Mushroom Ligninolytic Enzymes―Features and Application of Potential Enzymes for Conversion of Lignin into Bio-Based Chemicals and Materials

Abstract

Mushroom ligninolytic enzymes are attractive biocatalysts that can degrade lignin through oxido-reduction. Laccase, lignin peroxidase, manganese peroxidase, and versatile peroxidase are the main enzymes that depolymerize highly complex lignin structures containing aromatic or aliphatic moieties and oxidize the subunits of monolignol associated with oxidizing agents. Among these enzymes, mushroom laccases are secreted glycoproteins, belonging to a polyphenol oxidase family, which have a powerful oxidizing capability that catalyzes the modification of lignin using synthetic or natural mediators by radical mechanisms via lignin bond cleavage. The high redox potential laccase within mediators can catalyze the oxidation of a wide range of substrates and the polymerization of lignin derivatives for value-added chemicals and materials. The chemoenzymatic process using mushroom laccases has been applied effectively for lignin utilization and the degradation of recalcitrant chemicals as an eco-friendly technology. Laccase-mediated grafting has also been employed to modify lignin and other polymers to obtain novel functional groups able to conjugate small and macro-biomolecules. In this review, the biochemical features of mushroom ligninolytic enzymes and their potential applications in catalytic reactions involving lignin and its derivatives to obtain value-added chemicals and novel materials in lignin valorization are discussed.

Application of Deconica castanella ligninolytic enzymatic system in the degradation of hexachlorobenzene in soil

“…Furthermore, the degradation of organochlorides can be achieved by the synergistic action of enzymes and prooxidants, which are produced by the basidiomycetes, such as superoxide anion (O 2 − ), H 2 O 2 , hydroxyl radicals (-OH), and singlet oxygen ( 1 O 2 ). 27 The presence of HCB promoted the production of laccase isoforms by D. castanella with optimal pH and inhibition pattern typical of basidiomycetes, being the decrease in activity in presence of H 2 O 2 suggestive of absence of peroxidases in the brute extracts. 27,51,52 However, higher optimal temperatures were observed for D. castanella laccase when compared with the laccases produced by other basidiomycetes (55-60 • C), as well as higher thermostability, 52 thereby suggesting the applicability of this species and its enzymatic arsenal in the degradation of POP.…”

“…27 The presence of HCB promoted the production of laccase isoforms by D. castanella with optimal pH and inhibition pattern typical of basidiomycetes, being the decrease in activity in presence of H 2 O 2 suggestive of absence of peroxidases in the brute extracts. 27,51,52 However, higher optimal temperatures were observed for D. castanella laccase when compared with the laccases produced by other basidiomycetes (55-60 • C), as well as higher thermostability, 52 thereby suggesting the applicability of this species and its enzymatic arsenal in the degradation of POP. 33 Furthermore, these findings were also corroborated by other authors who observed the production of fungal laccases…”

Inhibitory Potential of New Phenolic Hydrazide-Hydrazones with a Decoy Substrate Fragment towards Laccase from a Phytopathogenic Fungus: SAR and Molecular Docking Studies

