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Comparative Studies of White-Rot Fungal Strains (Trametes hirsuta MTCC-1171 and Phanerochaete chrysosporium NCIM-1106) for Effective Degradation and Bioconversion of Ferulic Acid.

ABSTRACT: Biodegradation of ferulic acid, by two white-rot fungal strains (Trametes hirsuta MTCC-1171 and Phanerochaete chrysosporium NCIM-1106) was investigated in this study. Both strains could use ferulic acid as a sole carbon source when provided with basal mineral salt medium. T. hirsuta achieved complete degradation of ferulic acid (350 mg L-1) in 20 h, whereas P. chrysosporium degraded it (250 mg L-1) in 28 h. The metabolites produced during degradation were distinguished by gas chromatography-mass spectrometry. Bioconversion of ferulic acid to vanillin by P. chrysosporium was also investigated. The optimum experimental conditions for bioconversion to vanillin can be summarized as follows: ferulic acid concentration 250 mg L-1, temperature 35 °C, initial pH 5.0, mycelial inoculum 0.32 ± 0.01 g L-1 dry weight, and shaking speed 150 rpm. At optimized conditions, the maximum molar yield obtained was 3.4 ± 0.1%, after 20 h of bioconversion. Considering that the degradation of ferulic acid was determined by laccase and lignin peroxidase to some extent, the possible role of ligninolytic enzymes in overall bioconversion process was also studied. These results illustrate that both strains have the potential of utilizing ferulic acid as a sole carbon source. Moreover, P. chrysosporium can also be explored for its ability to transform ferulic acid into value-added products.

SUBMITTER: Patil PD

PROVIDER: S-EPMC6289575 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature

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Comparative Studies of White-Rot Fungal Strains (Trametes hirsuta MTCC-1171 and Phanerochaete chrysosporium NCIM-1106) for Effective Degradation and Bioconversion of Ferulic Acid.

Patil Pravin D PD Yadav Ganapati D GD

ACS omega 20181105 11

Biodegradation of ferulic acid, by two white-rot fungal strains (Trametes hirsuta MTCC-1171 and Phanerochaete chrysosporium NCIM-1106) was investigated in this study. Both strains could use ferulic acid as a sole carbon source when provided with basal mineral salt medium. T. hirsuta achieved complete degradation of ferulic acid (350 mg L-1) in 20 h, whereas P. chrysosporium degraded it (250 mg L-1) in 28 h. The metabolites produced during degrada ...[more]

PMID: 30555994

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Project description:BackgroundCellobiose dehydrogenase from Phanerochaete chrysosporium (PcCDH) is a key enzyme in lignocellulose depolymerization, biosensors and biofuel cells. For these applications, it should retain important molecular and catalytic properties when recombinantly expressed. While homologous expression is time-consuming and the prokaryote Escherichia coli is not suitable for expression of the two-domain flavocytochrome, the yeast Pichia pastoris is hyperglycosylating the enzyme. Fungal expression hosts like Aspergillus niger and Trichoderma reesei were successfully used to express CDH from the ascomycete Corynascus thermophilus. This study describes the expression of basidiomycetes PcCDH in T. reesei (PcCDHTr) and the detailed comparison of its molecular, catalytic and electrochemical properties in comparison with PcCDH expressed by P. chrysosporium and P. pastoris (PcCDHPp).ResultsPcCDHTr was recombinantly produced with a yield of 600 U L-1 after 4 days, which is fast compared to the secretion of the enzyme by P. chrysosporium. PcCDHTr and PcCDH were purified to homogeneity by two chromatographic steps. Both enzymes were comparatively characterized in terms of molecular and catalytic properties. The pH optima for electron acceptors are identical for PcCDHTr and PcCDH. The determined FAD cofactor occupancy of 70% for PcCDHTr is higher than for other recombinantly produced CDHs and its catalytic constants are in good accordance with those of PcCDH. Mass spectrometry showed high mannose-type N-glycans on PcCDH, but only single N-acetyl-D-glucosamine additions at the six potential N-glycosylation sites of PcCDHTr, which indicates the presence of an endo-N-acetyl-β-D-glucosaminidase in the supernatant.ConclusionsHeterologous production of PcCDHTr is faster and the yield higher than secretion by P. chrysosporium. It also does not need a cellulose-based medium that impedes efficient production and purification of CDH by binding to the polysaccharide. The obtained high uniformity of PcCDHTr glycoforms will be very useful to investigate electron transfer characteristics in biosensors and biofuel cells, which are depending on the spatial restrictions inflicted by high-mannose N-glycan trees. The determined catalytic and electrochemical properties of PcCDHTr are very similar to those of PcCDH and the FAD cofactor occupancy is good, which advocates T. reesei as expression host for engineered PcCDH for biosensors and biofuel cells.

Project description:The ability of white-rot fungi to degrade polysaccharides in lignified plant cell walls makes them a suitable reservoir for CAZyme prospects. However, to date, CAZymes from these species are barely studied, which limits their use in the set of choices for biomass conversion in modern biorefineries. The current work joined secretome studies of two representative white-rot fungi, Phanerochaete chrysosporium and Trametes versicolor, with expression analysis of cellobiohydrolase (CBH) genes, and use of the secretomes to evaluate enzymatic conversion of simple and complex sugarcane-derived substrates. Avicel was used to induce secretion of high levels of CBHs in the extracellular medium. A total of 56 and 58 proteins were identified in cultures of P. chrysosporium and T. versicolor, respectively, with 78-86% of these proteins corresponding to plant cell wall degrading enzymes (cellulolytic, hemicellulolytic, pectinolytic, esterase, and auxiliary activity). CBHI predominated among the plant cell wall degrading enzymes, corresponding to 47 and 34% of the detected proteins in P. chrysosporium and T. versicolor, respectively, which confirms that Avicel is an efficient CBH inducer in white-rot fungi. The induction by Avicel of genes encoding CBHs (cel) was supported by high expression levels of cel7D and cel7C in P. chrysosporium and T. versicolor, respectively. Both white-rot fungi secretomes enabled hydrolysis experiments at 10 FPU/g substrate, despite the varied proportions of CBHs and other enzymes present in each case. When low recalcitrance sugarcane pith was used as a substrate, P. chrysosporium and T. versicolor secretomes performed similarly to Cellic® CTec2. However, the white-rot fungi secretomes were less efficient than Cellic® CTec2 during hydrolysis of more recalcitrant substrates, such as acid or alkaline sulfite-pretreated sugarcane bagasse, likely because Cellic® CTec2 contains an excess of CBHs compared with the white-rot fungi secretomes. General comparison of the white-rot fungi secretomes highlighted T. versicolor enzymes for providing high glucan conversions, even at lower proportion of CBHs, probably because the other enzymes present in this secretome and CBHs lacking carbohydrate-binding modules compensate for problems associated with unproductive binding to lignin.

Dataset Information

Comparative Studies of White-Rot Fungal Strains (Trametes hirsuta MTCC-1171 and Phanerochaete chrysosporium NCIM-1106) for Effective Degradation and Bioconversion of Ferulic Acid.

Publications

Comparative Studies of White-Rot Fungal Strains (<i>Trametes hirsuta</i> MTCC-1171 and <i>Phanerochaete chrysosporium</i> NCIM-1106) for Effective Degradation and Bioconversion of Ferulic Acid.

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