First Evidence of a Potential Antimicrobial Activity of Bacterial Laccase Against Various Plant Pathogens

Verma, Ashwani Kumar; Shirkot, Poonam; Dhiman, Karuna; Sharma, R. L.; Chauhan, Anjali

doi:10.1007/s40009-018-0695-1

Cited by 3 publications

(2 citation statements)

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“…Interestingly, apart from acting as catalysts in the synthesis of biologically active molecules, laccases were investigated as potential therapeutics themselves. A recent example of such an investigation concluded that crude and purified Pseudomonas putida LUA15.1 laccase preparations inhibited the mycelial growth and morphology of six fungal pathogens [103]. In a report predating the former, laccase from a white rot fungus Abortiporus biennis demonstrated activity against Hep G2 and MCF-7 cells with IC 50 values of 12.5 µM and 6.7 µM, respectively, as well as inhibitory activity against HIV-1 reverse transcriptase [104].…”

Section: Pharma/cosmetics/agrochemicalsmentioning

confidence: 99%

Applications of Microbial Laccases: Patent Review of the Past Decade (2009–2019)

et al. 2019

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There is a high number of well characterized, commercially available laccases with different redox potentials and low substrate specificity, which in turn makes them attractive for a vast array of biotechnological applications. Laccases operate as batteries, storing electrons from individual substrate oxidation reactions to reduce molecular oxygen, releasing water as the only by-product. Due to society’s increasing environmental awareness and the global intensification of bio-based economies, the biotechnological industry is also expanding. Enzymes such as laccases are seen as a better alternative for use in the wood, paper, textile, and food industries, and they are being applied as biocatalysts, biosensors, and biofuel cells. Almost 140 years from the first description of laccase, industrial implementations of these enzymes still remain scarce in comparison to their potential, which is mostly due to high production costs and the limited control of the enzymatic reaction side product(s). This review summarizes the laccase applications in the last decade, focusing on the published patents during this period.

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Section: Pharma/cosmetics/agrochemicalsmentioning

confidence: 99%

Applications of Microbial Laccases: Patent Review of the Past Decade (2009–2019)

et al. 2019

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“…Melanin pigment that requires laccases to be synthetized has shown to be one of the important virulence factors in this opportunistic pathogen. By contrast, the exceptional versatility of laccases has also been demonstrated in a research work showing antimicrobial activity of Pseudomonas putida laccase against several fungal plant pathogens . In this context, several antimicrobial effects have been identified in some laccase‐catalyzed compounds (e.g.…”

Section: Interesting Roles In Naturementioning

confidence: 99%

Laccases as versatile enzymes: from industrial uses to novel applications

Moreno

Ibarra²,

Eugenio³

et al. 2019

J of Chemical Tech & Biotech

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The application of enzymes offers an enormous potential in the improvement of existing industrial procedures and in the establishment of new processes for obtaining high-added value products. Enzymes provide cleaner and more efficient industrial processes and contribute to the sustainability concept. In this sense, laccases are very versatile biocatalysts currently used in food, textile and pulp and paper sectors among others. During the last years, scientific efforts have been diverted to the exploitation of such interesting enzymes in novel fields like lignocellulosic biorefineries, biosensors or enzymatic biofuel cells. This review provides a general vision of the use of laccase enzymes describing their main characteristics and mode of action. Furthermore, their current uses in industrial processes are summarized and the most novel potential application of laccases are revealed. The increasing interest on laccases is also demonstrated by the research efforts on enzyme engineering as it is detailed in this review. wileyonlinelibrary.com/jctb www.soci.org AD Moreno et al. J Chem Technol Biotechnol 2020; 95: 481-494

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