Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase
Reexamination Certificate
2006-05-23
2006-05-23
Nashed, Nashaat T. (Department: 1656)
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Hydrolase
C435S197000, C435S196000, C435S440000, C435S135000, C426S533000
Reexamination Certificate
active
07049122
ABSTRACT:
The present invention provides mutant-type lipases which demonstrate superior lipolytic and esterific activities. The mutant-type lipases are characterized by an amino acid alteration at the residue immediately followed either the serine residue or the histidine residue or both residues of the Ser-His-Asp catalytic triad. The Ser-His-Asp catalytic triad is known to be the three residues, although occur far apart in the amino acid sequence of a lipase, that contribute to the hydrolytic activity in the active site of the lipase. The amino acid residue that follows the serine residue of the Ser-His-Asp catalytic triad is alanine. The amino acid residue that follows the histidine residue of the Ser-His-Asp catalytic triad is isoleucine. The wild-type lipase is preferably originated fromStaphylococcus,particularlyStaphylococcus epidermindis. The present invention also relates to a method for preparing the mutant-type lipases by site-directed mutagenesis using PCR and a method for utilizing the mutant-type lipase to catalyze synthesis of flavor esters to be used in food industry.
REFERENCES:
Wallace, A. et al.; Derivation of 3D coordinate templates for searching structural databases: Application to Ser-His-Asp catalytic triads in the serine proteinases and lipases; Protein Science, vol. 5, p. 1001-1013, (1996).
Sharrocks, A. et al.; Improved primer design for PCR-based, site-directed mutagenesis; Nucleic Acids Research, vol. 20, No. 5, p. 1147, (1992).
Chang, R. et al.; Synthesis of Fatty Acid Esters by RecombinantStaphylococcus epidermidisLipases in Aqueous Environment; Journal of Agricultural and Food Chemistry, vol. 49, No. 5, p. 2619-2622, (2001).
Chang, R. et al.; Site-Directed Mutagenesis of a Highly ActiveStaphylococcus epidermidisLipases Fragment Identifies Residues Essential for Catalysis; Journal of American Oil Chemists' Society, vol. 77, No. 10, p. 1021-1025, (2000).
Simons, J. et al.; Cloning, purification and charaterisation of the lipase fromStaphylococcus epidermidis—Comparison of the substrate selectivity with those of other microbial lipases; Eur. J. Biochem, vol. 253, p. 675-683, (1998).
Farrell, A. et al.; Molecular analysis and expression of the lipase ofStaphylococcus epidermidis; Journal of General Microbiology, vol. 139, p. 267-277, (1993).
Talon, R. et al.; Production of flavor esters by lipases ofStaphylococcus warneriandStaphylococcus xylosus; Enzyme and Microbial Technology, vol. 19, p. 620-622, (1996).
Chang Rey-Chang
Chou Shu-Jen
Shaw Jei-Fu
Academia Sinica
Bingham & McCutchen LLP
Chao Fei-Fei
Nashed Nashaat T.
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