Production, partial purification and characterization of ligninolytic enzymes from selected basidiomycetes mushroom fungi

Abstract

In recent years, many research on the quantity of lignocellulosic waste have been developed. The production, partial purification, and characterisation of ligninolytic enzymes from various fungi are described in this work. On the 21st day of incubation in Potato Dextrose (PD) broth, Hypsizygus ulmarius developed the most laccase (14.83 × 10 −6 IU/ml) and manganese peroxidase (24.11 × 10 −6 IU/ml), while Pleurotus florida produced the most lignin peroxidase (19.56 × −6 IU/ml). Laccase (Lac), lignin peroxidase (LiP), and manganese peroxidase (MnP), all generated by selected basidiomycetes mushroom fungi, were largely isolated using ammonium sulphate precipitation followed by dialysis. Laccase, lignin peroxidase, and manganese peroxidase purification findings indicated 1.83, 2.13, and 1.77 fold purity enhancements, respectively. Specific activity of purified laccase enzyme preparations ranged from 305.80 to 376.85 IU/mg, purified lignin peroxidase from 258.51 to 336.95 IU/mg, and purified manganese peroxidase from 253.45 to 529.34 IU/mg. H. ulmarius laccase (376.85 IU/mg) with 1.83 fold purification had the highest specific activity of all the ligninolytic enzymes studied, followed by 2.13 fold purification in lignin peroxidase (350.57 IU/mg) and manganese peroxidase (529.34 IU/mg) with 1.77-fold purification. Three notable bands with molecular weights ranging from 43 to 68 kDa and a single prominent band with a molecular weight of 97.4 kDa were identified on a Native PAGE gel from mycelial proteins of selected mushroom fungus. The SDS PAGE profiles of the mycelial proteins from the selected mushroom fungus were similar to the native PAGE. All three partially purified ligninolytic isozymes display three bands in native gel electrophoresis, with only one prominent band in enzyme activity staining. The 43 kDa, 55 kDa, and 68 kDa protein bands correspond to laccase, lignin peroxidase, and manganese peroxidase, respectively.

Fungal Proteases as Emerging Biocatalysts to Meet the Current Challenges and Recent Developments in Biomedical Therapies: An Updated Review

“…Novel acid protease was produced from A. oryzae FG76 from a culturing medium with 17-activity and showed high stability as compared to commercial enzymes [28]. Another novel protease was purified from basidiomycete fungus CTM10057 that acted as a potential candidate for industrial applications, especially in the detergent and laundry industries [150,151]. Pseudomonas aeruginosa CTM50182 secreted the AMPP protease with 70% activity that showed high stability as compared to commercial enzymes [28,152].…”

Olive and green tea leaves extract in Pleurotus ostreatus var. florida culture media: Effect on mycelial linear growth rate, diameter and growth induction index

“…IOP Publishing doi:10.1088/1755-1315/1090/1/012020 10 [21]; which means the colonization of 85 mm in around 14 days. The role of olive extract in the culture medium in increasing MGR to around 47.0-49.0 mm at day 4 was pointed out by [24].…”

Biodegradation of Turquoise Blue Textile Dye by Wood Degrading Local Fungi Isolated from Plantation Area

“…Fungi use extracellular enzymes to transform aromatic compounds, such as lignin, dyes, and polycyclic aromatic hydrocarbons into less toxic products [Yesilada et al, 2003]. Several strains of fungi have been reported to degrade the color of textile wastewater, including laccase enzymesproducing soil fungi of Aspergillus niger and Phanerochaete chrysosporium [Rani et (Illuri et al, 2021). The fungi from the Basidiomycetes class can degrade various dye structures, such as anthraquinone, triphenylmethane, and azo dyes [Machado et al, 2005].…”