Purification and characterization of yellow laccase from Trametes hirsuta MTCC-1171 and its application in synthesis of aromatic aldehydes

Optimization of different culture conditions for enhanced laccase production and its purification from Tricholoma giganteum AGHP

“…The enzyme was further purified by DEAE Sephadex A-50 ion exchange column chromatography with a specific activity of 3.49 × 10 5 U/mg and a final yield of 8.50 % with 10.80-fold purification. The purification of laccase obtained in the present study is comparable with Chaurasia et al (2014) who reported purification (10.42-fold) with 12.57 % yield of laccase from Trametes hirsuta MTCC-1171 using DEAE cellulose column chromatography. However, Yan et al (2014) reported 1.37-and 4.07-fold purification with 5.78 and 11.64 % yield of laccase from T. trogii S0301 using anionic exchange chromatography followed by Sephadex G-75 chromatography, respectively.…”

Study on improving the stability of adsorption-encapsulation immobilized Laccase@ZIF-67

“…Enzymes are thermosensitive and may irreversibly lose their catalytic activity at elevated temperature due to permanent conformational alteration occurring in structure [ 53 ]. Since there was no significant change in laccase activity from room temperature to 40 ℃, we determined the relative enzyme activity change at 40–80 ℃ ( Fig.…”

Insights into laccase producing organisms, fermentation states, purification strategies, and biotechnological applications

“…The structure of yellow laccase is similar to that of the blue laccase (four copper atoms), but the characteristic peak at 610 nm is missing. Trametes hirsuta MTCC‐1171 secretes a yellow laccase that lacks the 610 nm peak . Yellow laccases (e.g., the purified laccases from Panus tigrinus and Pleurotus ostreatus D1) oxidize nonphenolic aromatic compounds in the absence of mediators .…”

“…Trametes hirsuta MTCC-1171 secretes a yellow laccase that lacks the 610 nm peak. 27 Yellow laccases (e.g., the purified laccases from Panus tigrinus and Pleurotus ostreatus D1) oxidize nonphenolic aromatic compounds in the absence of mediators. 12,28 Other yellow laccase producers include the phytopathogenic ascomycete Gaeumannomyces graminis and the basidiomycetes Agaricus bisporus D621, Schizophyllum commune, Phlebia radiata, 27 and Phellinus ribis.…”

“…29 Recently, Mot et al 30 described the properties of an atypical laccase from Sclerotinia sclerotiorum that showed characteristics of blue (presence of the specific feature of the T1 center in the EPR spectrum) and yellow (absence of the 610 nm peak in ultraviolet (UV)/vis spectrum) laccases. Chaurasia et al 27 reported that the binding of aromatic compounds (obtained from lignin degradation) to the blue laccases led to the formation of yellow laccases during fungal growth in solid-state conditions. In contrast to yellow and blue laccases, white laccases contain only one copper atom, and additional metal ions, such as zinc, iron, or manganese, are present at the active site.…”