Production and Characterization of Highly Thermostable β-Glucosidase during the Biodegradation of Methyl Cellulose by Fusarium oxysporum

Production of β-glucosidase from Fusarium oxysporum was investigated during degradation of some cellulosic substrates (Avicel, α-cellulose, carboxymethyl cellulose (CMC), and methylcellulose). Optimized production of β-glucosidase using the cellulosic substrate that supported highest yield of enzyme...

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Main Authors: Folasade M. Olajuyigbe, Chidinma M. Nlekerem, Olusola A. Ogunyewo
Format: Article
Language:English
Published: Wiley 2016-01-01
Series:Biochemistry Research International
Online Access:http://dx.doi.org/10.1155/2016/3978124
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author Folasade M. Olajuyigbe
Chidinma M. Nlekerem
Olusola A. Ogunyewo
author_facet Folasade M. Olajuyigbe
Chidinma M. Nlekerem
Olusola A. Ogunyewo
author_sort Folasade M. Olajuyigbe
collection DOAJ
description Production of β-glucosidase from Fusarium oxysporum was investigated during degradation of some cellulosic substrates (Avicel, α-cellulose, carboxymethyl cellulose (CMC), and methylcellulose). Optimized production of β-glucosidase using the cellulosic substrate that supported highest yield of enzyme was examined over 192 h fermentation period and varied pH of 3.0–11.0. The β-glucosidase produced was characterized for its suitability for industrial application. Methyl cellulose supported the highest yield of β-glucosidase (177.5 U/mg) at pH 6.0 and 30°C at 96 h of fermentation with liberation of 2.121 μmol/mL glucose. The crude enzyme had optimum activity at pH 5.0 and 70°C. The enzyme was stable over broad pH range of 4.0–7.0 with relative residual activity above 60% after 180 min of incubation. β-glucosidase demonstrated high thermostability with 83% of its original activity retained at 70°C after 180 min of incubation. The activity of β-glucosidase was enhanced by Mn2+ and Fe2+ with relative activities of 167.67% and 205.56%, respectively, at 5 mM and 360% and 315%, respectively, at 10 mM. The properties shown by β-glucosidase suggest suitability of the enzyme for industrial applications in the improvement of hydrolysis of cellulosic compounds into fermentable sugars that can be used in energy generation and biofuel production.
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publishDate 2016-01-01
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series Biochemistry Research International
spelling doaj-art-b04c61d9a1ec4318a62ddd69a88451bd2025-02-03T01:22:35ZengWileyBiochemistry Research International2090-22472090-22552016-01-01201610.1155/2016/39781243978124Production and Characterization of Highly Thermostable β-Glucosidase during the Biodegradation of Methyl Cellulose by Fusarium oxysporumFolasade M. Olajuyigbe0Chidinma M. Nlekerem1Olusola A. Ogunyewo2Enzyme Biotechnology and Environmental Health Unit, Department of Biochemistry, Federal University of Technology, Akure 340001, NigeriaEnzyme Biotechnology and Environmental Health Unit, Department of Biochemistry, Federal University of Technology, Akure 340001, NigeriaEnzyme Biotechnology and Environmental Health Unit, Department of Biochemistry, Federal University of Technology, Akure 340001, NigeriaProduction of β-glucosidase from Fusarium oxysporum was investigated during degradation of some cellulosic substrates (Avicel, α-cellulose, carboxymethyl cellulose (CMC), and methylcellulose). Optimized production of β-glucosidase using the cellulosic substrate that supported highest yield of enzyme was examined over 192 h fermentation period and varied pH of 3.0–11.0. The β-glucosidase produced was characterized for its suitability for industrial application. Methyl cellulose supported the highest yield of β-glucosidase (177.5 U/mg) at pH 6.0 and 30°C at 96 h of fermentation with liberation of 2.121 μmol/mL glucose. The crude enzyme had optimum activity at pH 5.0 and 70°C. The enzyme was stable over broad pH range of 4.0–7.0 with relative residual activity above 60% after 180 min of incubation. β-glucosidase demonstrated high thermostability with 83% of its original activity retained at 70°C after 180 min of incubation. The activity of β-glucosidase was enhanced by Mn2+ and Fe2+ with relative activities of 167.67% and 205.56%, respectively, at 5 mM and 360% and 315%, respectively, at 10 mM. The properties shown by β-glucosidase suggest suitability of the enzyme for industrial applications in the improvement of hydrolysis of cellulosic compounds into fermentable sugars that can be used in energy generation and biofuel production.http://dx.doi.org/10.1155/2016/3978124
spellingShingle Folasade M. Olajuyigbe
Chidinma M. Nlekerem
Olusola A. Ogunyewo
Production and Characterization of Highly Thermostable β-Glucosidase during the Biodegradation of Methyl Cellulose by Fusarium oxysporum
Biochemistry Research International
title Production and Characterization of Highly Thermostable β-Glucosidase during the Biodegradation of Methyl Cellulose by Fusarium oxysporum
title_full Production and Characterization of Highly Thermostable β-Glucosidase during the Biodegradation of Methyl Cellulose by Fusarium oxysporum
title_fullStr Production and Characterization of Highly Thermostable β-Glucosidase during the Biodegradation of Methyl Cellulose by Fusarium oxysporum
title_full_unstemmed Production and Characterization of Highly Thermostable β-Glucosidase during the Biodegradation of Methyl Cellulose by Fusarium oxysporum
title_short Production and Characterization of Highly Thermostable β-Glucosidase during the Biodegradation of Methyl Cellulose by Fusarium oxysporum
title_sort production and characterization of highly thermostable β glucosidase during the biodegradation of methyl cellulose by fusarium oxysporum
url http://dx.doi.org/10.1155/2016/3978124
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