Phenolic mediators enhance the manganese peroxidase catalyzed oxidation of recalcitrant lignin model compounds and synthetic lignin

Nousiainen, Paula; Kontro, Jussi; Manner, Helmiina; Hatakka, Annele; Sipilä, Jussi

doi:10.1016/j.fgb.2014.07.008

Cited by 67 publications

(27 citation statements)

References 70 publications

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“…However, only small part of aromatic structures of lignin comprised of phenolic hydroxyl groups. The abundant nonphenolic substructures of lignin are not susceptible to the attack by chelated Mn 3+ ion [ 15 , 48 ]. Moreover, undistinguished role of MnP in lignin degradation was also published in study [ 49 ].…”

Section: Resultsmentioning

confidence: 99%

Production of Monomeric Aromatic Compounds from Oil Palm Empty Fruit Bunch Fiber Lignin by Chemical and Enzymatic Methods

Tang

Hassan

Maskat

et al. 2015

BioMed Research International

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In this study, oil palm empty fruit bunch (OPEFBF) was pretreated with alkali, and lignin was extracted for further degradation into lower molecular weight phenolic compounds using enzymes and chemical means. Efficiency of monomeric aromatic compounds production from OPEFBF lignin via chemical (nitrobenzene versus oxygen) and enzymatic [cutinase versus manganese peroxidase (MnP)] approaches was investigated. The effects of sodium hydroxide concentration (2, 5, and 10% wt.) and reaction time (30, 90, and 180 minutes) on the yield of aromatic compounds were studied. The results obtained indicated that nitrobenzene oxidation produced the highest yield (333.17 ± 49.44 ppm hydroxybenzoic acid, 5.67 ± 0.25 ppm p-hydroxybenzaldehyde, 25.57 ± 1.64 ppm vanillic acid, 168.68 ± 23.23 ppm vanillin, 75.44 ± 6.71 ppm syringic acid, 815.26 ± 41.77 ppm syringaldehyde, 15.21 ± 2.19 ppm p-coumaric acid, and 44.75 ± 3.40 ppm ferulic acid), among the tested methods. High sodium hydroxide concentration (10% wt.) was needed to promote efficient nitrobenzene oxidation. However, less severe oxidation condition was preferred to preserve the hydroxycinnamic acids (p-coumaric acid and ferulic acid). Cutinase-catalyzed hydrolysis was found to be more efficient than MnP-catalyzed oxidation in the production of aromatic compounds. By hydrolyzed 8% wt. of lignin with 0.625 mL cutinase g−1 lignin at pH 8 and 55°C for 24 hours, about 642.83 ± 14.45 ppm hydroxybenzoic acid, 70.19 ± 3.31 ppm syringaldehyde, 22.80 ± 1.04 ppm vanillin, 27.06 ± 1.20 ppm p-coumaric acid, and 50.19 ± 2.23 ppm ferulic acid were produced.

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Section: Resultsmentioning

confidence: 99%

Production of Monomeric Aromatic Compounds from Oil Palm Empty Fruit Bunch Fiber Lignin by Chemical and Enzymatic Methods

Tang

Hassan

Maskat

et al. 2015

BioMed Research International

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“…After the crude enzyme was obtained, the activity of lignin peroxidase was analyzed. Veratril alcohol serves as a mediator in redox reactions to stabilize the LiP-oxidation of lignocellulosic organic substrates (Nousiainen et al, 2014;Asgher et al, 2011). Indirectly, the difference in the value of the resulting LiP enzyme activity depends on the ability of the fungus to adapt to its constituent substrate and factors such as the biological, physical or chemical factors possessed by the enzyme.…”

Section: Enzyme Activitymentioning

confidence: 99%

Ligninolitic Enzyme Immobilization from Pleurotus ostreatus for Dye and Batik Wastewater Decolorization

Dewi

Ilyas

Sari

2019

JPII

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Batik wastewater is one of the environmental problems which has become a significant water pollution problem recently. It contains a large variety of synthetic dyes, chemicals, and has high chemical oxygen demand (COD). Synthetic dyes are difficult to degrade and have recalcitrant and toxic characteristics. Dyes can be degraded by ligninolytic enzymes, including laccase (Lac), manganese peroxidase (MnP), and lignin peroxidase (LiP). The immobilized ligninolytic enzyme is effectively used to enhance the degradation of the dye wastewater. Pleurotus ostreatus, the most abundant ligninolytic enzyme source, is the candidate to regenerate fungal biomass as the bioremediation agent. Immobilization of ligninolytic enzyme using alginate was observed in this study for its efficiency to decolorize and decrease COD concentration of RBBR dye and Naphtol batik wastewater in different time periods (0, 2, 4, 6, 24, 48, 72 h) and growth conditions (static and agitated). The results show that the Lac, MnP, LnP activities of P. ostreatus are 200.43, 9.714, 12938.60 U/l, respectively. Static conditions within 48 hours exhibit the highest percentage of decolorization of dye. Ligninolytic immobilized from its condition has decolorized RBBR dye up to 75.88%, while the percentage of decolorization of agitated culture is 68.09%. This ligninolytic immobilized has decolorized about 94.867% of batik wastewater within 24 hours under a static condition. It is also able to decrease the COD level of the batik wastewater containing Naphtol dye (504 to 233 mg/l) within 24 hours under a shaking condition. Immobilization of enzyme has been a promising alternative for decolorization of dye and batik wastewater.

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“…The improved MnP production is important for assisting to create environmentally sound biomass degradation alternatives and diminish the cost of energy and used chemicals in biofuel production industries. MnP has many applications in industrial processes like bio-pulping, bio-bleaching and biodegradation/bioremediation of pollutants [3,4,[19][20][21].…”

Section: Manganese Peroxidase: An Introductionmentioning

confidence: 99%

“…Further, chelated Mn 3+ ions generated by MnP act as S-S charge transfer mediators, allowing the oxidation of various phenolic substrates like simple phenols, amines, phenolic lignin and several dyes ( Fig. 1) [10,21].…”

Section: Manganese Peroxidase: An Introductionmentioning

confidence: 99%

Microbial manganese peroxidase: a ligninolytic enzyme and its ample opportunities in research

et al. 2018

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Microbial ligninolytic enzymes like laccase, manganese peroxidase, and lignin peroxidase have gained much attention in many industrial applications. Among these, manganese peroxidases are key contributors in the microbial ligninolytic system. It mainly oxidizes Mn(II) ions that remain present in wood and soils, into more reactive Mn 3+ form, stabilized by fungal chelators like oxalic acids. However, Mn 3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily. It has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries. This review article is focused on the sources, catalytic reaction mechanisms and different biotechnological applications. However, manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes. In addition, microbial MnPs can also convert lignin into biomass so that the sugar can be converted into bio-fuels. Thus, this review article is mainly focused and highlighted the current scenario and updated information on manganese peroxidase enzyme.

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Phenolic mediators enhance the manganese peroxidase catalyzed oxidation of recalcitrant lignin model compounds and synthetic lignin

Cited by 67 publications

References 70 publications

Production of Monomeric Aromatic Compounds from Oil Palm Empty Fruit Bunch Fiber Lignin by Chemical and Enzymatic Methods

Production of Monomeric Aromatic Compounds from Oil Palm Empty Fruit Bunch Fiber Lignin by Chemical and Enzymatic Methods

Ligninolitic Enzyme Immobilization from Pleurotus ostreatus for Dye and Batik Wastewater Decolorization

Microbial manganese peroxidase: a ligninolytic enzyme and its ample opportunities in research

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