“…8,31,32 However, very often the production yield is low, and recombinant enzymes form aggregates difficult to purify. 33 On the other hand, recombinant production of Streptomyces coelicolor laccase (SLAC) in Streptomyces lividans has yielded considerable large amount of laccase (350 mg l -1 ) with high purity. 34 The laccase from the ligninolytic fungus Cyathus bulleri has been just recently expressed in E. coli making it the first fungal laccase to be expressed in a bacterial host.…”
“…8,31,32 However, very often the production yield is low, and recombinant enzymes form aggregates difficult to purify. 33 On the other hand, recombinant production of Streptomyces coelicolor laccase (SLAC) in Streptomyces lividans has yielded considerable large amount of laccase (350 mg l -1 ) with high purity. 34 The laccase from the ligninolytic fungus Cyathus bulleri has been just recently expressed in E. coli making it the first fungal laccase to be expressed in a bacterial host.…”
“…Escherichia coli [44,[89][90][91] but successful expression of fungal laccases in E. coli has not been reported.…”
Section: Subtilis Thermus Thermophilus and Streptomyces Lavendulae Hmentioning
confidence: 99%
“…Another potential environmental application for laccases is the bioremediation of contaminated soils, as laccases and LMS are able to oxidize toxic organic pollutants, such as various xenobiotics, PAHs, chlorophenols, and other contaminants [16,89,130,177,210,[218][219][220][221][222][223][224][225][226]. Phenolic compounds are present in wastes from several industrial processes, as coal conversion, petroleum refining, production of organic chemicals and olive oil production among others [227,228].…”
Abstract:Laccases are an interesting group of multi copper enzymes, which have received much attention of researchers in last decades due to their ability to oxidize both phenolic and non-phenolic lignin related compounds as well as highly recalcitrant environmental pollutants. This makes these biocatalysts very useful for their application in several biotechnological processes. Such applications include the detoxification of industrial effluents, mostly from the paper and pulp, textile and petrochemical industries, polymer synthesis, bioremediation of contaminated soils, wine and beverage stabilization. Laccases are also used as catalysts for the manufacture of anti-cancer drugs and even as ingredients in cosmetics. Recently, the utility of laccases has also been applied to nanobiotechnology. This paper reviews recent and important patents related to the properties, heterologous production, molecular cloning, and applications of laccases within different industrial fields as well as their potential extension to the nanobiotechnology area.
“…This was well supported with laccase produced from Ganoderma sp. MK05 which was purified at 70% saturation and attained 3.07 fold purification (Khammuang and Sarnthima, 2009), S. lavendulae laccase (Suzuki et al, 2003) purified at 50% saturation showed 9 fold increase in activity. Also, laccase from S. psammoticus exhibited 4.3 fold purification with 60% saturation (Niladevi and Prema, 2007).…”
Laccases (benzenediol oxygen oxidoreductases, EC 1.10.3.2) are polyphenol oxidases (PPO) that catalyze the oxidation of various substituted phenolic compounds by using molecular oxygen as the electron acceptor. In the present study, Bacillus subtilis MTCC 2414 were employed for the production of laccase using guaiacol as a substrate under Submerged Fermentation (SmF) condition. Laccase was partially purified by salt precipitation method followed by dialysis. The synthetic dyes such as Orange 3R, Yellow GR and T-Blue were used for degradation studies using culture filtrate, free and immobilized laccases. The immobilized laccase obtained by entrapment method using sodium alginate was optimized and it exhibited maximum activity at pH 7 (321 U mLG 1 ) and temperature 35°C (317 U mLG 1 ). Similarly, free laccase was also optimized and the maximum activity was observed at pH 9 (309 U mLG 1 ) and temperature 35°C (339 U mLG 1 ). Surprisingly, Yellow GR dye was found to be highly degraded up to 81.72% by immobilized laccase when compared to free laccase (74.69% of T-Blue) and culture filtrate (72.16% of Orange 3R) respectively. The FTIR spectrum showed a spectrum peaks at 2110.12 c/m in control dye and degraded Yellow GR exposed peak at 3406.36 cmG 1 which represents C-N stretching of aromatic amine group in dyes. Therefore, high degradation ability of laccase from B. subtilis MTCC 2414 makes them attractive catalyst for biotechnological applications.
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