+ Site Statistics
+ Search Articles
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ PDF Full Text
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Translate
+ Recently Requested

High redox potential laccases from the ligninolytic fungi Pycnoporus coccineus and Pycnoporus sanguineus suitable for white biotechnology: from gene cloning to enzyme characterization and applications

High redox potential laccases from the ligninolytic fungi Pycnoporus coccineus and Pycnoporus sanguineus suitable for white biotechnology: from gene cloning to enzyme characterization and applications

Journal of Applied Microbiology 108(6): 2199-2213

Exploitation of natural biodiversity in species Pycnoporus coccineus and Pycnoporus sanguineus to screen for a new generation of laccases with properties suitable for the lignin-processing sector. Thirty strains originating from subtropical and tropical environments, mainly isolated from fresh specimens collected in situ, were screened for laccase activity. On the basis of levels of enzyme activity and percentage of similarity between protein sequences, the laccases from strains BRFM 938, BRFM 66 and BRFM 902 were selected for purification and characterization. Each BRFM 938, BRFM 66 and BRFM 902 laccase gene encoded a predicted protein of 518 amino acids; the three deduced proteins showed 68.7-97.5% similarity with other Polyporale laccases. The three laccases (59.5-62.9 kDa with 7-10% carbohydrate content) had high redox potentials (0.72-0.75 V vs normal hydrogen electrode at pH 6), remained highly stable up to 75-78 degrees C and at pH 5-7 mixtures, and were resistant to methyl and ethyl alcohols, acetonitrile and dimethylsulfoxide at concentrations as high as 50% (v/v). The best laccase-1-hydroxybenzotriazole systems permitted almost 100% of various polyphenolic dye decolourization and oxidation of adlerol and veratryl alcohol. The three laccases showed complementary biochemical features. BRFM 938 laccase had the highest thermo- and pH stability, catalytic efficiency towards 2,2'-azino-bis-[3-ethylthiazoline-6-sulfonate] and resistance to alcoholic solvents. BRFM 66 laccase had the highest rates of dye decolourization and oxidation of nonphenolic compounds. This study identified P. coccineus and P. sanguineus as outstanding producers of high redox potential laccases, easy to purify and scale-up for industrial production. Three new laccases proved to be suitable models for white biotechnology processes and for further molecular breeding to create a new generation of tailor-made enzymes.

(PDF emailed within 0-6 h: $19.90)

Accession: 053539844

Download citation: RISBibTeXText

PMID: 19968731

DOI: 10.1111/j.1365-2672.2009.04623.x

Related references

Cloning and characterization of a tyrosinase gene from the white-rot fungus Pycnoporus sanguineus, and overproduction of the recombinant protein in Aspergillus niger. Applied Microbiology and Biotechnology 70(5): 580-589, 2005

Structural studies of two thermostable laccases from the white-rot fungus Pycnoporus sanguineus. International Journal of Biological Macromolecules 107(Pt B): 1629-1640, 2017

Transformation of 2-hydroxydibenzofuran by laccases of the white rot fungi Trametes versicolor and Pycnoporus cinnabarinus and characterization of oligomerization products. Biodegradation 8(5): 321-328, 1997

Characterization of cellobiose dehydrogenase and its FAD-domain from the ligninolytic basidiomycete Pycnoporus sanguineus. Enzyme and Microbial Technology 53(6-7): 427-437, 2014

A High Redox Potential Laccase from Pycnoporus sanguineus RP15: Potential Application for Dye Decolorization. International Journal of Molecular Sciences 17(5): -, 2017

Properties of laccases produced by Pycnoporus sanguineus induced by 2,5-xylidine. Biotechnology Letters 28(9): 633-636, 2006

Pycnoporus sanguineus IDEA, a laccase-overproducing fungi with high potential in partial enzymatic conversion (PEC-Technology) of Venezuelan extra-heavy crude oil. Journal of Biotechnology 131(2-supp-S), 2007

Pycnoporus laccase-mediated bioconversion of rutin to oligomers suitable for biotechnology applications. Applied Microbiology and Biotechnology 90(1): 97-105, 2011

The ligninolytic system of the white rot fungus Pycnoporus cinnabarinus: purification and characterization of the laccase. Applied and Environmental Microbiology 62(4): 1151-1158, 1996

Oxidation of isoeugenol and coniferyl alcohol catalyzed by laccases isolated from Rhus vernicifera stokes and Pycnoporus coccineus. Journal of Molecular Catalysis B Enzymatic 10(6): 605-615, 1 November, 2000

Purification and characterization of laccase from Pycnoporus sanguineus and decolorization of an anthraquinone dye by the enzyme. Applied Microbiology and Biotechnology 74(6): 1232-1239, 2006

Enhanced production of thermostable laccases from a native strain of Pycnoporus sanguineus using central composite design. Journal of Zhejiang University. Science. B 15(4): 343-352, 2015

Purification and characterization of two thermostable laccases with high cold adapted characteristics from Pycnoporus sp. SYBC-L1. Process Biochemistry 45(10): 1720-1729, 2010

Characterization of a new tyrosinase from Pycnoporus species with high potential for food technological applications. Journal of Applied Microbiology 98(2): 332-343, 2005

Evaluation of the aggressiveness of wood decaying fungi: laboratory tests with Pycnoporus sanguineus (fungi, Basidiomycetes). Anales del Instituto de Biologia Universidad Nacional Autonoma de Mexico, Botanica 1987; 54: 227-232, 1983