Xenobiotics enhance laccase activity in alkali-tolerant γ-proteobacterium JB

Singh, Gursharan; Batish, Mona; Sharma, Prince; Capalash, Neena

doi:10.1590/s1517-83822009000100004

Cited by 14 publications

(9 citation statements)

References 30 publications

(35 reference statements)

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“…This find may be in accordance with others citation that reported the enhancement of laccase production in presence of L-glutamine, tyrosine, L-cystine, lysine, and isoleucine [16]. Contrary to other finding recorded that the L-valine, L-arginine, L-cysteine, and biotin caused repression of laccase titer [17,18] and phenylalanine, nicotinic acid and L-histidine HCl were recorded as enhancers for laccase production. Addition of organic solvents, with respect to their concentration, showed varied effects on laccase production.…”

Section: Effects Of Different Amino Acids and Vitamins On Laccase Prosupporting

confidence: 92%

Application of Central Composite Designs Utilized for Scale-up Strategies in the Optimization Process for Development Laccase Production and for the Bioremediation of Various Industrial Pollutants

Abdelgalil¹,

Attia²,

Reyed³

et al. 2019

Act Scie Micro

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Section: Effects Of Different Amino Acids and Vitamins On Laccase Prosupporting

confidence: 92%

Application of Central Composite Designs Utilized for Scale-up Strategies in the Optimization Process for Development Laccase Production and for the Bioremediation of Various Industrial Pollutants

Abdelgalil¹,

Attia²,

Reyed³

et al. 2019

Act Scie Micro

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“…27 However in case of bacteria, few reports are available on regulation of laccase production by media components. 15,18 Effect of phosphate on laccase production in M162 medium Phosphate levels beyond 100 mM inhibited laccase production in all the bacterial isolates in M162 agar medium (Table S2). In liquid M162 medium, minimum laccase inhibitory concentration (MLIC) of phosphate was observed which varied with species as 2L was most sensitive (MLIC, 30 mM) in comparison to JB (MLIC, 150 mM) whereas others (SS4, 9L, 3L, JJ5) ceased laccase production at 100 mM and above ( Figure 1).…”

Section: Resultsmentioning

confidence: 95%

“…It was also observed that phenolic substances in liquid medium play role in screening of different laccase producing fungi . However in case of bacteria, few reports are available on regulation of laccase production by media components …”

Section: Resultsmentioning

confidence: 99%

“…The enzyme productivity of microorganisms depends to a large extent on the medium constituents and their concentration. Nutrient agar, Minimal M162, medium and Luria broth supplemented with different concentrations of substrate (guaiacol, ABTS or syringaldazine) and copper ions as inducer were used for the isolation of laccase producing bacteria but no specific medium is known so far. On our way to isolate potential laccase producers, minimal M9 and M162 media were used in this study and different results were obtained.…”

Section: Introductionmentioning

confidence: 99%

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Impact of phosphate and other medium components on physiological regulation of bacterial laccase production

Kaur

Singh

Gupta

et al. 2016

Biotechnology Progress

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Laccases are multicopper oxidases known to catalyze the transformation of a wide range of phenolic and non-phenolic substrates using oxygen as electron acceptor and forming water as the only by product. Their potential relevance in several industries requires the constant search for novel laccases. Positive outcome of the isolation of laccase producing bacteria depends on the nature and concentration of media constituents. Several attempts to isolate laccase producing bacteria failed when the phosphate-containing M9 minimal medium was used. Shift to phosphate-less M162 medium led to successful isolations. Seven bacterial isolates belonging to genera Bacillus, Lysinibacillus, Bhargavaea and Rheinheimera were used to study the effect of medium constituents on laccase production. Inorganic phosphate (≥50 mM) was found to regulate laccase synthesis negatively though no inhibitory effect of phosphate (10-500 mM) was seen on laccase activity. All isolates ceased laccase synthesis when grown in the presence of tryptone (0.2-1%), with R. tangshanensis as an exception, or yeast extract (1.5-2%) as the only C/N source in M162 medium. Supplementation upto 0.1% of glucose in basal M162 medium increased laccase production in five isolates but decreased at higher concentrations. The influence of medium components on laccase synthesis was further affirmed by zymographic studies. These observations offer possibilities of isolating promising laccase producers from diverse environmental sources. © 2016 American Institute of Chemical Engineers Biotechnol. Prog., 33:541-548, 2017.

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“…3 Medium optimization for production of laccase by prokaryotes Submerged or solid state fermentation for ligninolytic enzyme production is highly regulated by the media composition or ingredients (Niladevi et al 2007;Singh and Chen 2008;Singh et al 2009a;Jing 2010), or essentially by the nutrient levels in fermentation medium. Moreover, medium optimization is an important and realizable option to reduce production cost (Singh and Chen 2008).…”

Section: Isolation and Screening Of Prokaryotes For Laccasesmentioning

confidence: 99%

Laccase from prokaryotes: a new source for an old enzyme

Singh

Bhalla

Kaur

et al. 2011

Rev Environ Sci Biotechnol

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135

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Laccases (benzenediol: oxygen oxidoreductase, EC 1.10.3.2) are multi-copper-containing enzymes capable of catalyzing the oxidation of a wide range of phenolic and non phenolic aromatic compounds. The available data indicates that laccases from prokaryotes are promising biological tools for green chemistry based applications, especially in decolorization of industrial textile dye effluents which constitute a major threat to soil and ground water reservoirs worldwide. Another appropriate application of prokaryotic laccases is bio-bleaching of different kind of pulps where there is indiscriminate use of hazardous chlorine based chemicals for brightness of the paper. In recent years, researchers have shown interest in the identification and characterization of laccases from prokaryotic sources. This catalyst is not commonly reported from this kingdom, although prokaryotes have immense environmental adaptability and biochemical versatility. Moreover, true laccases or laccase-like enzymes exist in many gram-negative, gram-positive bacteria and actinomycetes. Corresponding genes have been identified and functionally expressed in genetically developed hosts. This review summarizes the research efforts to characterize laccases and their properties from different prokaryotic sources, including bacteria and actinomycetes.

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Xenobiotics enhance laccase activity in alkali-tolerant γ-proteobacterium JB

Cited by 14 publications

References 30 publications

Application of Central Composite Designs Utilized for Scale-up Strategies in the Optimization Process for Development Laccase Production and for the Bioremediation of Various Industrial Pollutants

Application of Central Composite Designs Utilized for Scale-up Strategies in the Optimization Process for Development Laccase Production and for the Bioremediation of Various Industrial Pollutants

Impact of phosphate and other medium components on physiological regulation of bacterial laccase production

Laccase from prokaryotes: a new source for an old enzyme

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