Pilot scale production of extracellular thermo‐alkali stable laccase from Pseudomonas sp. S2 using agro waste and its application in organophosphorous pesticides degradation

Abstract

Background Laccases are multicopper oxidases that are able to oxidize various aromatic or nonaromatic compounds owing to their multifarious applications. However, till now only a few bacterial laccases have been isolated and characterized. Hence there is an urgent need to study an extracellular thermo‐alkali stable laccase. Results In the present study, an extracellular thermo‐alkali stable laccase was produced from Pseudomonas sp. S2 in a 100 L bioreactor using agro waste (potato peel). Production was 17‐fold higher than in the control. The enzyme (S2LAC) was purified 12.16 ± 1.6‐fold to homogeneity with specific activity of 1089.70 ± 16.8 U mg−1 and molecular mass of 38 kDa. The temperature and pH for maximum enzyme activity were 80 °C and 9.0, respectively. The metal ions Na+, K+, Pb+2, Ca+2, Cu+2 and Co+2 enhanced enzyme activity. The purified enzyme showed maximum specificity to Pyrogallol > PPD > L‐DOPA > Hydroquinone. The S2LAC was able to degrade organ‐phosphorous pesticide including dichlorophos, chlorpyrifos, monocrotophos and profenovos upto 45.99 ± 0.3%, 80.56 ± 0.6%, 75.45 ± 1.3%, 81.84 ± 0.6%, respectively, in the absence of any mediator. Conclusion S2LAC produced using agro waste was stable and capable of degrading organophosphorous pesticides making it attractive for industrial applications. © 2017 Society of Chemical Industry

Extra and intracellular laccase titers of xylophagic bacteria isolated from adult termite

“…Besides, both the genera have been well-described as laccase producers. Several reports demonstrated the Bacillus (Lončar, Gligorijević, Božić, & Vujčić, 2014;Mishra & Srivastava, 2016) and Pseudomonas (Chauhan & Jha, 2018;Peter & Vandana, 2014) are producers of ligninolytic enzymes.…”

Enhanced Thermostability and Anticancer Activity in Breast Cancer Cells of Laccase Immobilized on Pluronic-Stabilized Nanoparticles

“…Enzyme immobilization can affect the protein tertiary structure and partly or completely change enzyme activity. Therefore, the activity of laccase after immobilization was studied by the 2,2′-azino-bis­(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) colorimetric assay where the substrate is oxidized by the immobilized enzyme and the development of green color is quantified by a UV–vis spectrophotometer at 420 nm. , …”

“…Laccases (benzenediol/oxygen oxidoreductases; EC 1.10.3.2) are multi-Cu oxidases found in plants, fungi, and other microorganisms that catalyze the oxidation of a wide variety of organic and inorganic compounds to form water . They found use in many biotechnological applications such as biobleaching, decolorization of dyes, biosensors, bread industry, plastic degradation, and many more. − Moreover, antiproliferative and anticancer activities of different laccase-containing fungal extracts have been reported in the last years . The exact mechanism of laccase anticancer activity is still unknown because of the lack of identification of a possible protein domain responsible for it or understanding of the laccase role in different metabolic pathways and their broad substrate specificity .…”

Laccase-Driven Transformation of High Priority Pesticides Without Redox Mediators: Towards Bioremediation of Contaminated Wastewaters

“…Removal of chlorpyrifos obtained during this study was relatively low when compared to the laccase extracted from Pseudomonas sp. (80.56%) grown over agro-waste (Chauhan and Jha, 2018) and commercial laccase from T. versicolor (90%) with the presence of mediators tested in a buffer solution (Jin et al, 2016). On the contrary, other insecticides (carbofuran, acetamiprid, parathion, malathion, and chlorfenvinphos) that were tested for the BS-derived crude enzyme extract, and acetamiprid, parathion, malathion, and chlorfenvinphos, which were tested for commercial laccase, remained recalcitrant during the 24 h experiment.…”