Ligninolytic enzymes from corncob cultures of <i>Phanerochaete chrysosporium</i> under semi‐solid‐state conditions

Couto, Susana Rodrı́guez; Longo, María A.; Cameselle, Claudio; Sanromán, Á.

doi:10.1002/abio.370190104

Cited by 22 publications

(4 citation statements)

References 23 publications

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“…The induction of peroxidase in organisms by lignin model compounds has been reported from a number of studies . However, there is dearth of information on the inductive effect of lignin model compounds on peroxidase production by bacteria.…”

Section: Resultsmentioning

confidence: 99%

Agrowastes utilization by Raoultella ornithinolytica for optimal extracellular peroxidase activity

Falade

Mabinya

Okoh

et al. 2018

Biotech and App Biochem

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The industrial applications and prospects of microbial peroxidase are on the upwards trend, thus necessitating the search for sources with high turnaround time. Actinobacterial species have been a major source of peroxidase for the obvious reasons of having robust metabolite expression capabilities. However, other bacteria species have been underexplored for peroxidase production, hence the motivation for the investigation into the peroxidase production potential of Raoultella ornithinolytica OKOH-1 (KX640917). The bacteria expressed optimum specific peroxidase activity of 16.48 ± 0.89 U mg −1 , which is higher than those previously reported. The optimal fermentation conditions were pH 5 (3.44 ± 0.64 U mL −1 ), incubation temperature of 35 • C (5.25 ± 0.00 U mL −1 ), and agitation speed of 150 rpm (9.45 ± 2.57 U mL −1 ), with guaiacol and ammonium chloride as the best inducer and nitrogen supplement, respectively. On valorization of agrowastes as a sole carbon source for the secretion of peroxidase, sawdust gave the best peroxidase yield (15.21 ± 2.48 U mg −1 ) under solid-state fermentation. Also, a nonperoxide-dependent enzyme activity, which suggests probable laccase activity, was observed. The ability of the bacteria to utilize agrowastes is highly economical and as well a suitable waste management strategy. Consequently, R. ornithinolytica OKOH-1 is a promising industrial strain with dexterity for enhanced peroxidase production.

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Section: Resultsmentioning

confidence: 99%

Agrowastes utilization by Raoultella ornithinolytica for optimal extracellular peroxidase activity

Falade

Mabinya

Okoh

et al. 2018

Biotech and App Biochem

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“…Although the report on the induction of peroxidases by lignin monomers in bacteria is limited, there are quite a number of studies on the inductive effect of lignin monomers on peroxidase production by ligninolytic organisms, predominantly, fungi [44][45][46]. In this study, the effect of supplementing the production medium with 1 mM of different lignin monomers (Guaiacol-GA, Veratryl alcohol-VALC, vanillin-VAN, vanillic acid-VA and ferullic acid-FA) on exoperoxidase production was assessed and the results are shown in Figure 2a.…”

Section: Determination Of Process Parameters For Optimal Exoperoxidasmentioning

confidence: 99%

Exoproduction and Molecular Characterization of Peroxidase from Ensifer adhaerens

et al. 2019

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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 Ensifer adhaerens 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−1 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−1) 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 Ensifer adhaerens 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.

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“…obtenidos son reportados por Risdianto et al (2012) y Rodriguez-Couto et al (1999),quienes para esta especie y bajo condiciones comparables de fermentación del residuo tusa de maíz registran la ausencia de lacasa[84],[85]. Sin embargo, este último autor encontró valores considerables de actividad enzimática al séptimo día de fermentación, cuando el medio fue suplementado con alcohol veratrílico, señalando que la producción de lacasa por Phanerochaete chrysosporium es dependiente de la presencia de ciertos inductores, los cuales no se evaluaron en esta etapa de la investigación.Por su parte, la especieTrametes pubescens presentó su mayor actividad enzimática promedio (3.3 U/gss) al séptimo día de fermentación.…”

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Optimization of enzyme immobilization on functionalized magnetic nanoparticles for laccase biocatalytic reactions

Fortes

Daniel‐da‐Silva

Xavier

et al. 2017

Chemical Engineering and Processing: Process Intensification

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Ligninolytic enzymes from corncob cultures of Phanerochaete chrysosporium under semi‐solid‐state conditions

Cited by 22 publications

References 23 publications

Agrowastes utilization by Raoultella ornithinolytica for optimal extracellular peroxidase activity

Agrowastes utilization by Raoultella ornithinolytica for optimal extracellular peroxidase activity

Exoproduction and Molecular Characterization of Peroxidase from Ensifer adhaerens

Optimization of enzyme immobilization on functionalized magnetic nanoparticles for laccase biocatalytic reactions

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