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Purification and characterization of a novel laccase from Cerrena sp. HYB07 with dye decolorizing ability.

Yang J, Lin Q, Ng TB, Ye X, Lin J - PLoS ONE (2014)

Bottom Line: Its gene and cDNA sequences were obtained.Putative cis-acting transcriptional response elements were identified in the promoter region.The high production yield and activity, robustness and dye decolorizing capacity make LacA and Cerrena sp.

View Article: PubMed Central - PubMed

Affiliation: College of Biological Sciences and Technology, Fuzhou University, Fuzhou, Fujian, China; National Engineering Laboratory for Enzyme Expression, Fuzhou, Fujian, China.

ABSTRACT
Laccases (EC 1.10.3.2) are a class of multi-copper oxidases with important industrial values. A basidiomycete strain Cerrena sp. HYB07 with high laccase yield was identified. After cultivation in the shaking flask for 4 days, a maximal activity of 210.8 U mL(-1) was attained. A 58.6-kDa laccase (LacA) with 7.2% carbohydrate and a specific activity of 1952.4 U mg(-1) was purified. 2,2'-Azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) was the optimal substrate, with Km and kcat being 93.4 µM and 2468.0 s(-1), respectively. LacA was stable at 60°C, pH 5.0 and above, and in organic solvents. Metal ions Na+, K+, Ca2+, Mg2+, Mn2+, Zn2+ enhanced LacA activity, while Fe2+ and Li+ inhibited LacA activity. LacA decolorized structurally different dyes and a real textile effluent. Its gene and cDNA sequences were obtained. Putative cis-acting transcriptional response elements were identified in the promoter region. The high production yield and activity, robustness and dye decolorizing capacity make LacA and Cerrena sp. HYB07 potentially useful for industrial and environmental applications such as textile finishing and wastewater treatment.

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Effects of pH and temperature on activity and stability of LacA.(A) Effect of pH on LacA activity with ABTS, guaiacol, 2,6-DMP and catechol as substrates. (B) Effect of pH on LacA stability with ABTS as substrate. (C) Effect of temperature on LacA activity with ABTS, guaiacol, 2,6-DMP and catechol as substrate. (D) Effect of temperature on LacA stability with ABTS as substrate. Bars indicate standard deviations of triplicate determinations.
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pone-0110834-g003: Effects of pH and temperature on activity and stability of LacA.(A) Effect of pH on LacA activity with ABTS, guaiacol, 2,6-DMP and catechol as substrates. (B) Effect of pH on LacA stability with ABTS as substrate. (C) Effect of temperature on LacA activity with ABTS, guaiacol, 2,6-DMP and catechol as substrate. (D) Effect of temperature on LacA stability with ABTS as substrate. Bars indicate standard deviations of triplicate determinations.

Mentions: The pH optimum was 3.0 for ABTS and 2,6-DMP, 4.0 for guaiacol and 4.5 for catechol (Fig. 3A). After storage at pH 4.0 for 105 h, 56% residual enzyme activity was retained. At pH 5.0 or higher, >80% activity remained. In contrast, LacA activity decreased to only approximately 1% and 20% at the end of 105-h incubation at pH 2.0 and 3.0, with t1/2 being 18 h and 43 h, respectively (Fig. 3B).


Purification and characterization of a novel laccase from Cerrena sp. HYB07 with dye decolorizing ability.

Yang J, Lin Q, Ng TB, Ye X, Lin J - PLoS ONE (2014)

Effects of pH and temperature on activity and stability of LacA.(A) Effect of pH on LacA activity with ABTS, guaiacol, 2,6-DMP and catechol as substrates. (B) Effect of pH on LacA stability with ABTS as substrate. (C) Effect of temperature on LacA activity with ABTS, guaiacol, 2,6-DMP and catechol as substrate. (D) Effect of temperature on LacA stability with ABTS as substrate. Bars indicate standard deviations of triplicate determinations.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4214704&req=5

pone-0110834-g003: Effects of pH and temperature on activity and stability of LacA.(A) Effect of pH on LacA activity with ABTS, guaiacol, 2,6-DMP and catechol as substrates. (B) Effect of pH on LacA stability with ABTS as substrate. (C) Effect of temperature on LacA activity with ABTS, guaiacol, 2,6-DMP and catechol as substrate. (D) Effect of temperature on LacA stability with ABTS as substrate. Bars indicate standard deviations of triplicate determinations.
Mentions: The pH optimum was 3.0 for ABTS and 2,6-DMP, 4.0 for guaiacol and 4.5 for catechol (Fig. 3A). After storage at pH 4.0 for 105 h, 56% residual enzyme activity was retained. At pH 5.0 or higher, >80% activity remained. In contrast, LacA activity decreased to only approximately 1% and 20% at the end of 105-h incubation at pH 2.0 and 3.0, with t1/2 being 18 h and 43 h, respectively (Fig. 3B).

Bottom Line: Its gene and cDNA sequences were obtained.Putative cis-acting transcriptional response elements were identified in the promoter region.The high production yield and activity, robustness and dye decolorizing capacity make LacA and Cerrena sp.

View Article: PubMed Central - PubMed

Affiliation: College of Biological Sciences and Technology, Fuzhou University, Fuzhou, Fujian, China; National Engineering Laboratory for Enzyme Expression, Fuzhou, Fujian, China.

ABSTRACT
Laccases (EC 1.10.3.2) are a class of multi-copper oxidases with important industrial values. A basidiomycete strain Cerrena sp. HYB07 with high laccase yield was identified. After cultivation in the shaking flask for 4 days, a maximal activity of 210.8 U mL(-1) was attained. A 58.6-kDa laccase (LacA) with 7.2% carbohydrate and a specific activity of 1952.4 U mg(-1) was purified. 2,2'-Azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) was the optimal substrate, with Km and kcat being 93.4 µM and 2468.0 s(-1), respectively. LacA was stable at 60°C, pH 5.0 and above, and in organic solvents. Metal ions Na+, K+, Ca2+, Mg2+, Mn2+, Zn2+ enhanced LacA activity, while Fe2+ and Li+ inhibited LacA activity. LacA decolorized structurally different dyes and a real textile effluent. Its gene and cDNA sequences were obtained. Putative cis-acting transcriptional response elements were identified in the promoter region. The high production yield and activity, robustness and dye decolorizing capacity make LacA and Cerrena sp. HYB07 potentially useful for industrial and environmental applications such as textile finishing and wastewater treatment.

Show MeSH
Related in: MedlinePlus