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Literature summary for 1.10.3.2 extracted from

  • Wang, Z.; Cai, Y.; Liao, X.; Zhang, F.; Zhang, D.; Li, Z.
    Production and characterization of a novel laccase with cold adaptation and high thermal stability from an isolated fungus (2009), Appl. Biochem. Biotechnol., 162, 280-294.
    View publication on PubMed
Search for more literature for 1.10.3.2

Application

Application Comment Organism
industry Pycnoporus sp. SYBC-L1 is a potential candidate for industrial application. It can be exploited for a number of industrial and environmental applications, such as paper pulping and bleaching, textile dye bleaching, bioremediation, and detoxification, overview Pycnoporus sp. (in: Fungi)
synthesis Pycnoporus sp. SYBC-L1 is a potential candidate for laccase production Pycnoporus sp. (in: Fungi)

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Pycnoporus sp. (in: Fungi)
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ activates 1.8fold at 2.0 mM Pycnoporus sp. (in: Fungi)

Organism

Organism UniProt Comment Textmining
Pycnoporus sp. (in: Fungi)
-
 isolated from a decayed Elaeocarpus sylvestris, identification
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Pycnoporus sp. (in: Fungi) SYBC-L1
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 isolated from a decayed Elaeocarpus sylvestris, identification
-

Source Tissue

Source Tissue Comment Organism Textmining
basidiocarp resupinate without stem Pycnoporus sp. (in: Fungi)
-
additional information the highest laccase activity of 24.1 U/ml, approximately 40fold than that in basal medium, is achieved in optimal culture medium in submerged fermentation, optimization, e.g. to 35°C, 2 mM Cu2+, and pH 3.5, overview Pycnoporus sp. (in: Fungi)
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,6-dimethylphenol + O2
-
 Pycnoporus sp. (in: Fungi) ?
-
 ?
2,6-dimethylphenol + O2
-
 Pycnoporus sp. (in: Fungi) SYBC-L1 ?
-
 ?
additional information the laccase can effectively decolorize two commercial wool dyes, weak acid blue AS and diamond black PV, up to 88% and 74.7%, respectively, within 2 h in the absence of any redox mediators Pycnoporus sp. (in: Fungi) ?
-
 ?
additional information the laccase can effectively decolorize two commercial wool dyes, weak acid blue AS and diamond black PV, up to 88% and 74.7%, respectively, within 2 h in the absence of any redox mediators Pycnoporus sp. (in: Fungi) SYBC-L1 ?
-
 ?

Synonyms

Synonyms Comment Organism
benzenediol-oxygen oxidoreductase
-
 Pycnoporus sp. (in: Fungi)

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
70
-
-
 Pycnoporus sp. (in: Fungi)

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
-
 100 a cold adaptation enzyme with a relative catalytic activity of 30.2% at 0°C, but also a high thermostable enzyme. About 50-70% of relative activity at 10-30°C Pycnoporus sp. (in: Fungi)

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
 half-life is 85.5 h Pycnoporus sp. (in: Fungi)
70
-
 half-life is 37.2 h Pycnoporus sp. (in: Fungi)
80
-
 half-life is 2.6 h Pycnoporus sp. (in: Fungi)
100
-
 half-life is 8.7 min Pycnoporus sp. (in: Fungi)

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4 4.5
-
 Pycnoporus sp. (in: Fungi)

pH Range

pH Minimum pH Maximum Comment Organism
3 10
-
 Pycnoporus sp. (in: Fungi)

pH Stability

pH Stability pH Stability Maximum Comment Organism
4 10 the laccase has a broad stable pH range. After 72 h incubation at 30°C, the enzyme shows a different stability pattern: the laccase activity decreases rapidly at pH 2.0, 43% remaining activity at pH 4.0 and pH 8.0, over 70% remaining activity at pH 10.0 with a half-life of more than 130 h, the laccase is more stable in an alkaline condition Pycnoporus sp. (in: Fungi)