Heterologous laccase production and its role in industrial applications

Piscitelli, Alessandra; Pezzella, Cinzia; Giardina, Paola; Faraco, Vincenza; Sannia, Giovanni

doi:10.4161/bbug.1.4.11438

Cited by 144 publications

(116 citation statements)

References 156 publications

(134 reference statements)

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“…Recombinant hosts used to successfully produce high titers of bacterial lignocellulose-degrading enzymes and the tools to transform these organisms have also been well studied. Piscitelli et al (2010) have reviewed heterologous laccase production. Lactic acid bacteria are commonly used in the food industry for the production of dairy products and are characterized by their ability to grow at low pH.…”

Section: Modification and Recombinant Expression Of Lignocellulose-dementioning

confidence: 99%

Bacterial biodegradation and bioconversion of industrial lignocellulosic streams

Mathews

Pawlak

Grunden

2015

Appl Microbiol Biotechnol

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Lignocellulose is a term for plant materials that are composed of matrices of cellulose, hemicellulose, and lignin. Lignocellulose is a renewable feedstock for many industries. Lignocellulosic materials are used for the production of paper, fuels, and chemicals. Typically, industry focuses on transforming the polysaccharides present in lignocellulose into products resulting in the incomplete use of this resource. The materials that are not completely used make up the underutilized streams of materials that contain cellulose, hemicellulose, and lignin. These underutilized streams have potential for conversion into valuable products. Treatment of these lignocellulosic streams with bacteria, which specifically degrade lignocellulose through the action of enzymes, offers a low-energy and low-cost method for biodegradation and bioconversion. This review describes lignocellulosic streams and summarizes different aspects of biological treatments including the bacteria isolated from lignocellulose-containing environments and enzymes which may be used for bioconversion. The chemicals produced during bioconversion can be used for a variety of products including adhesives, plastics, resins, food additives, and petrochemical replacements.

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Section: Modification and Recombinant Expression Of Lignocellulose-dementioning

confidence: 99%

Bacterial biodegradation and bioconversion of industrial lignocellulosic streams

Mathews

Pawlak

Grunden

2015

Appl Microbiol Biotechnol

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“…Laccases are also employed in the processing of beverages (wine, fruit juice, and beer), gelation of sugar beet pectin, baking, and the design of biosensors (Osma et al, 2010;Gassara-Chatti et al, 2013;Lanzellotto et al, 2014). The promising and valuable applications of laccases in many biotechnological processes have resulted in increased demand for isolation of new laccase genes from different sources Piscitelli et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

Heterologous expression and characterization of a high redox potential laccase from Coriolopsis polyzona MUCL 38443

Pinar¹,

Tamerler²,

Karataş³

2017

Turk J Biol

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In this study, a novel laccase gene, named as Cplcc1, and its corresponding cDNA were isolated and characterized from the Coriolopsis polyzona MUCL 38443 strain. The Cplcc1 gene consists of a 1563-bp open reading frame encoding a protein of 520 amino acids with a 20-residue putative signal peptide. The size of the Cplcc1 gene is 2106 bp and it contains ten introns and five potential N-glycosylation sites. Additionally, the isolated full-length Cplcc1 cDNA was successfully expressed in Pichia pastoris. The heterologous expression conditions were also optimized and the highest activity value increased to 800 U L -1 with 1.5% methanol, 0.8 mM CuSO 4 , and 0.6% L-alanine supplementation. The recombinant laccase was partially purified and the molecular weight was found as approximately 54 kDa. The maximum oxidation activity was observed for 2,2-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) at pH 3.0. The optimal temperature was found as 70 °C. On the other hand, at 30 °C, the enzyme was stable for more than a week and its half-life was longer than 8 h. The K m , V max , k cat , and k cat K m -1 values of the recombinant laccase were identified as 0.137 mM, 288.6 µmol min -1 L -1 , 5.73 × 10 5 min -1 , and 4.18 × 10 6 min -1 mM -1 , respectively. Sodium azide, L-cysteine, and SDS were found as usual inhibitors.

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“…In this study, we examined the transcriptome and activity profile of the phenol oxidase (laccase; EC 1.10.3.2) family of lignin-degrading enzymes under different culture conditions. Laccases catalyze the oxidation of various aromatic substrates with a subsequent reduction of molecular oxygen to water (41). The broad substrate specificity of laccases permits their use in multiple biotechnological and industrial applications as inexpensive biologically and environmentally friendly tools for the pretreatment of lignocellulose for bioethanol production, pulp bleaching, dye degradation, and xenobiotic transformation and detoxification (20).…”

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confidence: 99%

Transcriptional and Enzymatic Profiling of Pleurotus ostreatus Laccase Genes in Submerged and Solid-State Fermentation Cultures

Castanera

Pérez

Omarini

et al. 2012

Appl Environ Microbiol

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ABSTRACTThe genome of the white rot basidiomycetePleurotus ostreatusincludes 12 phenol oxidase (laccase) genes. In this study, we examined their expression profiles in different fungal strains under different culture conditions (submerged and solid cultures) and in the presence of a wheat straw extract, which was used as an inducer of the laccase gene family. We used a reverse transcription-quantitative PCR (RT-qPCR)-based approach and focused on determining the reaction parameters (in particular, the reference gene set for the normalization and reaction efficiency determinations) used to achieve an accurate estimation of the relative gene expression values. The results suggested that (i) laccase gene transcription is upregulated in the induced submerged fermentation (iSmF) cultures but downregulated in the solid fermentation (SSF) cultures, (ii) theLacc2andLacc10genes are the main sources of laccase activity in the iSmF cultures upon induction with water-soluble wheat straw extracts, and (iii) an additional, as-yet-uncharacterized activity (Unk1) is specifically induced in SSF cultures that complements the activity of Lacc2 and Lacc10. Moreover, both the enzymatic laccase activities and theLaccgene family transcription profiles greatly differ between closely related strains. These differences can be targeted for biotechnological breeding programs for enzyme production in submerged fermentation reactors.

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Heterologous laccase production and its role in industrial applications

Cited by 144 publications

References 156 publications

Bacterial biodegradation and bioconversion of industrial lignocellulosic streams

Bacterial biodegradation and bioconversion of industrial lignocellulosic streams

Heterologous expression and characterization of a high redox potential laccase from Coriolopsis polyzona MUCL 38443

Transcriptional and Enzymatic Profiling of Pleurotus ostreatus Laccase Genes in Submerged and Solid-State Fermentation Cultures

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