Inhibitor formation and detoxification during lignocellulose biorefinery: A review.

Enzymes and enzymatic mechanisms in enzymatic degradation of lignocellulosic biomass: A mini-review.

Reviewing the contributions of macrofungi to forest ecosystem processes and services

Microbial manganese peroxidases (MnPs) are ligninolytic enzymes primarily responsible for degrading lignin, but they are also capable of degrading dyes, organic pollutants, and emerging contaminants in wastewater. They have been isolated and characterized from many white-rot fungi and few bacteria. For microbial MnPs, the optimum pH range is between 3.5 and 9.0; the optimum temperature range is between 25°C and 70°C. Their molecular weights range between 25 kDa and 68 kDa. By oxidizing Mn2+ to Mn3+, they can oxidize a wide range of phenolic and non-phenolic substrates. MnPs can be used in a wide range of industrial applications, including delignification of pulp, wastewater treatment, biofuel production, dye removal, biopulping, biobleaching, and juice extract clarification. The purpose of this review is to summarize biotechnological applications of manganese peroxidases.

https://www.frontiersin.org/articles/10.3389/fenvs.2022.875157/pdf

Biotechnological Applications of Manganese Peroxidases for Sustainable Management

Two laccase isoenzymes (LacA and LacB) were isolated from a novel Trichoderma harzianum S7113 isolate employing ammonium sulfate precipitation, Sephadex G100, and DEAE Sepharose ion exchange chromatography. The molecular weights of the purified LacA and LacB laccases were estimated to be 63 and 48 kDa, respectively. The two isoenzymes had their optimum activities at the same temperature (50 °C), but at slightly different pH values (pH 3.0 for LacA and pH 2.5 for LacB). LacA and LacB had the same thermal stability at 40 °C and pH stability at pH 9.0. The two isoenzymes also showed a high level of specific activity toward ABTS, where the Km values of LacA and LacB were 0.100 and 0.065 mM, whereas their Vmax values were 0.603 and 0.182 µmol min-1, respectively. LacA and LacB catalytic activity was stimulated by Mg2+, Zn2+, K+, and Ni2+, whereas it was inhibited by Hg2+ and Pb2+, β-mercaptoethanol, EDTA, and SDS, and completely inhibited by sodium azide. Our findings indicate that purified laccase has a promising capacity for bisphenol A (BPA) bioremediation across a broad pH range. This finding opens up new opportunities for the commercialization of this technique in a variety of biotechnology-based applications, particularly for removing endocrine chemicals from the environment. 

/pdf/purification-and-biochemical-characterization-of-two-laccase-q81uo3tk.pdf

Purification and biochemical characterization of two laccase isoenzymes isolated from Trichoderma harzianum S7113 and its application for bisphenol A degradation

http://www.cell.com/article/S2405844022001530/pdf

Biodelignification of lignocellulose using ligninolytic enzymes from white-rot fungi

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Biodelignification of lignocellulose using ligninolytic enzymes from white-rot fungi