Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Transferase other than ribonuclease
Reexamination Certificate
1999-12-02
2001-03-13
Prats, Francisco (Department: 1651)
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Transferase other than ribonuclease
C435S262000, C435S265000
Reexamination Certificate
active
06200789
ABSTRACT:
BACKGROUND OF THE INVENTION
The manufacture of high quality leather goods results in an almost equal weight of solid waste material. The U.S. leather industry generates more than 50,000 metric tons of chrome-tanned trimmings, shavings and buffing dust each year, while the world-wide total is about ten times as much (Brown, E. M., et al., JALCA, 91: 270-276 (1996)). Animal by-products, such as trimmings and shavings from the leather industry and feathers from the poultry industry, have traditionally been disposed in landfills. However, increasing environmental concerns and escalating landfill costs necessitate that uses be found for these protein-containing by-products. This invention relates to the use of transglutaminase to produce useful products from such animal by-products. The method of producing such useful products involves incubating animal by-products in a transglutaminase-containing solution to produce transglutaminase-treated animal by-products, compressing the transglutaminase-treated animal by-products to produced a compressed product, and drying the compressed product. The transglutaminase-containing solution need not contain casein. The resulting product is stronger in comparison to controls as measured by force in compression.
The use of transglutaminase to cross-link a variety of proteins, resulting in products with unique properties and improved functionality, has been widely described in the literature. For example, transglutaminase has been used to improve the functional properties of food proteins such as wheat gluten and milk proteins (Chobert, J. M., et al., Nahrung, 40 (4): 177-182 (1996). Microbial transglutaminase treated caseinate has been used to produce larger pieces of restructured meat from their smaller pieces (Motoki, M., and K. Seguro, Trends in Food Science & Technology, 9(5): 204-210 (1998)). U.S. Pat. No. 5,531,795 described the use of microbial transglutaminase in conjunction with casein (which has long been used as a finishing agent for leather) in the area of leather finishing where transglutaminase-improved casein finishes are applied to leather; this patent is actually describing the enhancement of casein finishes with transglutaminase and then the application of these products to leather, not the binding of the finishes to leather or the binding of leather to leather.
SUMMARY OF THE INVENTION
A method of producing useful products from animal by-products by incubating animal by-products in a transglutaminase-containing solution to produce transglutaminase-treated animal by-products, compressing the transglutaminase-treated animal by-products to produced a compressed product, and drying the compressed product. The transglutaminase-containing solution need not contain casein.
DETAILED DESCRIPTION OF THE INVENTION
Animal by-products such as feathers, chrome shavings (waste leather from the process of producing chromium-tanned leather), and aldehyde- and vegetable-tanned leather can be treated with microbial transglutaminase and then compressed and dried to give useful products that are stronger in comparison to controls as measured by force in compression.
The method of producing such useful products involves incubating such animal by-products in a transglutaminase-containing solution to produce transglutaminase-treated animal by-products, compressing the transglutaminase-treated animal by-products to produce a compressed product, and drying the compressed product. The transglutaminase-containing solution need not contain casein.
Transglutaminase of all origins (e.g., human, animal, microbial) may be used in this method. Preferably the transglutaminase is of microbial origin.
Generally the concentration of enzyme in the transglutaminase containing solution is between 1 to 100 units of transglutaminase/g of substrate (i.e., animal by-products); preferably between 6 to 50 units/g of substrate is utilized. The pH of the transglutaminase-containing solution is generally from about 5 to about 10, preferably about 6 to about 7, most preferably about 6.5. The amount of water in the transglutaminase-containing solution is generally about 1-25 parts water to 1 part of substrate, preferably about 1-10 parts water to 1 part of substrate, most preferably about 5 parts water to 1 part of substrate; for example 10 g of by-product in 50 ml water. The incubation time of the animal by-products in the transglutaminase-containing solution is generally up to about 18 hours (if zero time is used then the enzymatic reaction occurs entirely during compression), preferably the incubation time is about one to about eight hours, most preferably about four hours. The incubation temperature is generally from about 5° C. to less than about 85° C. (transglutaminase generally is inactivated at temperatures of above about 85° C.), preferably the incubation temperature is from about 30° C. to about 60° C., most preferably about 50° C.
