Exoproduction and Molecular Characterization of Peroxidase from <em>Ensifer adhaerens</em>

The increased industrial application potentials of peroxidase have led to high market demand, which has outweighed the commercially available peroxidases. Hence, the need for alternative and efficient peroxidase-producers is imperative. This study reported the process parameters for enhanced exopero...

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Main Authors: Ayodeji Falade, Atef Jaouani, Leonard Mabinya, Anthony Okoh, Uchechukwu Nwodo
Format: Article
Language:English
Published: MDPI AG 2019-08-01
Series:Applied Sciences
Subjects:
Online Access:https://www.mdpi.com/2076-3417/9/15/3121
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spelling doaj-22d12822c1f343419ffa6bd28dcfe4d72020-11-25T00:31:00ZengMDPI AGApplied Sciences2076-34172019-08-01915312110.3390/app9153121app9153121Exoproduction and Molecular Characterization of Peroxidase from <em>Ensifer adhaerens</em>Ayodeji Falade0Atef Jaouani1Leonard Mabinya2Anthony Okoh3Uchechukwu Nwodo4SAMRC Microbial Water Quality Monitoring Centre, University of Fort Hare, Private Bag X1314, Alice 5700, South AfricaLaboratory of Microorganisms and Active Biomolecules, Faculty of Sciences of Tunis, University of Tunis El Manar, Tunis 2092, TunisiaSAMRC Microbial Water Quality Monitoring Centre, University of Fort Hare, Private Bag X1314, Alice 5700, South AfricaSAMRC Microbial Water Quality Monitoring Centre, University of Fort Hare, Private Bag X1314, Alice 5700, South AfricaSAMRC Microbial Water Quality Monitoring Centre, University of Fort Hare, Private Bag X1314, Alice 5700, South AfricaThe increased industrial application potentials of peroxidase have led to high market demand, which has outweighed the commercially available peroxidases. Hence, the need for alternative and efficient peroxidase-producers is imperative. This study reported the process parameters for enhanced exoperoxidase production by <i>Ensifer adhaerens</i> NWODO-2 (accession number: KX640918) for the first time, and characterized the enzyme using molecular methods. Peroxidase production by the bacteria was optimal at 48 h, with specific productivity of 12.76 U mg<sup>−1</sup> at pH 7, 30 °C and 100 rpm in an alkali lignin fermentation medium supplemented with guaiacol as the most effective inducer and ammonium sulphate as the best inorganic nitrogen source. Upon assessment of some agricultural residues as sources of carbon for the enzyme production, sawdust gave the highest peroxidase productivity (37.50 U mg<sup>−1</sup>) under solid-state fermentation. A search of the polymerase chain reaction (PCR)-amplified peroxidase gene in UniProtKB using blastx showed 70.5% similarity to an uncharacterized protein in <i>Ensifer adhaerens</i> but phylogenetic analysis suggests that the gene may encode a catalase-peroxidase with an estimated molecular weight of approximately 31 kDa and isoelectric point of about 11. The nucleotide sequence of the detected gene was deposited in the GenBank under the accession number MF374336. In conclusion, the ability of the strain to utilize lignocellulosic materials for peroxidase production augurs well for biotechnological application as this would greatly reduce cost, which is a major challenge in industrial enzyme production.https://www.mdpi.com/2076-3417/9/15/3121catalase-peroxidasemicrobial enzymeperoxidasepolymerase chain reactionproteobacteria
collection DOAJ
language English
format Article
sources DOAJ
author Ayodeji Falade
Atef Jaouani
Leonard Mabinya
Anthony Okoh
Uchechukwu Nwodo
spellingShingle Ayodeji Falade
Atef Jaouani
Leonard Mabinya
Anthony Okoh
Uchechukwu Nwodo
Exoproduction and Molecular Characterization of Peroxidase from <em>Ensifer adhaerens</em>
Applied Sciences
catalase-peroxidase
microbial enzyme
peroxidase
polymerase chain reaction
proteobacteria
author_facet Ayodeji Falade
Atef Jaouani
Leonard Mabinya
Anthony Okoh
Uchechukwu Nwodo
author_sort Ayodeji Falade
title Exoproduction and Molecular Characterization of Peroxidase from <em>Ensifer adhaerens</em>
title_short Exoproduction and Molecular Characterization of Peroxidase from <em>Ensifer adhaerens</em>
title_full Exoproduction and Molecular Characterization of Peroxidase from <em>Ensifer adhaerens</em>
title_fullStr Exoproduction and Molecular Characterization of Peroxidase from <em>Ensifer adhaerens</em>
title_full_unstemmed Exoproduction and Molecular Characterization of Peroxidase from <em>Ensifer adhaerens</em>
title_sort exoproduction and molecular characterization of peroxidase from <em>ensifer adhaerens</em>
publisher MDPI AG
series Applied Sciences
issn 2076-3417
publishDate 2019-08-01
description The increased industrial application potentials of peroxidase have led to high market demand, which has outweighed the commercially available peroxidases. Hence, the need for alternative and efficient peroxidase-producers is imperative. This study reported the process parameters for enhanced exoperoxidase production by <i>Ensifer adhaerens</i> NWODO-2 (accession number: KX640918) for the first time, and characterized the enzyme using molecular methods. Peroxidase production by the bacteria was optimal at 48 h, with specific productivity of 12.76 U mg<sup>−1</sup> at pH 7, 30 °C and 100 rpm in an alkali lignin fermentation medium supplemented with guaiacol as the most effective inducer and ammonium sulphate as the best inorganic nitrogen source. Upon assessment of some agricultural residues as sources of carbon for the enzyme production, sawdust gave the highest peroxidase productivity (37.50 U mg<sup>−1</sup>) under solid-state fermentation. A search of the polymerase chain reaction (PCR)-amplified peroxidase gene in UniProtKB using blastx showed 70.5% similarity to an uncharacterized protein in <i>Ensifer adhaerens</i> but phylogenetic analysis suggests that the gene may encode a catalase-peroxidase with an estimated molecular weight of approximately 31 kDa and isoelectric point of about 11. The nucleotide sequence of the detected gene was deposited in the GenBank under the accession number MF374336. In conclusion, the ability of the strain to utilize lignocellulosic materials for peroxidase production augurs well for biotechnological application as this would greatly reduce cost, which is a major challenge in industrial enzyme production.
topic catalase-peroxidase
microbial enzyme
peroxidase
polymerase chain reaction
proteobacteria
url https://www.mdpi.com/2076-3417/9/15/3121
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