Chemistry: molecular biology and microbiology – Micro-organism – per se ; compositions thereof; proces of... – Bacteria or actinomycetales; media therefor
Reexamination Certificate
2005-10-14
2011-10-04
Fronda, Christian (Department: 1652)
Chemistry: molecular biology and microbiology
Micro-organism, per se ; compositions thereof; proces of...
Bacteria or actinomycetales; media therefor
C435S183000, C435S320100, C536S023200
Reexamination Certificate
active
08030053
ABSTRACT:
An improved hydroxynitrile lyase characterized by having a mutation of substitution of at least one amino acid residue in the amino acid sequence of a wild-type hydroxynitrile lyase with another amino acid and by its hydroxynitrile lyase activity per transformant being higher than the hydroxynitrile lyase activity per transformant into which the wild-type hydroxynitrile lyase gene is introduced; and a method for producing a hydroxynitrile lyase, comprising expressing the improved hydroxynitrile lyase in a host and recovering the improved hydroxynitrile lyase from the resultant culture.
REFERENCES:
patent: 0 969 095 (2000-01-01), None
patent: 1 033 405 (2000-09-01), None
patent: WO 97/03204 (1997-01-01), None
patent: WO 97/03204 (1997-01-01), None
patent: 01 48178 (2001-07-01), None
patent: WO 03/016551 (2003-02-01), None
patent: WO 2004/083424 (2004-09-01), None
patent: 2005 095602 (2005-10-01), None
Chica et al. Curr Opin Biotechnol. Aug. 2005;16(4):378-84.
Sen et al. Appl Biochem Biotechnol. Dec. 2007;143(3):212-23.
Gonghong Yan, et al., “A Single Residual Replacement Improves the Folding and Stability of Recombinant Cassava Hydroxynitrile Lyase inE. coli”, Biotechnology Letters, vol. 25, No. 13, pp. 1041-1047, 2003.
PH.-Herve Hirel, et al., “Extent of N-Terminal Methionine Excision FromEscherichia coliProteins is Governed by the Side-Chain Length of the Penultimate Amino Acid”, Proc. Natl. Acad. Sci. USA, vol. 86, No. 21, pp. 8247-8251, 1989.
Alexander Varshavsky, “The N-End Rule: Functions, Mysteries, Uses”, Proc. Natl. Acad. Sci. USA, vol. 93, No. 22, pp. 12142-12149, 1996.
Holger Bühler, et al., “Substrate Specificity of Mutants of the Hydroxynitrile Lyase fromManihot esculenta”, ChemBioChem: A European Journal of Chemical Biology, vol. 4, No. 2-3, XP 002462622, ISSN: 1439-4227, Mar. 3, 2003, pp. 211-216.
R. Weis, et al., “Biocatalytic conversion of unnatural substrates by recombinant almondR-HNL isoenzyme 5”, Journal of Molecular Catalysis B: Enzymatic, Elsevier, vol. 29, No. 1-6, XP 002382495, ISSN: 1381-1177, Jun. 21, 2004, pp. 211-218.
Extended European Search Report issued Sep. 20, 2010, European Patent Application No. 10171423.6.
Database Geneseq, “Manihot esculentaS-acetone-cyanohydrin lyase protein”, Nov. 20, 2003, XP002600065.
Database UniProt, “SubName: Full=Alpha-hydroxynitrile lyase”, Jun. 1, 1998, XP00260066.
Database Geneseq, “Hevea brasiliensis(S)-hydroxynitrilase”, Jan. 9, 1998, XP002600067.
European Search Report issued Oct. 20, 2010, European Patent Application No. 10171421.0.
Akiyama Takanori
Asano Yasuhisa
Sato Eiji
Yu Fujio
Fronda Christian
Mitsubishi Rayon Co. Ltd.
Oblon, Spivak McClelland, Maier & Neustadt, L.L.P.
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