Characterization of a recombinant laccase from Fusarium oxysporum HUIB02 for biochemical application on dyes removal

Huy, Nguyễn Đức; Le, Nguyen Thi My; Chew, Kit Wayne; Park, Seung-Moon; Show, Pau Loke

doi:10.1016/j.bej.2021.107958

Cited by 22 publications

(7 citation statements)

References 38 publications

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“…The degradation rate catalyzed by the coupled enzyme irradiated by near-infrared light is better than that of the nonirradiated coupled enzyme and free laccase. When the reaction time reached 18 h, the catalytic degradation rate reached 81.6%, in which the degraded rate was higher than that in ref ; meanwhile, it is also higher than79.8%, and 66.5%, respectively, indicating that the ability to degrade methylene blue was significantly improved after the laccase was modified. Importantly, NIR-light irradiation further strengthened the degradation rate, in which more • OH and oxygen were beneficial for the biodegradation of laccase-Cys-Pt to methylene blue, where the increase in temperature promoted H 2 O 2 decomposition.…”

Section: Results and Discussionmentioning

confidence: 75%

Photoenzymatic Activity of Artificial–Natural Bienzyme Applied in Biodegradation of Methylene Blue and Accelerating Polymerization of Dopamine

Zheng

Cui

Zhou

et al. 2021

ACS Appl. Mater. Interfaces

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Enzymes as biocatalysts have attracted extensive attention. In addition to immobilizing or encapsulating various enzymes for combating the easy loss of enzymatic activity, strengthening the enzymatic activity upon light irradiation is a challenge. To the best of our knowledge, the work of spatiotemporally modulating the catalytic activity of artificialnatural bienzymes with a near-infrared light irradiation has not been reported. Inspired by immobilized enzymes and nanozymes, herein a platinum nanozyme was synthesized; subsequently, the platinum nanozyme was grafted on the body of laccase, thus successfully obtaining the artificial-natural bienzyme. The threedimensional structure of the artificial-natural bienzyme was greatly different from that of the immobilized enzyme or the encapsulated enzyme. The platinum nanozyme possessed excellent laccase-like activity, which was 3.7 times higher than that of laccase. Meanwhile, the coordination between the platinum nanozyme and laccase was proved. Besides, the cascaded catalysis of artificialnatural bienzyme was verified with hydrogen peroxide as a mediator. The enzymatic activities of artificial-natural bienzyme with and without near-infrared light irradiation were, respectively, 46.2 and 29.5% higher than that of free laccase. Moreover, the reversible catalytic activity of the coupled enzyme could be manipulated with and without a near-infrared light at 808 nm. As a result, the degradation rates of methylene blue catalyzed by the coupled enzyme and the platinum nanozyme were higher than that of laccase. Furthermore, accelerating polymerization of the dopamine was also demonstrated. Briefly, this facile strategy may provide a universal approach to control the catalytic activity of other natural enzymes.

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Section: Results and Discussionmentioning

confidence: 75%

Photoenzymatic Activity of Artificial–Natural Bienzyme Applied in Biodegradation of Methylene Blue and Accelerating Polymerization of Dopamine

Zheng

Cui

Zhou

et al. 2021

ACS Appl. Mater. Interfaces

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“…The expression of laccases in heterologous hosts, such as bacteria, filamentous fungi, and yeast is an effective method to increase their production [ 32 ]. Among those hosts, P. pastoris has received more attention because of its easy to manipulation and high protein secretion capacity [ 29 , 33 , 34 ], and has successfully expressed so far over 40 fungal laccases [ 35 ]. T .…”

Section: Discussionmentioning

confidence: 99%

“…In this study, rLac1 showed a strong tolerance to metal ions of Mg 2+ , Mn 2+ , and Zn 2+ , and its activity was still retained over 60% in the presence of these ions at 100 mM, while Fe 2+ inhibited enzyme activity ( Figure 4 ). Cu 2+ is considered to be an inducer of laccase activity, but the activity promotion often occurs at low concentrations [ 34 , 38 , 39 ]. However, the activity of rLac1 was obviously improved by Cu 2+ at high concentration (100 mM).…”

Section: Discussionmentioning

confidence: 99%

“…Therefore, it may be believed that Cu 2+ is helpful to the improvement of the activity of group B laccase and its production in Trametes . Fungal laccase is usually highly sensitive to Fe 2+ , probably due to the competitive inhibition of Fe 2+ in laccase electron transport [ 34 , 39 , 41 ]. The concentration of organic solvent seems to be a critical factor affecting laccase activity.…”

Section: Discussionmentioning

confidence: 99%

“…rLac1, as an inducible laccase, was found to have excellent decolorization of RBBR, and its decolorization rate is more than 90% regardless of the presence or absence of ABTS ( Table 4 ). In comparison, the decolorization rate of laccase from T. pubescens and Fusarium oxysporum to RBBR is much lower in the absence of mediator [ 34 , 41 ]. ABTS is the first synthetic mediator for laccase, and has been shown to enhance the decolorization ability of laccase.…”

Section: Discussionmentioning

confidence: 99%

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Characterization of a Recombinant Laccase B from Trametes hirsuta MX2 and Its Application for Decolorization of Dyes

Jia

Huang

Zhu³

et al. 2022

Molecules

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Trametes hirsuta is able to secrete laccase isoenzymes including constitutive and inducible forms, and has potential application for bioremediation of environmental pollutants. Here, an inducible group B laccase from T. hirsuta MX2 was heterologously expressed in Pichia pastoris, and its yield reached 2.59 U/mL after 5 days of methanol inducing culture. The optimal pH and temperature of recombinant laccase (rLac1) to 2,2′-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) were 2.5 and 60 °C, respectively. Metal ions showed different effect on rLac1 which Mg2+, Cu2+, and K+ increased enzyme activity as their concentration increased, whereas Zn2+, Na+, and Fe2+ inhibited enzyme activity as their concentration increased. rLac1 showed good tolerance to organic solvents, and more than 42% of its initial activity remained in 10% organic solvents. Additionally, rLac1 exhibited a more efficient decolorization ability for remazol brilliant blue R (RBBR) than for acid red 1 (AR1), crystal violet (CV), and neutral red (NR). Molecular docking results showed RBBR has a stronger binding affinity with laccase than other dyes by interacting with substrate binding cavity of enzyme. The results indicated rLac1 may be a potential candidate for dye removal from textile wastewater.

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Microbial Inoculants and Their Potential Application in Bioremediation

Puranik,

Sruthy,

Manoj

et al. 2024

Microbes Based Approaches for the Management of Hazardous Contaminants

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Characterization of a recombinant laccase from Fusarium oxysporum HUIB02 for biochemical application on dyes removal

Cited by 22 publications

References 38 publications

Photoenzymatic Activity of Artificial–Natural Bienzyme Applied in Biodegradation of Methylene Blue and Accelerating Polymerization of Dopamine

Photoenzymatic Activity of Artificial–Natural Bienzyme Applied in Biodegradation of Methylene Blue and Accelerating Polymerization of Dopamine

Characterization of a Recombinant Laccase B from Trametes hirsuta MX2 and Its Application for Decolorization of Dyes

Microbial Inoculants and Their Potential Application in Bioremediation

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