Isolated polypeptide having arabinofuranosidase activity

Details Isolated polypeptide having arabinofuranosidase activity Isolated polypeptide having arabinofuranosidase activity

2004-05-28

2010-02-23

Fronda, Christian L (Department: 1652)

Chemistry: molecular biology and microbiology

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

Hydrolase

C435S183000, C435S252300, C435S320100, C435S484000, C510S320000, C536S023200

Reexamination Certificate

active

07666648

ABSTRACT:
Described herein are novel gene sequences isolated fromTrichoderma reesei. Two genes encoding proteins comprising a cellulose binding domain, one encoding an arabionfuranosidase and one encoding an acetylxylanesterase are described. The sequences, CIP1 and CIP2, contain a cellulose binding domain. These proteins are especially useful in the textile and detergent industry and in pulp and paper industry.cip1 cDNA sequence (SEQ ID NO: 1)GACTAGTTCA TAATACAGTA GTTGAGTTCA TAGCAACTTC50ACTCTCTAGCTGAACAAATT ATCTGCGCAA ACATGGTTCG CCGGACTGCT100CTGCTGGCCCTTGGGGCTCT CTCAACGCTC TCTATGGCCC AAATCTCAGA150CGACTTCGAGTCGGGCTGGG ATCAGACTAA ATGGCCCATT TCGGCACCAG200ACTGTAACCAGGGCGGCACC GTCAGCCTCG ACACCACAGT AGCCCACAGC250GGCAGCAACTCCATGAAGGT CGTTGGTGGC CCCAATGGCT ACTGTGGACA300CATCTTCTTCGGCACTACCC AGGTGCCAAC TGGGGATGTA TATGTCAGAG350CTTGGATTCGGCTTCAGACT GCTCTCGGCA GCAACCACGT CACATTCATC400ATCATGCCAGACACCGCTCA GGGAGGGAAG CACCTCCGAA TTGGTGGCCA450AAGCCAAGTTCTCGACTACA ACCGCGAGTC CGACGATGCC ACTCTTCCGG500ACCTGTCTCCCAACGGCATT GCCTCCACCG TCACTCTGCC TACCGGCGCG550TTCCAGTGCTTCGAGTACCA CCTGGGCACT GACGGAACCA TCGAGACGTG600GCTCAACGGCAGCCTCATCC CGGGCATGAC CGTGGGCCCT GGCGTCGACA650ATCCAAACGACGCTGGCTGG ACGAGGGCCA GCTATATTCC GGAGATCACC700GGTGTCAACTTTGGCTGGGA GGCCTACAGC GGAGACGTCA ACACCGTCTG750GTTCGACGACATCTCGATTG CGTCGACCCG CGTGGGATGC GGCCCCGGCA800GCCCCGGCGGTCCTGGAAGC TCGACGACTG GGCGTAGCAG CACCTCGGGC850CCGACGAGCACTTCGAGGCC AAGCACCACC ATTCCGCCAC CGACTTCCAG900GACAACGACCGCCACGGGTC CGACTCAGAC ACACTATGGC CAGTGCGGAG1000GGATTGGTTACAGCGGGCCT ACGGTCTGCG CGAGCGGCAC GACCTGCCAG1050GTCCTGAACCCATACTACTC CCAGTGCTTA TAAGGGGATG AGCATGGAGT1100GAAGTGAAGTGAAGTGGAGA GAGTTGAAGT GGCATTGCGC TCGGCTGGGT1150AGATAAAAGTCAGCAGCTAT GAATACTCTA TGTGATGCTC ATTGGCGTGT1200ACGTTTTAAAAAAAAAAAAA AAAAAAAAAA AAAAAAAAAA AAAAAAAAAA1250AAAAAAAAAAAAAAAAAAAG GGGGCGGCCG C1271

