Microbial Laccase: a robust enzyme and its industrial applications

Singh, Deepti; Gupta, Neeraj

doi:10.2478/s11756-019-00414-9

Cited by 116 publications

(62 citation statements)

References 98 publications

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“…BbLac2 contained a 1773 bp‐open reading frame (ORF) that encoded a 519‐amino‐acid protein including ten putative N‐glycosylation sites at positions 82, 98, 125, 291, 348, 365, 420, 439, 472 and 493, and a typical N‐terminal signal peptide (18 amino acids). Three predicted copper‐oxidase domains present in BbLac2, which are similar to pfam07732 (9 e ‐13 ), pfam00394 (9 e ‐10 ) and pfam07731 (5 e ‐15 ) respectively, characteristics of a laccase (Hakulinen and Rouvinen, 2015; Singh and Gupta, 2020). A leucine residue presents in the T1 copper centre of BbLac2 (Supporting Information Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Insect melanogenesis is related to innate immunity and cell haemostasis, contributing to elimination of pathogens (Sugumaran, 2002; González‐Santoyo and Córdoba‐Aguilar, 2012). Similar to laccases, PPOs also belong to the family of MCOs, which share with laccase‐like molecular structures and similar catalytic functions (Madhavi and Lele, 2009; Singh and Gupta, 2020). Insects synthesize melanin via L‐DOPA pathway, which is from phenylalanine and involved in PO enzymes (the active form of proPO).…”

Section: Discussionmentioning

confidence: 99%

“…In invertebrates, laccases are involved in activation of cuticle sclerotization, keratinocyte tanning, pigmentation, food detoxification and oxidative stress response, even in innate immunity (Arakane et al ., 2005; Karlovsky et al ., 2016; Chen et al ., 2020). Laccases produced by fungi play a variety of physiological functions in aspects of growth and development (decomposition of lignocellulose polymers, pigmentation and sporulation process), abiotic stress response and pathogenesis (Crowe and Olsson, 2001; Jaszek et al ., 2006 a, b; Cañero and Roncero, 2008; Fang et al ., 2010; Yang et al ., 2012; Janusz et al ., 2020; Singh and Gupta, 2020).…”

Section: Introductionmentioning

confidence: 99%

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Multifunctional role of a fungal pathogen‐secreted laccase 2 in evasion of insect immune defense

Deng

Wang

et al. 2021

Environmental Microbiology

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Summary Laccases are widely present in bacteria, fungi, plants and invertebrates and involved in a variety of physiological functions. Here, we report that Beauveria bassiana, an economic important entomopathogenic fungus, secretes a laccase 2 (BbLac2) during infection that detoxifies insect immune response‐generated reactive oxygen species (ROS) and interferes with host immune phenoloxidase (PO) activation. BbLac2 is expressed in fungal cells during proliferation in the insect haemocoel and can be found to distribute on the surface of haemolymph‐derived in vivo fungal hyphal bodies or be secreted. Targeted gene‐knockout of BbLac2 increased fungal sensitivity to oxidative stress, decreased virulence to insect, and increased host PO activity. Strains overexpressing BbLac2 showed increased virulence, with reduced host PO activity and lowered ROS levels in infected insects. In vitro assays revealed that BbLac2 could eliminate ROS and oxidize PO substrates (phenols), verifying the enzymatic functioning of the protein in detoxification of cytotoxic ROS and interference with the PO cascade. Moreover, BbLac2 acted as a cell surface protein that masked pathogen associated molecular patterns (PAMPs), enabling the pathogen to evade immune recognition. Our data suggest a multifunctional role for fungal pathogen‐secreted laccase 2 in evasion of insect immune defenses.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Multifunctional role of a fungal pathogen‐secreted laccase 2 in evasion of insect immune defense

Deng

Wang

et al. 2021

Environmental Microbiology

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“…Laccase is one widely used oxidoreductase catalyst of interest due to its catalysis potential of different dyes (Bilal et al, 2019). As a matter of fact, new sources for fungal and bacterial laccases have been increasingly demanded to degrade dye effluents, or most commonly known as dye waste (Dauda and Erkurt, 2020;Jeon and Park, 2020;Joshi et al, 2020;Singh and Gupta, 2020).…”

Section: Introductionmentioning

confidence: 99%

“…An estimate of 700,000 tons of different synthetic dyes are produced annually ( Holkar et al, 2016 ; Bilal et al, 2017 ; Katheresan et al, 2018 ). Those dyes have stable chemical structures that make them resistant to degradation by heat, light, or water ( Lu et al, 2012a , b ; Singh and Gupta, 2020 ). Some even form water-soluble complexes that are toxic to human, animal, and marine life ( Bilal et al, 2019 ).…”

Section: Introductionmentioning

confidence: 99%

Current Development in Decolorization of Synthetic Dyes by Immobilized Laccases

et al. 2020

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The world today is in a quest for new means of environmental remediation as the methods currently used are not sufficient to halt the damage. Mostly, a global direction is headed toward a shift from traditional chemical-based methods to a more ecofriendly alternative. In this context, biocatalysis is seen as a cost-effective, energy saving, and clean alternative. It is meant to catalyze degradation of recalcitrant chemicals in an easy, rapid, green, and sustainable manner. One already established application of biocatalysis is the removal of dyes from natural water bodies using enzymes, notably oxidoreductases like laccases, due to their wide range of substrate specificity. In order to boost their catalytic activity, various methods of enhancements have been pursued including immobilization of the enzyme on different support materials. Aside from increased catalysis, immobilized laccases have the advantages of higher stability, better durability against harsh environment conditions, longer half-lives, resistance against protease enzymes, and the ability to be recovered for reuse. This review briefly outlines the current methods used for detoxification and decolorization of dye effluents stressing on the importance of laccases as a revolutionary biocatalytic solution to this environmental problem. This work highlights the significance of laccase immobilization and also points out some of the challenges and opportunities of this technology.

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