“…The general procedure starting from 3-phenyl-salicylic aldehyde (6) (149 mg, 0.75 mmol) [108], 2-hydroxybenzohydrazide (16) (114 mg, 0.75 mmol), CH 3 OH (30 mL), and AcOH (75 µL) was employed with a 3.5 h reaction time and crystallization with concentration to obtain a white solid the 2-hydroxy-N -[(E)-(2-hydroxy-3-phenyl-phenyl)methylidene] benzohydrazide (4m) (206 mg, 0.62 mmol) with 83% yield, which melts in 224-227 J = 7.9 Hz, 4 J = 1.6 Hz, 1H, H-6), 7.61 (dd, 3 J = 8.1 Hz, 4 J = 1.2 Hz, 2H, PhH-2,6), 7.48 (dd, 3 J = 7.6 Hz, 4 J = 1.5 Hz, 1H, ArH-6), 7.47 (ddd, 3 J = 8.3 Hz, 3 J = 7.2 Hz, 4 J = 1.6 Hz, 1H, H-4), 7.45 (ddd, 3 J = 8.1 Hz, 3 J = 7.4 Hz, 2H, PhH-3,5), 7.41 (dd, 3 J = 7.5 Hz, 4 J = 1.5 Hz, 1H, ArH-4), 7.36 (tt, 3 J = 7.4 Hz, 4 J = 1.2 Hz, 1H, PhH-4), 7.06 (dd, 3 J = 7.6 Hz, 3 J = 7.5 Hz, 1H, ArH-5), 7.01 (dd, 3 J = 8.3 Hz, 4 J = 1.0 Hz, 1H, H-3), 6.98 (ddd, 3 J = 7.9 Hz, 3 J = 7.2 Hz, 4 J = 1.0 Hz, 1H, H-5) ppm; 13 (dd, 3 J = 7.9 Hz, 3 J =7.3 Hz, 2H, PhH-3.5), 7.40 (dd, 3 J = 7.6 Hz, 4 J = 1.4 Hz, 1H, ArH-4), 7.37 (t, 3 J = 7.9 Hz, 1H, PhH-4), 7.32-7.37 (m, 3H, H-2, H-5, H-6), 7.04 (dd, 3 J = 7.6 Hz, 3 J = 7.6 Hz, 1H, ArH-5), 7.02 (ddd, 3 J = 7.8 Hz, 4 J = 2.3 Hz, 4 J = 1.2 Hz, 1H, H-4) ppm; 13 The general procedure starting from 3-tert-butyl-5-methyl-salicylic aldehyde (8) (192 mg, 1.0 mmol) [108], 1-hydroxy-2-naphthohydrazide (19) (202 mg, 1.0 mmol) [109], CH 3 OH (65 mL), and AcOH (100 µL) was employed with a 6 h reaction time and concentrated by slow distillation before crystallization to obtain the colorless prisms of N -[(E)-(3-tert-butyl-2-hydroxy-5-methylphenyl)methylidene]-2-(1-hydroxynaphtho)hydrazide (5a) (345 mg, 0.916 mmol) with 92% yield, which melts at 215-217 3 J = 8.9 Hz, 1H, H-3), 7.92 (d, 3 J = 8.1 Hz, 1H, H-5), 7.69 (ddd, 3 J = 6.8 Hz, 3 J = 6.8 Hz, 4 J = 1.2 Hz, 1H, H-6), 7.62 (d, 3 J = 7.7 Hz, 2H, PhH-2,6), 7.60 (ddd, 3 J = 8.2 Hz, 3 J = 6.8 Hz, 4 J = 1.1 Hz, 1H, H-7), 7.53 (dd, 3 J = 7.7 Hz, 4 J = 1.4 Hz, 1H, ArH-6), 7.49 (d, 3 J = 8.9 Hz, H-4), 7.46 (dd, 3 J = 7.7 Hz, 3 J = 7.3 Hz, 2H, PhH-3,5), 7.43 (dd, 3 J = 7.5 Hz, 4 J = 1.4 Hz, 1H, ArH-4), 7.36 (t, 3 J = 7.3 Hz, 1H, PhH-4), 7.07 (t, 3 J = 7.7 Hz, 3 J = 7.5 Hz, 1H, ArH-5) ppm; 13 The general procedure starting from 3,5-di-tert-butyl-salicylic aldehyde (9) (234 mg, 1.0 mmol) [108], 1-hydroxy-2-naphthohydrazide (19) (202 mg, 1.0 mmol) [109], CH 3 OH (75 mL), and AcOH (100 µL) was employed with a 2 h reaction time, decolorization with charcoal and concentration slow by distillation before crystallization to obtain N -[(E)-…”

“…It has the exceptional ability to one electron oxidize both low-and high-molecular-weight substrates via direct or mediated reactions applied in green chemistry [1]. This nonspecific property has been reflected in numerous industrial, medical, and environmental applications [2][3][4][5]. Prokaryotes [6] and eukaryotes such as insects [7], plants, and fungi [8] produce laccase.…”

“…(3,5-di-tert-butyl-2-hydroxy-phenyl)methylidene]-2-(1-hydroksynaphtho)hydrazide (5c) (397 mg, 0.881 mmol) as yellow needles with 88% yield crystallized with one molecule of methyl alcohol, which melts at 122-123• C. Selected FT-IR (ATR): ν max 3650 (CH 3 OH), 3392 (O-H), 3322 (N-H), 3060 (C Ar -H), 1611 (C=O), 1596 (C=C), 1584 (N-H), 1563 (C=N), 1531, 1467, 1390, 1356, 1278, 1250 (C Ar -O), 1207 (C Ar -O), 1173, 1027, 815, 759, 709, 535, 494, 419 cm −1 ; 1 H NMR (400 MHz, DMSO-d 6 ): δ 13.85 (s, 1H, O-H), 12.50 (s, 1H, NHCO), 12.24 (s, 1H, O-H), 8.70 (s, 1H, CH=N), 8.32 (d, 3 J = 8.2 Hz, 1H, H-8), 7.98 (d, 3 J = 8.8 Hz, 1H, H-3), 7.92 (d,3 J = 8.0 Hz, 1H, H-5), 7.69 (dd, 3 J = 8.0 Hz, 3 J = 7.2 Hz, 1H, H-6), 7.60 (dd, 3 J = 8.2 Hz, 3 J = 7.2 Hz, 1H, H-7), 7.50 (d, 3 J = 8.8 Hz, 1H, H-4), 7.35 (d, 4 J = 2.0 Hz, 1H, ArH-4), 7.28 (d, 4 J = 2.0 Hz, 1H, ArH-6), 4.10 (s, 1H, CH 3 OH), 3.17 (s, 3H, CH 3 OH), 1.43 (s, 9H, Ar-3t-Bu), 1.30 (s, 9H, Ar-5-t-Bu) ppm;13 C NMR (100 MHz, DMSO-d 6 ): δ 166.59 (C), 160.14 (C=O), 154.83 (C), 152.72 (CH=N), 140.52 (C), 135.97 (C), 135.73 (C), 129.34 (CH), 127.51 (CH), 126.08 (CH), 126.01 (CH), 125.97 (CH), 124.53 (C), 123.04 (CH), 122.25 (CH), 118.06 (CH), 116.78 (C), 105.79 (C), 48.52 (CH 3 OH), 34.62 (C), 33.85 (C), 31.22 (3 × CH 3 -t-Bu), 29.23 (3 × CH 3 -t-Bu) ppm; HRMS (TOF, MS, ESI) m/z for C 26 H 30 N 2 O 3 + Na + : calculated 441.2149; found: 441.2152.…”