Recombinant kid pregastric esterase and methods for its...

Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase

Reexamination Certificate

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C435S196000, C435S197000, C435S252300, C435S320100, C530S350000, C536S023200

Reexamination Certificate

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06582948

ABSTRACT:

Throughout this specification, various references are identified by a number in parantheses. The citation to the reference corresponding to the identified number can be found in the section entitled References Cited preceding the claims. The references in that section are hereby incorporated by reference.
BACKGROUND OF THE INVENTION
Esterases (also referred to as lipases) are enzymes that cleave triglycerides (fats or lipids) or esters into carboxylic acids (fatty acids) and mono- and di-glycerides. For an explanation of the slightly different definitions given to lipases and esterases see Siezen, R. J. and van den Berg, (37). A pregastric esterase is an esterolytic or lipolytic enzyme secreted by the oral tissues of mammals. Animal esterases in an unpurified form called rennet have been used in the production of dairy food products and, in particular, the production of enzyme modified cheeses or EMCs. (8), (9), (10), (17), (18), (33),. (40), and (41). In particular, cheeses like Romano and Provolone have a “peppery” or “piccante” flavor due to the fatty acid composition created by the enzyme in the rennet paste. (26), (37).
Traditionally EMCs are prepared by esterases obtained from the gullet of slaughtered animals from which a rennet paste or powder is obtained. The rennet is used to treat whey to impart flavor into the cheese product. Kid pregastric estersase (kPGE or kid PGE) in rennet paste is contaminated with proteins which are found in the gullet of the kid and other substances used in the preparation of the rennet. It would be useful to have an uncontaminated kPGE to produce EMC's. Such EMC's could be produced in a manner acceptable to kosher and vegetarian consumers. A recombinant kPGE (rKPGE) could be produced in very pure form free of the other substances found in the present commercial rennet formulations.
SUMMARY OF THE INVENTION
The present invention provides kPGE and derivative polypeptides which are capable of being produced by genetic recombination and used to produce EMCs. This invention further provides nucleic acid sequences encoding kPGE and derivative pplypeptides which can be used to create recombinant host cells that express kPGE and derivative polypeptides. A further subject of the present of invention is a fusion polypeptide called polyHis-enterokinase which increases expression of esterases and lipases when fused to the N-terminal of the esterase or lipase. This invention also provides a method for treating animals with an esterase or lipase deficiency by administering rkPGE to the animal in a therapeutically effective amount.


REFERENCES:
patent: 2531329 (1950-11-01), Farnham
patent: 2794743 (1957-04-01), Farnham
patent: 3081225 (1963-03-01), Farnham et al.
patent: 3256150 (1966-06-01), Nelson et al.
patent: 5320959 (1994-06-01), Peters et al.
patent: 5372941 (1994-12-01), Peters et al.
patent: 5521088 (1996-05-01), Fujii et al.
patent: 5529917 (1996-06-01), Andreoli et al.
patent: 5691181 (1997-11-01), Lowe
patent: 5728412 (1998-03-01), Fujii et al.
patent: 0 502 474 (1992-09-01), None
patent: 542629 (1993-05-01), None
patent: WO 86/03778 (1984-07-01), None
patent: WO86/01532 (1986-03-01), None
patent: WO94/13816 (1994-06-01), None
Anderson, R.A. and Sando, G.N.J. Biol.Chem. 26:22740-84 (1991).
Bernbach, et al., Eur.J.Biochem. 148:233-238 (1985).
Birschbach, Bulletin of the IDF 269:36-39 (1992).
Carriere, F., et al, Eur.J.Biochem. 202:75-83 (1991).
Godfrey and West Eds. Chapter 2.12 Industrial Enzymology, 2ndEd. Stockton Press, 1996.
Chaudhari & Richardson, J. of Dairy Science 54:467-71 (1971).
Crabbe, et al, Protein Expression and Purification, 7:229-236 (1996).
DeLaborde de Monpesat, et al, Chemical Abstracts 114:278 (1991).
Docherty, et al, Nuc. Ac. Res. 13:1891-1903 (1985).
D'Souza & Oriel, Appl. Biochem. And Biotech. 36:183-198 (1992).
Fox & Law, Food Biotechnology 5:239-262 (1991).
Ha & Lindsay, Chem. Abstr. 118:85-66 (1993).
Ha & Lindsay, Int. Dairy Journ. 2:179-193 (1992).
Hamosh, N., Nutrition 6:421-428 (1990).
Lai, et al, JAOCS 75:411-416 (1998).
Komaromy & Schotz, PNAS USA 84:626-630 (1987).
Moreau, et al, Biochem. And Biophys. Acta 960:286-293 (1988).
Nelson, et al., J.Dairy Sci. 60:327-362 (1976).
Richardson, et al., J. Dairy Sci. 54:643-647 (1970).
Richardson & Nelson, J. Dairy Sci 50:1061-1065 (1967).
Siezen & van den Berg, Bulletin of the IDF 294:4-6 (1994).
Sweet et al., Arch.Biochem. and Biophys., 234:144-150 (1984).
Timmermans, et al., Gene 147:259-262 (1994).
Vorderwulbecke, et al., Enzyme Microb. Technol. 14:631-39 (1992).
Brockerhoff, H., “Determination of the Positional Distribution of Fatty Acids in Glycerolipids”, General Analytical Methods, 315-325.
Chapter 12, “Hard Italian Cheeses”, Cheese and Fermented Milk Foods, 213-227.
Eastman Kodak Company, “Yeast N-Terminal FLAG® Expression System”, FLAG Biosystem 1994.
Food Chemicals Codex, National Academy Press, (Washington, D.C. 1981), pp. 480-493.
Parry, R.M., Jr., et al, “Rapid and Sensitive Assay for Milk Lipase”, Journal of Dairy Science 49, 356-360.
Invitrogen Corp., “Pichia Expression Kit:Protein Expression”, Version 3.0, Calalog No. K1710-01.
Ramsey, Harold A., “Electrophoretic Separation of Esterases Present in Various Tissues of the Calf”, Journal of Dairy Science, 1185-1186.
Ramsey, Harold A., “Photometric Procedure for Determining Esterease Activity”, Clinical Chemistry 3:185-194.
Ramsey, Harold A and Young, J.W., “Substrate Specificity of Pregastric Esterease from the Calf”, Journal of Dairy Science, 2304-2306.
Sambrook, J., et al, “Moleclar Cloning:A Laboratory Manual”, (Cold Spring Harbor, 1989).
Scorer, Carol A., et al, “Rapid Selection Using G418 of High Copy Number Transformants of Pichia pastoris for High-level Foreign Gene Expression”, Bio/Technology 12:181 (Feb. 12, 1994).

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