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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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Alignment of deduced amino acid sequence of LacA with other laccases (indicated by the GenBank accession numbers).Laccases used in alignment are: Cerrena sp. HYB07 LacA: KF317949; Cerrena sp. WR1 Lcc1: ACZ58367; Cerrena sp. WR1 Lcc2: ACZ58368; Cerrena sp. WR1 Lcc3: ACZ58369; Cerrena maxima laccase chain A: 2H5U_A; Cerrena maxima laccase chain A: 3DIV_A; Cerrena sp. CTL-2011 laccase: AEL16568; Cerrena unicolor laccase: AEQ35306; Cerrena unicolor Lac1: ACL93462; Spongipellis sp. FERM P-18171 laccase 1 precursor: BAE79811; Panus rudis laccase A: AAW28932; Rigidoporus microporus laccase: ACL93333; Meripilus giganteus laccase: CBV46340; Steccherinum murashkinskyi laccase 2: AFI41889; Trametes sp. 420 laccase C: AAW28938; Coriolopsis trogii laccase: CAC13040; Pleurotus eryngii laccase: ACI62809. Four conserved copper binding domains are underlined. Conserved His residues are numbered, and conserved Cys residues are labeled.
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pone-0110834-g005: Alignment of deduced amino acid sequence of LacA with other laccases (indicated by the GenBank accession numbers).Laccases used in alignment are: Cerrena sp. HYB07 LacA: KF317949; Cerrena sp. WR1 Lcc1: ACZ58367; Cerrena sp. WR1 Lcc2: ACZ58368; Cerrena sp. WR1 Lcc3: ACZ58369; Cerrena maxima laccase chain A: 2H5U_A; Cerrena maxima laccase chain A: 3DIV_A; Cerrena sp. CTL-2011 laccase: AEL16568; Cerrena unicolor laccase: AEQ35306; Cerrena unicolor Lac1: ACL93462; Spongipellis sp. FERM P-18171 laccase 1 precursor: BAE79811; Panus rudis laccase A: AAW28932; Rigidoporus microporus laccase: ACL93333; Meripilus giganteus laccase: CBV46340; Steccherinum murashkinskyi laccase 2: AFI41889; Trametes sp. 420 laccase C: AAW28938; Coriolopsis trogii laccase: CAC13040; Pleurotus eryngii laccase: ACI62809. Four conserved copper binding domains are underlined. Conserved His residues are numbered, and conserved Cys residues are labeled.

Mentions: The deduced amino acid sequence of LacA was aligned with other fungal laccases, including 8 Cerrena laccases (Fig. 5). The LacA protein possessed four conserved copper-binding motifs typical of fungal laccases, Cu I (HWHGFFQ), Cu II (HSHLSTQ), Cu III (HPFHLHGH) and Cu IV (HCHIDWHL), as well as 10 conserved His involved in copper atom coordination and 5 conserved Cys residues. LacA was most similar to and exhibited 86% identity to the laccase 1 precursor from Spongipellis sp. FERM P-18171 (BAE79811), followed by Lac1 from Cerrena unicolor (ACL93462) with 81% identity, Lcc3 from Cerrena sp. WR1 (ACZ58369) with 78% identity and laccase from Cerrena sp. CTL-2011 (AEL16568) with 74% identity. On the other hand, LacA was more distantly related to Trametes and Pleurotus laccases (with no higher than 70% identity).


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)

Alignment of deduced amino acid sequence of LacA with other laccases (indicated by the GenBank accession numbers).Laccases used in alignment are: Cerrena sp. HYB07 LacA: KF317949; Cerrena sp. WR1 Lcc1: ACZ58367; Cerrena sp. WR1 Lcc2: ACZ58368; Cerrena sp. WR1 Lcc3: ACZ58369; Cerrena maxima laccase chain A: 2H5U_A; Cerrena maxima laccase chain A: 3DIV_A; Cerrena sp. CTL-2011 laccase: AEL16568; Cerrena unicolor laccase: AEQ35306; Cerrena unicolor Lac1: ACL93462; Spongipellis sp. FERM P-18171 laccase 1 precursor: BAE79811; Panus rudis laccase A: AAW28932; Rigidoporus microporus laccase: ACL93333; Meripilus giganteus laccase: CBV46340; Steccherinum murashkinskyi laccase 2: AFI41889; Trametes sp. 420 laccase C: AAW28938; Coriolopsis trogii laccase: CAC13040; Pleurotus eryngii laccase: ACI62809. Four conserved copper binding domains are underlined. Conserved His residues are numbered, and conserved Cys residues are labeled.
© Copyright Policy
Related In: Results  -  Collection

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

pone-0110834-g005: Alignment of deduced amino acid sequence of LacA with other laccases (indicated by the GenBank accession numbers).Laccases used in alignment are: Cerrena sp. HYB07 LacA: KF317949; Cerrena sp. WR1 Lcc1: ACZ58367; Cerrena sp. WR1 Lcc2: ACZ58368; Cerrena sp. WR1 Lcc3: ACZ58369; Cerrena maxima laccase chain A: 2H5U_A; Cerrena maxima laccase chain A: 3DIV_A; Cerrena sp. CTL-2011 laccase: AEL16568; Cerrena unicolor laccase: AEQ35306; Cerrena unicolor Lac1: ACL93462; Spongipellis sp. FERM P-18171 laccase 1 precursor: BAE79811; Panus rudis laccase A: AAW28932; Rigidoporus microporus laccase: ACL93333; Meripilus giganteus laccase: CBV46340; Steccherinum murashkinskyi laccase 2: AFI41889; Trametes sp. 420 laccase C: AAW28938; Coriolopsis trogii laccase: CAC13040; Pleurotus eryngii laccase: ACI62809. Four conserved copper binding domains are underlined. Conserved His residues are numbered, and conserved Cys residues are labeled.
Mentions: The deduced amino acid sequence of LacA was aligned with other fungal laccases, including 8 Cerrena laccases (Fig. 5). The LacA protein possessed four conserved copper-binding motifs typical of fungal laccases, Cu I (HWHGFFQ), Cu II (HSHLSTQ), Cu III (HPFHLHGH) and Cu IV (HCHIDWHL), as well as 10 conserved His involved in copper atom coordination and 5 conserved Cys residues. LacA was most similar to and exhibited 86% identity to the laccase 1 precursor from Spongipellis sp. FERM P-18171 (BAE79811), followed by Lac1 from Cerrena unicolor (ACL93462) with 81% identity, Lcc3 from Cerrena sp. WR1 (ACZ58369) with 78% identity and laccase from Cerrena sp. CTL-2011 (AEL16568) with 74% identity. On the other hand, LacA was more distantly related to Trametes and Pleurotus laccases (with no higher than 70% identity).

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