Purified Coprinus laccases and nucleic acids encoding same

Details Purified Coprinus laccases and nucleic acids encoding same Purified Coprinus laccases and nucleic acids encoding same

1998-10-28

2001-06-05

Slobodyansky, Elizabeth (Department: 1652)

Chemistry: molecular biology and microbiology

Enzyme , proenzyme; compositions thereof; process for...

Oxidoreductase

C435S041000, C435S254100, C435S190000

Reexamination Certificate

active

06242232

ABSTRACT:

BACKGROUND OF THE INVENTION
1. Field of the Invention
The present invention relates to polypeptides having laccase activity and isolated nucleic acid sequences encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the nucleic acid sequences as well as methods for producing the polypeptides.
2. Description of the Related Art
Laccases (benzenediol:oxygen oxidoreductases) are multi-copper containing enzymes that catalyze the oxidation of phenolics. Laccase-mediated oxidations result in the production of aryloxy-radical intermediates from suitable phenolic substrate; the ultimate coupling of the intermediates so produced provides a combination of dimeric, oligomeric, and polymeric reaction products. Such reactions are important in nature in biosynthetic pathways which lead to the formation of melanin, alkaloids, toxins, lignins, and humic acids. Laccases are produced by a wide variety of fungi, including ascomycetes such as Aspergillus, Neurospora, and Podospora, the deuteromycete Botrytis, and basidiomycetes such as Collybia, Fomes, Lentinus, Pleurotus, Trametes, and perfect forms of Rhizoctonia. Laccase exhibits a wide range of substrate specificity, and each different fungal laccase usually differs only quantitatively from others in its ability to oxidize phenolic substrates. Because of the substrate diversity, laccases generally have found many potential industrial applications. Among these are lignin modification, paper strengthening, dye transfer inhibition in detergents, phenol polymerization, juice manufacture, phenol resin production, and waste water treatment.
Although the catalytic capabilities are similar, laccases made by different fungal species do have different temperature and pH optima. A number of these fungal laccases have been isolated, and the genes for several of these have been cloned. For example, Choi et al. (1992
, Mol. Plant
-
Microbe Interactions
5: 119-128) describe the molecular characterization and cloning of the gene encoding the laccase of the chestnut blight fungus Cryphonectria parasitica. Kojima et al. (1990
, Journal of Biological Chemistry
265: 15224-15230; JP 2-238885) provide a description of two allelic forms of the laccase of the white-rot basidiomycete
Coriolus hirsutus
. Gerrnann and Lerch (1985
, Experientia
41: 801; 1986
, Proceedings of the National Academy of Sciences
USA 83: 8854-8858) have reported the cloning and partial sequencing of the
Neurospora crassa
laccase gene. Saloheimo et al. (1985
, Journal of General Microbiology
137:1537-1544; WO 92/01046) have disclosed a structural analysis of the laccase gene from the fungus
Phlebia radiata.
It is an object of the present invention to provide polypeptides having laccase activity and nucleic acid constructs encoding these polypeptides.
SUMMARY OF THE INVENTION
The present invention relates to isolated polypeptides having laccase activity, obtained from a Coprinus strain. The present invention further relates to isolated polypeptides having laccase activity which have: (a) a pH optimum in the range of about 5 to about 9 at 20° C. using syringaldazine as a substrate; and (b) an isoelectric point in the range of about 3.7 to about 4.0. The present invention also relates to isolated polypeptides which have an amino acid sequence which has at least 65% identity with the amino acid sequence set forth in SEQ ID NO:27, SEQ ID NO:29, or SEQ ID NO:33.
The present invention further relates to isolated nucleic acid sequences encoding the and to nucleic acid constructs, vectors, and host cells comprising the nucleic acid sequences as well as methods for producing the polypeptides.


REFERENCES:
patent: WO 91/05839 (1991-05-01), None
patent: WO 92/18683 (1992-10-01), None
patent: WO 92/18687 (1992-10-01), None
patent: WO 96/00290 (1996-01-01), None
patent: WO 96/06930 (1996-03-01), None
Abstract, Kyowa Hakko Kogyo K.K., Takemitsu Arai, “Preparation of Laccase”, 60-156385, vol. 9, No. 324 (C-320).
Giardina et al., “The Gene, Protein And Glycam Structures Of Laccase From Pleurotus Ostreatus”, Eur. J. Biochem 235., pp. 508-515, 1996.
Kojima et al., The Journal of Biological Chemistry, Inc., vol. 265, No. 25.
Kim et al., “Selection Of Laccase Over-Secreting Mutant In Coprinus Congregatus”, Jour. Microbiol., Jun. 1995, pp. 146-148.

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