View in EDS

Proteins having tyrosinase activity

Saved in:
Bibliographic Details
Title: Proteins having tyrosinase activity
Patent Number: 7,910,344
Publication Date: March 22, 2011
Appl. No: 11/815988
Application Filed: February 09, 2006
Abstract: Extracellular tyrosinases obtainable from Trichoderma spp. and methods for producing them by recombinant technology. The enzymes are particularly useful in cross-linking food proteins.
Inventors: Kruus, Kristiina (Espoo, FI); Selinheimo, Emilia (Espoo, FI); Autio, Karin (Espoo, FI); Buchert, Johanna (Espoo, FI); Saloheimo, Markku (Helsinki, FI); Lantto, Raija (Klaukkala, FI)
Assignees: Valtion teknillinen tutkimuskeskus (Espoo, FI)
Claim: 1. An isolated protein comprising an amino acid sequence having at least 95% identity to residues 19-410 of SEQ ID NO: 4, wherein said amino acid sequence has tyrosinase activity.
Claim: 2. The isolated protein of claim 1 , obtained from Trichoderma spp.
Claim: 3. The isolated protein of claim 1 comprising a signal sequence at the N-terminal end.
Claim: 4. The isolated protein of claim 1 consisting of amino acids 19-410 of SEQ ID NO: 4.
Claim: 5. The isolated protein of claim 1 , wherein the isolated protein is encoded by a polynucleotide obtainable from DNA of Trichoderma spp. by amplification with the primer pair having the sequences set forth in SEQ ID NO:7 and SEQ ID NO:8.
Claim: 6. The isolated protein of claim 1 , wherein the isolated protein is encoded by a polynucleotide obtainable from Trichoderma reesei.
Claim: 7. The isolated protein of claim 1 , wherein the isolated protein is encoded by a polynucleotide comprising the sequence as set forth in SEQ ID NO:2.
Claim: 8. The isolated protein of claim 1 comprising the amino acid sequence as set forth in SEQ ID:4.
Claim: 9. The isolated protein of claim 1 wherein the amino acid sequence is a tyrosinase active fragment of the amino acid sequence as set forth in SEQ ID NO:4.
Claim: 10. The isolated protein of claim 1 having a molecular weight of about 42.9 kDa, a pI of about 9, a pH optimum at about 8-8.5, and tyrosinase activity at alkaline or neutral pH.
Claim: 11. A protein obtained by a method comprising: a) inserting into a host cell a DNA sequence encoding an extracellular tyrosinase, wherein said DNA sequence is obtainable from Trichoderma spp. DNA by amplification with the primer pair having the sequences as set forth in SEQ ID NO: 7 and SEQ ID NO: 8, b) growing said host cell in growth medium under conditions suitable for expression and secretion of the protein, and c) recovering the secreted protein from the growth medium, and optionally purifying the protein, wherein the protein comprises an amino acid sequence having at least 95% identity to residues 19-410 of SEQ ID NO: 4, said amino acid sequence having tyrosinase activity.
Claim: 12. An enzyme preparation comprising the isolated protein of claim 1 .
Current U.S. Class: 435/189
Patent References Cited: 5340734 August 1994 Della-Cioppa et al.
6242221 June 2001 Robinson
10174586 June 1998
2001157586 June 2001
2004201545 July 2004
0214595 February 2002
03007728 January 2003
Other References: Van Gelder et al, Sequence and structural features of plant and fungal tyrosinases. Phytochemistry. Aug. 1997;45(7):1309-23. cited by examiner
Galye et al, Identification of regions in interleukin-1 alpha important for activity. J Biol Chem. Oct. 15, 1993; 268(29):22105-11. cited by examiner
Whisstock et al, Prediction of protein function from protein sequence and structure. Q Rev Biophys. Aug. 2003;36(3):307-40. Review. cited by examiner
EST database Acc. No. CF871153 Oct. 31, 2003 from Diener et al, FEMS Microbiol Lett 230(2) (2004) 275-282. Alignment with Seq Id No. 4. cited by examiner
Chang et al, Dissecting Intracellular Signaling Pathways with Membrane-Permeable Peptides Sci. STKE, Aug. 29, 2000 vol. 2000, Issue 47, p. 1-11. cited by examiner
“Shiitake mushroom tyrosinase enzyme”, Dec. 18, 2001, XP002484520, Database accession No. AAG67089. cited by other
“Shiitake tyrosinase protein sequence”, Sep. 17, 1998, XP002484521, Database accession No. AAW62552. cited by other
“Aspergillus oryzae meID protein SeqID1”, Oct. 7, 2004, XP002484522, Database accession No. ADQ58743. cited by other
“Tobacco polyphenol oxidase partial polypeptide TOBPPO25”, Jun. 21, 1999, XP002484523, Database accession No. AAW97991. cited by other
“Tobacco polyphenol oxidase GTP01”, Mar. 23, 1998, XP002484662, Database accession No. AAW23666. cited by other
Selinheimo Emilia et al., “Production and characterization of a secreted, C-terminally processed tyrosinase from the filamentous fungus Trichoderma reesei”, Sep. 2006, The Febs Journal Sep. 2006, pp. 4322-4335. cited by other
European search report in corresponding EP 06708959. cited by other
Halaouli S et al. Characterization of a new tyrosinase from Pycnoporus species with high potential for food technological applications. Journal of Applied Microbiology, Feb. 2005, vol. 98, issue 2, pp. 332-343, the whole document. cited by other
Database EMBL [Online] Aug. 16, 2005 Birren B W et al: “Hypothetical protein” retrieved fro EBI, Database accession No. Q4IAY0 50% identity with Seq Id No. 3 in 607 aa overlap (6-602:4-554). cited by other
Database EMBL [Online] Aug. 16, 2005 Birren B W et al.: “Hypothetical protein” retrieved from EBI, Database accession No. Q4HZT6 47% identity with Seq Id No. 4 in 560 aa overlap (2-557:15-550). cited by other
Score et al “extracellular phenoloxidase and oeroxidase enzyme production during interspesific fungal interactions”. Int. Biodeterioration and Biodegradation vol. 39, No. 2-3, 1997. s. 225-233. (tiivistelma, taulukko 1 ja 2, 228). cited by other
Mackie et al. “Effects and incidence of volatile organic compound interactions between bacterial and fungal isolates”. Soil Biology and Biochemistry. vol. 31, 1999. s. 375-385. (tiivistelma, taulukko 1) . cited by other
Obata et al. Cloning of novel tyrosinase-enciding gene (melB) from Aspergillus oryzae and its overexpression in solid-state culture (rice koji). Journal of Bioscience vol. 97, No. 6, 2004. s. 400-405. cited by other
NCBI/GenBank AN: BAD51402. “Photo-regulated tyrosinase gene in Polyporus arcularius”. Morinaga Sep. 17, 2003. cited by other
NCBI/GenBank AN AAB07484. “Molecular and functional characterization of the tyrosinase gene of the filamentous fungus Podospora anserina”. Marbach et al., Aug. 8, 1996. cited by other
Primary Examiner: Swope, Sheridan
Attorney, Agent or Firm: Young & Thompson
Accession Number: edspgr.07910344
Database: USPTO Patent Grants
Description
Abstract:Extracellular tyrosinases obtainable from Trichoderma spp. and methods for producing them by recombinant technology. The enzymes are particularly useful in cross-linking food proteins.