Bio-Prospecting Laccases in the Bacterial Diversity of Activated Sludge From Pulp and Paper Industry

Gupta, Vijaya; Capalash, Neena; Gupta, Naveen; Sharma, Prince

doi:10.1007/s12088-016-0624-2

Cited by 10 publications

(4 citation statements)

References 31 publications

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“…Thus, the genomes of APG isolates were examined for the presence of oxidases. Laccases are copper-containing oxidases catalyzing the oxidation of aromatics coupled to the synthesis of water as a by-product [ 51 ]. Notably, none of the genomes possessed genes encoding this enzyme which is in agreement with our experimental results [ 24 ].…”

Section: Resultsmentioning

confidence: 99%

Genome analysis to decipher syntrophy in the bacterial consortium ‘SCP’ for azo dye degradation

2021

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Background A bacterial consortium SCP comprising three bacterial members, viz. Stenotrophomonas acidaminiphila APG1, Pseudomonas stutzeri APG2 and Cellulomonas sp. APG4 was developed for degradation of the mono-azo dye, Reactive Blue 28. The genomic analysis of each member of the SCP consortium was done to elucidate the catabolic potential and role of the individual organism in dye degradation. Results The genes for glycerol utilization were detected in the genomes of APG2 and APG4, which corroborated with their ability to grow on a minimal medium containing glycerol as the sole co-substrate. The genes for azoreductase were identified in the genomes of APG2 and APG4, while no such trait could be determined in APG1. In addition to co-substrate oxidation and dye reduction, several other cellular functions like chemotaxis, signal transduction, stress-tolerance, repair mechanisms, aromatic degradation, and copper tolerance associated with dye degradation were also annotated. A model for azo dye degradation is postulated, representing the predominant role of APG4 and APG2 in dye metabolism while suggesting an accessory role of APG1. Conclusions This exploratory study is the first-ever attempt to divulge the genetic basis of azo-dye co-metabolism by cross-genome comparisons and can be harnessed as an example for demonstrating microbial syntrophy.

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Section: Resultsmentioning

confidence: 99%

Genome analysis to decipher syntrophy in the bacterial consortium ‘SCP’ for azo dye degradation

2021

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“…Laccase is a multi-copper oxidase that catalyzes the oxidation of phenolics, and non-phenolics compounds [10,31,32]. Laccases are important enzymes due to their broad biotechnological applications: (1) biodegradation and bioremediation in (a) paper and pulp industry, (b) textile and food processing industry, (2) biosensor, and (3) biofuel production [8,10,21,22,33]. The immobilization of laccases is required for improving the process economy through enhanced activity, stability, and reusability [10,28].…”

Section: Introductionmentioning

confidence: 99%

Rhus vernicifera Laccase Immobilization on Magnetic Nanoparticles to Improve Stability and Its Potential Application in Bisphenol A Degradation

et al. 2020

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In the present study, Rhus vernicifera laccase (RvLac) was immobilized through covalent methods on the magnetic nanoparticles. Fe 2 O 3 and Fe 3 O 4 nanoparticles activated by 3-aminopropyltriethoxysilane followed with glutaraldehyde showed maximum immobilization yields and relative activity up to 81.4 and 84.3% at optimum incubation and pH of 18 h and 5.8, respectively. The maximum RvLac loading of 156 mg/g of support was recorded on Fe 2 O 3 nanoparticles. A higher optimum pH and temperature of 4.0 and 45 °C were noted for immobilized enzyme compared to values of 3.5 and 40 °C for free form, respectively. Immobilized RvLac exhibited better relative activity profiles at various pH and temperature ranges. The immobilized enzyme showed up to 16-fold improvement in the thermal stability, when incubated at 60 °C, and retained up to 82.9% of residual activity after ten cycles of reuses. Immobilized RvLac exhibited up to 1.9-fold higher bisphenol A degradation efficiency potential over free enzyme. Previous reports have demonstrated the immobilization of RvLac on nonmagnetic supports. This study has demonstrated that immobilization of RvLac on magnetic nanoparticles is very efficient especially for achieving high loading, better pH and temperature profiles, and thermal-and solvents-stability, high reusability, and higher degradation of bisphenol A.

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“…Although, in recent years, extensive isolation of prokaryotic laccases has been attempted, and a few bacterial laccases have been characterized, however in general, these enzymes are not suited to the harsh industrial condi- tions in the pulp and paper industries (Singh et al, 2015). Most bacterial laccases are intracellular or spore bounded, and this restricts their implementation on an industrial scale by making the downstream processing expensive (Gupta et al, 2017;Sharma et al, 2007). Bacillus sp.…”

Section: Introductionmentioning

confidence: 99%

Thermo and halo tolerant laccase from <i>Bacillus</i> sp. SS4: Evaluation for its industrial usefulness

Singh

Kaur

et al. 2019

J. Gen. Appl. Microbiol.

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Laccases are unable to oxidize the non-phenolic components of complex lignin polymer due to their less redox potential (E0). Catalytic efficiency of laccases relies on the mediators that potentiates their oxidative strength; for breaking the recalcitrant lignin. Laccase from Bacillus sp. SS4 was evaluated for its compatibility with natural and synthetic mediators. (2 mM). It was found that acetosyringone, vanillin, orcinol and veratraldehyde have no adverse effect on the laccase activity up to 3 h. Syringaldehyde, p-coumaric acid, ferulic acid and hydroquinone reduced the enzyme activity ≥50% after 1.0 h, but laccase activity remained 100 to ~120% in the presence of synthetic mediators HBT (1-Hydroxylbenzotrizole) and ABTS. (2,2'-azino-bis (3-ethylbenzothiazoline-6-sulphonic acid) after 3 h. MgSO and MnSO (40 mM) increased the enzyme activity 3.5 fold and the enzyme possessed ≥70% activity at a very high concentration. (2 M) of NaCl. The enzyme retained 40-110% activity in the presence of 10% DMSO (dimethylsulfoxide), acetone, methanol and ethyl acetate. On the other hand, CuSO (100 μM) induced the laccase production 8.5 fold without increasing the growth of bacterial cells. Laccase from SS4 appropriately decolorized the indigo carmine (50 μM) completely in the presence of acetosyringone (100 μM) within 10 min and 25% decolorization was observed after 4 h without any mediator.

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Bio-Prospecting Laccases in the Bacterial Diversity of Activated Sludge From Pulp and Paper Industry

Cited by 10 publications

References 31 publications

Genome analysis to decipher syntrophy in the bacterial consortium ‘SCP’ for azo dye degradation

Genome analysis to decipher syntrophy in the bacterial consortium ‘SCP’ for azo dye degradation

Rhus vernicifera Laccase Immobilization on Magnetic Nanoparticles to Improve Stability and Its Potential Application in Bisphenol A Degradation

Thermo and halo tolerant laccase from <i>Bacillus</i> sp. SS4: Evaluation for its industrial usefulness

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