sodium azide, L-cystein, thiourea, EDTA, thioglycolic acid and metallic ions i

sodium azide, L-cystein, thiourea, EDTA, thioglycolic acid and metallic ions i.e. at high temperature and alkaline pH. The laccase activity was enhanced by Cu+2, Zn+2 and Mn+2. In addition, the dye decolorization potential of purified laccase was much higher in terms of extent as well as time. The purified laccase decolorized (96%) of anthraquinonic dye Reactive blue- 4 within 4 h and its biodegradation studies was monitored by UV visible spectra, FTIR and HPLC which concluded that cyanobacterial laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. Intro Laccases (benezenediol:oxygen oxidoreductase (EC 1.10.3.2) are group of oxidases that contains multi copper atoms and catalyzes the oxidation of different phenolic and non-phenolic compounds with simultaneous reduction of oxygen to water [1]. Laccases are Versipelostatin found mostly as monomers, dimmers and are generally extracellular glycoproteins comprising four copper atoms per monomer. The active site consists of at least one type-1 (T1) copper, associated with oxidation of substrates; one type-2 (T2) and two type-3 (T3) coppers arranged inside a trinuclear cluster, where reduction of molecular oxygen occurs. The low substrate specificity makes this enzyme interesting for commercial biotechnology and environmental applications such as food and makeup products industries, paper and pulp industries, textile industries, as well as biotransformation of environmental pollutants, biosensor, biofuel and organic synthesis applications [2]. The presence of laccase are extensively reported among vegetation, fungi and in some bacteria that are involved in diverse physiological functions, lignin degradation, pigmentation, pathogenesis, melanin production and spore coating resistance [3C5]. Usually, fungi are the most efficient laccase suppliers and commercially been used till day whereas, fewer studies have been carried out in prokaryotes [6]. In cyanobacterial strain, only and shown to have laccase activity till day but their purification has not been done so far. Bacterial laccases reported to have much higher thermostability as compared to fungal laccases [4, 7]. Recently, 1st laccase purification from green algae was reported [8]. The vast software of laccases in various biotechnological sector requires high amounts of cost effective enzyme production and hence scientist needs adequate attention towards exploration of efficient laccase maker. Cyanobacteria are prokaryotic organism that have capabilities to survive under intense environment. Due to phototrophic mode of nutrition, short generation time and easy mass cultivation as compared to fungal source, cyanobacteria may be used as potential candidate for laccase production. The low production yield and high cost of purification methods of laccases from native sources are not suitable for large-scale production in industrial purposes. However, heterologous manifestation favours the high market demands of higher laccase productivity in shorter period with desired properties such as different substrate specificities, enhanced stabilities and cost effectiveness. It has reported that fungal laccases are glycoproteins with carbohydrate material between 5 to 30% and glycosylation is definitely important for secretion, activation, structure, and stability of fungal laccases [9]. Glycosylation causes problems in heterologous manifestation of fungal laccases that cannot be conquer easily and that make manifestation in prokaryotic systems nearly impossible [10]. However, cyanobacterial laccases can be overproduced more easily in heterologous sponsor like due to development of host-vector system for prokaryotic manifestation. [11]. Very few studies have been reported within the degradation of textile dyes through cyanobacteria and enzyme involvement in degradation of recalcitrant compounds such as dye and dyestuffs have not yet been characterized [12, 13]. Textile dyes form a large group of organic Versipelostatin substances posing undesirable and harmful effects on the environment. Due to complex aromatic structure these dyes are not very easily degraded and stable against light, water and oxidizing providers. Once discharged in.The peaks Rabbit Polyclonal to AKR1A1 located at 1272.13 cm-1 are those C-O extension. was much higher in terms of extent as well as time. The purified laccase decolorized (96%) of anthraquinonic dye Reactive blue- 4 within 4 h and its biodegradation studies was monitored by UV visible spectra, FTIR and HPLC which concluded that cyanobacterial laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. Intro Laccases (benezenediol:oxygen oxidoreductase (EC 1.10.3.2) are group of oxidases that contains multi copper atoms and catalyzes the oxidation of different phenolic and non-phenolic compounds with simultaneous reduction of oxygen to water [1]. Laccases are found mostly as monomers, dimmers and are generally extracellular glycoproteins comprising four copper atoms per monomer. The active site consists of at least one type-1 (T1) copper, associated with oxidation of substrates; one type-2 (T2) and two type-3 (T3) coppers arranged inside a trinuclear cluster, where reduction of molecular oxygen occurs. The low substrate specificity makes this enzyme interesting for commercial biotechnology and environmental applications such as food and makeup products industries, paper and pulp industries, textile industries, as well as biotransformation of environmental pollutants, biosensor, biofuel and organic synthesis applications [2]. The presence of laccase are extensively reported among vegetation, fungi and in some bacteria that are involved in diverse physiological functions, lignin degradation, pigmentation, pathogenesis, melanin production and spore coating resistance [3C5]. Usually, fungi are the most efficient laccase suppliers and commercially been used till day whereas, fewer studies have been carried out in prokaryotes [6]. In cyanobacterial strain, only and shown to have laccase activity till day but their purification has not been done so far. Bacterial laccases reported to have much higher thermostability as compared to fungal laccases [4, 7]. Recently, 1st laccase purification from green algae was reported [8]. The vast software of laccases in various biotechnological sector requires high amounts of cost effective enzyme production and hence scientist needs adequate attention towards exploration of efficient laccase maker. Cyanobacteria are prokaryotic organism that have capabilities to survive under intense environment. Due to phototrophic mode of nutrition, short generation time and easy mass cultivation as compared to fungal resource, cyanobacteria may be used as potential candidate for laccase production. The low production yield and high cost of purification methods of laccases from native sources are not suitable for large-scale production in industrial purposes. However, heterologous manifestation favours the high market demands of higher laccase productivity in shorter period with desired properties such as different substrate specificities, enhanced stabilities and cost effectiveness. It has reported that fungal laccases are glycoproteins with carbohydrate material between 5 to 30% and glycosylation is definitely important for secretion, activation, structure, and stability of fungal laccases [9]. Glycosylation causes problems in heterologous manifestation of fungal laccases that cannot be conquer easily and that make manifestation in prokaryotic systems nearly impossible [10]. However, cyanobacterial laccases can be overproduced more easily Versipelostatin in heterologous sponsor like due to development of host-vector system for prokaryotic manifestation. [11]. Very few studies have been reported within the degradation of textile dyes through cyanobacteria and enzyme involvement in degradation of recalcitrant compounds such as dye and dyestuffs have not yet been characterized [12, 13]. Textile dyes form a large group of organic substances posing undesirable and harmful effects on the environment. Due to complex aromatic structure these dyes are not very easily degraded and stable against light, water and oxidizing providers. Once discharged in water bodies, they reduce transparency, thereby influencing the photosynthetic activity and dissolved oxygen concentration for the aquatic existence. Thus, there is a need to decolorize textile dye. Numerous physical and chemical treatments such as precipitation, photo degradation, adsorption and chemical degradation are expensive, time-consuming and present methodological disadvantages [14]. Thus, biological process is considered environmental friendly and effective tool in the decolorization of textile dyes [15]. Considering the potential software of laccase for solving environmental problems, in present study, the purification and characterization of cyanobacterial CFTRI laccase was carried out and the decolorization of anthraquinonic dye Reactive blue 4 by purified laccase was evaluated. Materials and methods Chemicals 2, 2 Azino bis[3 ethylbenzthiazoline 6 sulfonate] (ABTS), acrylamide, ammonium persulfate, bis-acrylamide, coomassie amazing blue R-250, and TEMED (N,.