REFERENCES:
patent: 4797361 (1989-01-01), Montenecourt
patent: 5246856 (1993-09-01), Gaarslev
patent: 5475101 (1995-12-01), Ward et al.
patent: 6268328 (2001-07-01), Mitchinson et al.
patent: 6486112 (2002-11-01), Bettiol et al.
patent: 0507369 (1992-10-01), None
patent: WO92/06209 (1992-04-01), None
patent: WO94/28117 (1994-12-01), None
patent: WO 95/16782 (1995-06-01), None
patent: WO 96/06935 (1996-03-01), None
patent: WO 97/13853 (1997-04-01), None
patent: WO98/31821 (1998-07-01), None
patent: WO 01/46357 (2001-06-01), None
patent: WO 03/031477 (2003-04-01), None
patent: WO 2005/030998 (2005-04-01), None
Chica et al. Curr Opin Biotechnol. Aug. 2005;16(4):378-84.
Nogawa et al. Appl Environ Microbiol. Sep. 1999;65(9): 3964-8.
Sen et al. Appl Biochem Biotechnol. Dec. 2007;143(3):212-23.
Tsujibo et al. Accession JC7820. Jun. 3, 2002.
Tsujibo et al. Biosci Biotechnol Biochem. Feb. 2002;66(2):434-8.
Biely, P., et al. “Acetyl Xylan Esterases in Fungal Cellulolytic Systems.”FEBS Letters, vol. 186, No. 1, pp. 80-84, Jul. 1985.
Database EMBL Oct. 15, 1999 “Aspergillus sojaearfmRNA for alpha-L-arabinofuranosidase, complete cds.” Database accession No. AB033289.
Database EMBL Feb. 6, 2002, “TrEST-A4294 TrEST-AHypocrea jecorinacDNA clone Tr-A4294 5′ similar to hypothetical protein [Neurospora crassa], mRNA sequence.” Database accession No. BM077051.
Database EMBL Apr. 26, 2003 “T. reeseimycelial culcture, Version 3 aprilHypocrea jecorinacDNA clone tric018xa22, mRNA sequence.” Database accession No. CB899258.
Database EMBL Apr. 26, 2003, “T. reeseimycelial culture, Version 3 aprilHypocrea jecorinacDNA clone tric028xe15, mRNA sequence.” Database accession No. CB901909.
Database EMBL Apr. 26, 2003, “T. reeseimycelial culture, Version 3 aprilHypocrea jecorinacDNA clojne tric035xa22 mRNA sequence.” Database accession No. CB903527.
Database EMBL Apr. 26, 2003 “T. reeseimycelial culcture, Version 3 aprilHypocrea jecorinacDNA clone tric030xn12 mRNA sequence.” Database accession No. CB902576.
Database EMBL Apr. 26, 2003 “T. reeseimycelial culcture, Version 3 aprilHypocrea jecorinacDNA clone tric082xo13, mRNA sequence.” Database accession No. CB907643.
Database Geneseq Mar. 13, 2001 “Trichoderma reeseiEST Seq ID No. 7425.” Database accession No. AAF14902.
Foreman, P.K., et al. “Transcriptional regulation of biomass-degrading enzymes in the filamentous fungusTrichoderma reesei.” J. Biolog. Chem., vol. 278, No. 34, pp. 31988-31997, Aug. 22, 2003.
Gutierrez, R., et al. “Acetyl xylan esterase II fromPenicillium purporogenumis similar to an esterase fromTrichoderma reeseibut lacks a cellulose binding domain.”FEBS Letters, vol. 423, No. 1, pp. 35-38, Feb. 13, 1998.
Li, X-L., et al. “Identification of genes encoding microbial glucuronoyl esterases.”FEBS Letters, vol. 581, No. 21, pp. 4029-4035, Aug. 10, 2007.
Margolles-Clark, E. et al. “Acetyl xylan esterase fromTrichoderma reeseicontains an active-site serine residue and a cellulose-binding domain.”Eur. J. Biochem., vol. 237, No. 3, pp. 553-560, May 1, 1996.
