Expression of industrially relevant laccases: prokaryotic style

Santhanam, Navaneetha; Vivanco, Jorge M.; Decker, Stephen R.; Reardon, Kenneth F.

doi:10.1016/j.tibtech.2011.04.005

Cited by 165 publications

(103 citation statements)

References 77 publications

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“…For instance, laccases are used in the process of paper-pulp bleaching to degrade lignin (Larsson et al 2001). Furthermore, MCO, as one of laccases, has a high demand in different manufacturing processes such as wine production, medical analysis, electrochemical detection , bioremediation (Santhanam et al 2011), and gold nanoparticle preparation (Guo et al 2015).…”

Section: Introductionmentioning

confidence: 99%

Heterologous expression of an acidophilic multicopper oxidase in Escherichia coli and its applications in biorecovery of gold

Tan

2017

Bioresour. Bioprocess.

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Background:Copper oxidase is a promising enzyme for detection of oxidation, which can function as a biosensor and in bioremediation. Previous reports have revealed that the activity of the multicopper oxidase (MCO, EC 1.10.3.2) from the Proteus hauseri ZMd44 is induced by copper ions, and has evolved to participate in the mechanism of copper transfer.Results: From P. hauseri ZMd44, a full-length, 1497-base-pair gene, lacB, encoding 499 amino acids without signal peptide, was cloned into Escherichia coli (E. coli) to obtain high amounts of MCO. The use of the pET28a vector yielded better enzyme activity, which was approximately 400 and 500 U/L for the whole cell and soluble enzyme extracts, respectively. The crude enzyme showed activity at an optimal temperature of 55 °C and it remained highly active in the range of 50-65 °C. The optimal pH was 2.2 but the activity was significantly inhibited by chloride ions. This MCO has great potential for Au adsorption (i.e., 38% w/w) and the Au@NPs were directly adsorbed on enzyme's surface. Conclusion:An acidophilic MCO from bioelectricity generating bacterium, P. hauseri, is first cloned and heterologously expressed in E. coli with high amounts and activity. This MCO has great potential for Au adsorption and can be used as a biosensor or applied to bioremediation of electronic waste.

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Section: Introductionmentioning

confidence: 99%

Heterologous expression of an acidophilic multicopper oxidase in Escherichia coli and its applications in biorecovery of gold

Tan

2017

Bioresour. Bioprocess.

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“…One crucial property of laccase was oxidative capability toward myriads of nutrient substrates. That is, laccase was not a highly specific functioning and could be used for miscellaneous industrial applications (e.g., dye decolorization, polymers degradation, bioremediation, and organic synthesis) (Mayer and Staples 2002;Santhanam et al 2011). For example, P. hauseri could express McoA-laccase under induction of copperstimulating condition .…”

Section: Genomic and Enzymes Studies Of Proteusmentioning

confidence: 99%

Electron transport phenomena of electroactive bacteria in microbial fuel cells: a review of Proteus hauseri

Hsueh

Chen

2017

Bioresour. Bioprocess.

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This review tended to decipher the expression of electron transfer capability (e.g., biofilm formation, electron shuttles, swarming motility, dye decolorization, bioelectricity generation) to microbial fuel cells (MFCs). As mixed culture were known to perform better than pure microbial cultures for optimal expression of electrochemically stable activities to pollutant degradation and bioenergy recycling, Proteus hauseri isolated as a "keystone species" to maintain such ecologically stable potential for power generation in MFCs was characterized. P. hauseri expressed outstanding performance of electron transfer (ET)-associated characteristics [e.g., reductive decolorization (RD) and bioelectricity generation (BG)] for electrochemically steered bioremediation even though it is not a nanowire-generating bacterium. This review tended to uncover taxonomic classification, genetic or genomic characteristics, enzymatic functions, and bioelectricity-generating capabilities of Proteus spp. with perspectives for electrochemical practicability. As a matter of fact, using MFCs as a tool to evaluate ET capabilities, dye decolorizer(s) could clearly express excellent performance of simultaneous bioelectricity generation and reductive decolorization (SBG and RD) due to feedback catalysis of residual decolorized metabolites (DMs) as electron shuttles (ESs). Moreover, the presence of reduced intermediates of nitroaromatics or DMs as ESs could synergistically augment efficiency of reductive decolorization and power generation. With swarming mobility, P. hauseri could own significant biofilm-forming capability to sustain ecologically stable consortia for RD and BG. This mini-review evidently provided lost episodes of great significance about bioenergysteered applications in myriads of fields (e.g., biodegradation, biorefinery, and electro-fermentation). Keywords

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“…Besides, the industrial processes are often conducted in harsh conditions such as extreme pH, temperature, or ionic strength and therefore such robust enzymes supply economically appealing materials. 32,33 The isolation and comprehensively characterization of pure laccase from Bacillus sp. SL-1 revealed its high production yield and stability.…”

Section: Oxidoreductases (Ec 1)mentioning

confidence: 99%

Identification and Molecular Characterization of Genes Coding Pharmaceutically Important Enzymes from Halo-Thermo Tolerant Bacillus

Safary¹,

Moniri²,

Hamzeh‐Mivehroud³

et al. 2016

Adv Pharm Bull

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Expression of industrially relevant laccases: prokaryotic style

Cited by 165 publications

References 77 publications

Heterologous expression of an acidophilic multicopper oxidase in Escherichia coli and its applications in biorecovery of gold

Heterologous expression of an acidophilic multicopper oxidase in Escherichia coli and its applications in biorecovery of gold

Electron transport phenomena of electroactive bacteria in microbial fuel cells: a review of Proteus hauseri

Identification and Molecular Characterization of Genes Coding Pharmaceutically Important Enzymes from Halo-Thermo Tolerant Bacillus

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