After the animal by-products have been incubated in the transglutaminase-containing solution, the resulting transglutaminase-treated animal by-products are then compressed at a compression weight of generally about 50 to about 500 kg (preferably about 50 to about 150 kg, most preferably about 100 kg) for generally about 5 to about 50 hours (preferably about 10 to about 30 hours, most preferably about 24 hours). The temperature during compression is generally from about 5° C. to less than about 85° C.; preferably ambient temperature (RT) is utilized. The compressed product is then dried for up to one minute or longer, if vacuum dried, and up to one week or longer if dried at ambient temperature and pressure.
The following examples are intended only to further illustrate the invention and are not intended to limit the scope of the invention as defined by the claims.
REFERENCES:
patent: 3643339 (1972-02-01), Plechac et al.
patent: 5487889 (1996-01-01), Eckert et al.
patent: 5531795 (1996-07-01), Rasmussen et al.
patent: 5686124 (1997-11-01), Moller et al.
patent: 5968568 (1999-10-01), Kuraishi et al.
Brown, E.M., et al., “Production and Potential Uses of Co-Products from Solid Tannery Waste”,JALCA, vol. 91, pp. 270-276, 1996.
Chobert, J.M., et al., “Recent Advances in Enzymatic Modification of Food Proteins for Improving Their Functional Properties”,Nahrung, vol. 40(4), S., pp. 177-182, 1996.
Motoki, M., et al., “Transglutaminase and It's Use for Food Processing”,Trends in Food Science&Technology, vol. 9, pp. 204-210, 1998.
Kuraishi, C., “Production of Restructed Meat using Microbial Transglutaminase without Salt or Cooking”,Journal of Food Science, vol. 62(3), pp. 488-490 & p. 515, 1997.
Eric Dickinson, “Enzymic Crosslinking as a Tool for Food Colloid Rheology Control and Interfacial Stabilization”,Trends in Food Science&Technology, vol. 8, pp. 334-339, 1997.
Ikura, K., et al., “Crosslinking of Casein Components by Transglutaminase”,Agric. Biol. Chem., vol. 44(7), pp. 1567-1573, 1980.
Motoki, M., et al., “Glutamine-specific Deamidation of ∝s1-Casein by Transglutaminase”,Agric. Biol. Chem., vol. 50 (12) pp. 3025-3030, 1986.
Nio, N., et al., “Gelation of Casein and Soybean Globulins by Transglutaminase”,Agric. Biol. Chem., vol. 49(8), pp. 2283-2286, 1985.
Sakamoto, H., et al., “Strength of Protein Gels Prepared with Microbial Transglutaminase as Related to Reaction Conditions”,Journal of Food Science, vol. 59(4), pp. 866-871, 1994.
Lorenzen, P. Chr., et al., “Crosslinking of Sodium Caseinate by a Microbial Transglutaminase”,Nahrung, vol. 42(3/4), S., pp. 151-154, 1998.
Nielsen, G.S., et al., “Impact of Salt, Phosphate and Temperature on the Effect of a Transglutaminse (F XIIIa) on the Texture of Restructured Meat”,Meat Science, vol. 41(3), pp. 293-299, 1995.
Akamittath, J.G., et al., “Transglutaminase Mediated Polymerization of Crude Actomyosin Refined from Mechanically Deboned Poultry Meat”,Journal of Muscle Foods, vol. 3, pp. 1-14, 1992.
Toda, H., et al., “Determination of Protein-Bound Glutamine”,Biochim. Biophys. Acta, vol. 175, pp. 430-433, 1969.
Kleman, J., et al., “Transglutaminase-Catalyzed Cross-Linking of Fibrils of Colla
Brown Eleanor M.
Cabeza Luisa F.
Marmer William N.
Taylor Maryann M.
Fado John D.
Ge Susan D.
Prats Francisco
Silverstein M. Howard
Stover G. Byron
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