Margolles-Clark, E., et al. “Cloning of genes encoding alpha-L-arabinofuranosidase and beta-xylosidase fromTrichoderma reeseiby expression inSaccharomyces cerevisiae.” Appl. Environ. Microbiol, vol. 62, No. 10, pp. 3840-3846, Oct. 1996.
Nogawa, M., et al., “An alpha-L-arabinofurnosidase fromTrichoderma reeseicontaining a noncatalytic xylan-binding domain.”Appl. Environ. Microbiol, vol. 65. No. 9, pp. 3964-3968, Sep. 1999.
Ouyang, J., et al. “A complete protein pattern of cellulase and meicellulase genes in the filamentous fungusTrichoderma reesei.” Biotech. J., vol. 1, No. 11, pp. 1266-1274, Nov. 2006.
Poutanen, K. et al. “Deacetylation of Xylans by Acetyl Esterases ofTrichoderma reesei.” Appl. Microbiol. Biotechnol., vol. 33, No. 5, pp. 506-510, 1990.
Saha, B., et al. “Alpha-L-arabinofuranosidases: Biochemistry, molecular biology and application in biotechnology.”Biotech. Advanc., vol. 18, No. 5, pp. 403-423, Aug. 2000.
Sundberg, M., et al. “Purification and Properties of Two Acetylxylan esterases ofTrichoderma reesei.” Biotech. and Appl. Biochem., vol. 13, No. 1, pp. 1-11, 1991.
Altschul, S. F., et al., Nucleic Acids Res. 25:3389-3402, 1997.
Aro et al., J. Biol. Chem., 10.1074/ M003624200, Apr. 13, 2001.
Aubert, J. P. et al., Academic Press, pp. 71-86, 1988 and Ilmen, M. et al., Appl.
Ausubel FM et al., Current Protocols in Molecular Biology, John Wiley & Sons, New York, N.Y., 1993.
Ausubel et al., eds.,Current Protocols in Molecular Biology(1994)).
Ausubel, et al., ed. Greene Publishing and Wiley-Interscience, New York (1987.
Bennett, J.W. and Lasure, L.L. (eds.) More Gene Manipulations in Fungi. Academic Press, pp. 396-428( Sep. 1991).
Bhikhabhai et al., J. Appl. Biochem. 6:336, 1984.
Brumbauer, et al., Bioseparation 7:287-295, 1999).
Davies, G. and Henrissat, B. Structures and mechanisms of glycosyl hydrolases, Biochem.J. 280 309-316 (1991).
Deutscher, Methods Enzymol. 182:779-80, 1990; Scopes, Methods Enzymol. 90 Pt E:479-90, 1982.
Ellouz et al., J. Chromatography 396:307, 1987.
Fliess et al., Eur. J. Appl. Microbiol. Biotechnol. 17:314, 1983.
Goedegebuur et al, Curr. Genet (2002) 41: 89-98.
Goyal et al., Bioresource Technol. 36:37, 1991.
Hale & Marham, The Harper Collins Dictionary of Biology, Harper Perennial, NY (1991).
Hu et al., Mol Cell Biol. 11:5792-9, 1991.
Henrissat, B. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem.J. 293 781-788 (1993).
Henrissat, B. and Bairoch, A. Updating the sequence-based classification of glycosyl hydrolases; Structure 3 853-859 (1995).
Kriegler,Gene Transfer and Expression: A Laboratory Manual(1990.
Krishna et al., Bioresource Tech. 77:193-196, 2001.
Medve et al., J. Chromatography A 808:153, 1998.
Ohmiya et al., Biotechnol. Gen. Engineer. Rev. 14:365-414, 1997.
Pourquie, J. et al., Biochemistry and Genetics of Cellulose Degradation, eds,

Affiliated with

Also associated with

Rating

Isolated polypeptide having arabinofuranosidase activity does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Isolated polypeptide having arabinofuranosidase activity, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Isolated polypeptide having arabinofuranosidase activity will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-4151368