Biodegradation of dyes and polyaromatic hydrocarbons by two allelic forms of Lentinula edodes laccase expressed from Pichia pastoris

Wong, Kin‐Sing; Huang, Qianli; Au, Chun Hang; Wang, Jun; Kwan, Hoi Shan

doi:10.1016/j.biortech.2011.10.097

Cited by 43 publications

(24 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Mendes et al (2011) found maximum decolorization and detoxification of model dye containing wastewaters when azoreductase and laccase are used simultaneously. Wong et al (2012) cloned two laccase genes from RNA of Lentinula edodes L54 mycelium and showed that the efficient biodegradation of dyes and polyaromatic hydrocarbons take place by two allelic forms of L. edodes laccase expressed from methylotrophic yeast Pichia pastoris. These genes appear as allelic forms with 1573 bp long and differed only by 21 nucleotides.…”

Section: Decolorization and Degradation Of Azo Dyes By Laccasesmentioning

confidence: 99%

Enzymatic decolorization and degradation of azo dyes – A review

Singh

2015

International Biodeterioration & Biodegradation

502

192

View full text Add to dashboard Cite

Section: Decolorization and Degradation Of Azo Dyes By Laccasesmentioning

confidence: 99%

Enzymatic decolorization and degradation of azo dyes – A review

Singh

2015

International Biodeterioration & Biodegradation

502

192

View full text Add to dashboard Cite

“…Laccases (benzenediol:oxygen oxidoreductase, E.C.1.10.3.2) are multi-Cu oxidases which demonstrate a high relevance to various environment-friendly applications, such as bioremediations and biorefinery [1], [2], [3]. The enzymes catalyze a single-electron oxidation of small aromatic substrates with a concomitant reduction of molecular oxygen into water [1], [4], [5].…”

Section: Introductionmentioning

confidence: 99%

A Novel Lentinula edodes Laccase and Its Comparative Enzymology Suggest Guaiacol-Based Laccase Engineering for Bioremediation

Wong

Cheung

et al. 2013

PLoS ONE

Self Cite

View full text Add to dashboard Cite

Laccases are versatile biocatalysts for the bioremediation of various xenobiotics, including dyes and polyaromatic hydrocarbons. However, current sources of new enzymes, simple heterologous expression hosts and enzymatic information (such as the appropriateness of common screening substrates on laccase engineering) remain scarce to support efficient engineering of laccase for better “green” applications. To address the issue, this study began with cloning the laccase family of Lentinula edodes. Three laccases perfectio sensu stricto (Lcc4A, Lcc5, and Lcc7) were then expressed from Pichia pastoris, characterized and compared with the previously reported Lcc1A and Lcc1B in terms of kinetics, stability, and degradation of dyes and polyaromatic hydrocarbons. Lcc7 represented a novel laccase, and it exhibited both the highest catalytic efficiency (assayed with 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) [ABTS]) and thermostability. However, its performance on “green” applications surprisingly did not match the activity on the common screening substrates, namely, ABTS and 2,6-dimethoxyphenol. On the other hand, correlation analyses revealed that guaiacol is much better associated with the decolorization of multiple structurally different dyes than are the two common screening substrates. Comparison of the oxidation chemistry of guaiacol and phenolic dyes, such as azo dyes, further showed that they both involve generation of phenoxyl radicals in laccase-catalyzed oxidation. In summary, this study concluded a robust expression platform of L. edodes laccases, novel laccases, and an indicative screening substrate, guaiacol, which are all essential fundamentals for appropriately driving the engineering of laccases towards more efficient “green” applications.

show abstract

“…Laccase biotechnological and environmental applications require great enzyme quantities; unfortunately laccases obtained from natural sources are not suitable for long growth periods, low product/biomass ( Y p / x ) or product/substrate ( Y p / s ) yield, and prolonged, complex, and costly isolation procedures [3, 6, 11]. Therefore, heterologous expression is a promising option for greater scale production, using the potential of hosts that are easy to handle and culture, such as bacteria and yeast [12].…”

Section: Introductionmentioning

confidence: 99%

Plackett-Burman Design for rGILCC1 Laccase Activity Enhancement in Pichia pastoris: Concentrated Enzyme Kinetic Characterization

et al. 2017

View full text Add to dashboard Cite

Laccases are multicopper oxidases that catalyze aromatic and nonaromatic compounds with concomitant reduction of molecular oxygen to water. They are of great interest due to their potential biotechnological applications. In this work we statistically improved culture media for recombinant GILCC1 (rGILCC1) laccase production at low scale from Ganoderma lucidum containing the construct pGAPZαA-GlucPost-Stop in Pichia pastoris. Temperature, pH stability, and kinetic parameter characterizations were determined by monitoring concentrate enzyme oxidation at different ABTS substrate concentrations. Plackett-Burman Design allowed improving enzyme activity from previous work 36.08-fold, with a laccase activity of 4.69 ± 0.39 UL−1 at 168 h of culture in a 500 mL shake-flask. Concentrated rGILCC1 remained stable between 10 and 50°C and retained a residual enzymatic activity greater than 70% at 60°C and 50% at 70°C. In regard to pH stability, concentrated enzyme was more stable at pH 4.0 ± 0.2 with a residual activity greater than 90%. The lowest residual activity greater than 55% was obtained at pH 10.0 ± 0.2. Furthermore, calculated apparent enzyme kinetic parameters were a Vmax of 6.87 × 10−5 mM s−1, with an apparent Km of 5.36 × 10−2 mM. Collectively, these important stability findings open possibilities for applications involving a wide pH and temperature ranges.

show abstract

Biodegradation of dyes and polyaromatic hydrocarbons by two allelic forms of Lentinula edodes laccase expressed from Pichia pastoris

Cited by 43 publications

References 34 publications

Enzymatic decolorization and degradation of azo dyes – A review

Enzymatic decolorization and degradation of azo dyes – A review

A Novel Lentinula edodes Laccase and Its Comparative Enzymology Suggest Guaiacol-Based Laccase Engineering for Bioremediation

Plackett-Burman Design for rGILCC1 Laccase Activity Enhancement in Pichia pastoris: Concentrated Enzyme Kinetic Characterization

Contact Info

Product

Resources

About