages>777-</pages><issn>1082-6068</issn><eissn>1532-2297</eissn><abstract>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.</abstract><cop>Philadelphia</cop><pub>Taylor & Francis Ltd</pub><doi>10.1080/10826068.2018.1509083</doi></addata></record> |
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subjects | Byssochlamys spectabilis Catalysis Cultivation Denaturation Enzymes Ethanol Fermentation Glucosidase Lichtheimia corymbifera Optimization Parameters pH effects Saccharification Substrates Thermal stability Thermodynamic properties Thermophilic fungi |
title | Catalytic and thermodynamic properties of [beta]-glucosidases produced by Lichtheimia corymbifera and Byssochlamys spectabilis |
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