Hemicellulase use in feeds with low caloric content

Food or edible material: processes – compositions – and products – Fermentation processes – Of plant or plant derived material

Patent

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

426 46, 426630, A23K 100, A23L 120

Patent

active

06162473&

DESCRIPTION:

BRIEF SUMMARY
BACKGROUND OF THE INVENTION

1. Field of the Invention
The present invention relates to methods for feeding monogastric animals, and more particularly to methods employing one or more hemicellulases, such as mannanase, that decrease the feed to gain, or increase the weight gain of animals fed a low caloric diet containing the enzyme.
2. Background
The world population continues to grow, but land for food production is finite. J. E. Cohen, Discover 17: 42-47, (1996). In order to keep up with the growing food demand, improvements in the utilization of food resources will be needed to maintain the current living standards. One approach to improved efficiency has been to enhance the digestion of feeds by the inclusion of enzymes. Chesson, A., Supplementary enzymes to improve the utilization of pig and poultry diets, pp 71-89, In Haresign, W. and D. J. A. Cole (eds), Recent Advances in Animal Nutrition--1987, Butterworths, London. Enzymatically aided digestion not only yields more meat per pound of feed, but also reduces the volume of manure and the disposal cost.
Four types of enzymes have been clearly recognized in the marketplace for their value in animal feeds. In diets that contain wheat, rye or triticale, the enzyme xylanase (endo-1,4-.beta.-D-xylanohydrolase, E.C. 3.2.1.8) has been shown to be beneficial. Pettersson et al., British Journal of Nutrition 62: 139-149, 1989). Wheat, rye and the wheat/rye hybrid triticale contain large amounts of the non-starch polysaccharide arabinoxylan in the endosperm cell wall. The arabinoxylan is not digested by monogastric animals, but is hydrolyzed by microbial xylanase.
A second example of an enzyme with widespread use in feeds is .beta.-glucanase [cellulase, endo-1,4-.beta.-D-glucan 4-glucanohydrolase E.C. 3.2.1.4; or endo-1,3-(1,3;1,4)-.beta.-D-glucan 3(4)-glucanohydrolase E.C. 3.2.1.6] that has been shown to be especially beneficial in diets containing barley and oats. Rotter et al., Nutrition Reports International 39: 107-120 (1989). As well as interfering with digestion, the glucan causes wet sticky manure that induces breast blisters on poultry. In practice, xylanase and .beta.-glucanase are applied together since arabinoxylan and glucan are both present in the cereal grains. Pettersson et al., Animal Production 51: 201-20 (1990).
The use of enzymes that cleave phosphorus from phytic acid (myo-inositol hexakisphosphate) is a third example of the beneficial use of enzymes in animal feed. Simons et al., British Journal of Nutrition 64: 525-540 (1990). In monogastric animals the phosphate is not released from phytic acid during digestion but is released in the manure through microbial action. Phytic acid has a significant content in typical feeds. Phosphate run-off becomes a problem during manure disposal by causing eutrophication of nearby rivers, lakes or bays. Incorporation of phytase lowers the phosphate content in the manure and significantly decreases the need to add phosphate salts to diets.
Mannanase is another enzyme that has gained commercial use in corn and soybean based diets. The decreased feed to gain, or increased weight gain, of monogastric animals fed a diet containing mannanase was unexpected in a diet based on corn. Until the discovery that bacterial endo-1,4-.beta.-D-mannanase (E.C. 3.2.1.78, also known as mannan endo-1,4-.beta.-mannosidase, see McCleary, B. V., .beta.-D-Mannanase, Methods in Enzymology 160: 596-609, 1988) increases feed efficiency in corn-soybean diets, enzymes were infrequently used in poultry or swine feeds grown on corn-soy diets. U.S. Pat. No. 5,429,828, incorporated herein by reference, teaches a method of improving the energy efficiency of hemicellulose-containing animal feed by means of adding a hemicellulase, specifically mannanase, to the diet.
The positive effect of adding endo-1,4-.beta.-D-mannanase on feeding efficiency was unexpected in a diet based on corn. In barley or oats that contain mixed-linked glucan, or wheat, rye and triticale that contain arabinoxylan, the anti-nutritive polymer represents a large perce

REFERENCES:
patent: 3365440 (1968-01-01), Circle et al.
patent: 4822814 (1989-04-01), Ohyama et al.
patent: 5429828 (1995-07-01), Fodge et al.
patent: 5476775 (1995-12-01), Fodge et al.
patent: 5723443 (1998-03-01), Kagawa et al.
Easter et al., Dietary nututrient allowances for swine, Adjustments to nutrient allowance, Feedstuffs, (Jul. 1995), pp 41, 44 and 46.
Park W. Walthrop, Dietary nutrients allowances for poultry, Feedstuffs, (Jul. 1995), pp 69-72, 74 and 76.
Nick Dale, Ingredient analysis table: 1995 edition, Feedstuffs, (Jul. 1995), pp 24, 31, 32, 34, 36, 38, 39.
Schwartz et al., Journal of Agricultural and Food Chemistry, A Publication of the American Chemical Society, vol. 10, No. 2 (1962), pp 131-133.
R. L. Whistler, Polysaccharide Chemistry, Academic Press, Inc., (1953), pp 292-303.
R. T. Rowlands, Review: Industrial strain improvement: mutagenesis and random screening procedures, Enzyme Microb. Technology, vol. 6, (1984), pp 3-10.
Hansson et al., "The Journal of Biological Chemistry", Expression and Characterization of Biologically Active Human Extracellular Superoxide Dismutase in Milk of Transgenic Mice, vol, 269, No. 7, (1994).
Velander et al., Proceedings of the National Academy of Sciences:, High-level expression of a heterologous protein in the milk of transgenic swine using the cDNA encoding human protein C transgenic swine using the cDNA encoding human protein C, (1992), pp 12003-12007.
Whistler et al., Polysaccharide Chemistry, Academic Press, Inc., (1953), pp 152-161.
Biely et al., [65] Remazole Brilliant Blue-Xylan: A Soluble Chromogenic Substrate for Xylanases, Methods in Enzymology, vol. 160, (1967), pp 536-541.
Van Rooijen et al., Plant Seed Oil-Bodies as Carriers for Foreign Proteins, Bio/Technology, vol. 13, (1995), pp 72-77.
Emi et al., Crystallization and Some Properties of Mannanase, [Agr. Biol. Chem., vol. 36, No. 6, (1972), pp 991-1001.
Kusakabe et al., .beta.-Mannanase of Streptomyces, Methods in Enzymology vol. 160, pp 611-615 (date N.A.).
Takahashi et al., Purification and Some Properties of Mannanase from Streptomyces sp, Agric. Biol. Chem, (1984), pp 2189-2195.
Bicho et al., The characterisation of a thermostable endo-.beta.-1,4-mannanase cloned from "Caldocellum saccharolyticum", Appt. Microbiol Biotechnology, (1991), pp 337-343.
K. G. Johnson, Exocellular .beta.-mannanases from hemicellulolytic fungi, World Journal of Microbiology and Biotechnology 6, (1990), pp 209-217.
Kusakabe et al., Specificity of .beta.-Mannanase from Penicillium purpurogenum for Knojac Glucomannan, agric. Biol. Chem., 52 (2), (1988), pp 519-524.
Araujo et al., Studies on the galactomannan-degrading enzymes produced by Sporotrichum cellulophilum, Journal of Industrial Microbiology, 8 (1991), pp 229-236.
Colaco et al., Research/Extraordinary stability of enzymes dried in Trehalose: Simplified molecular biology, vol. 10, (1992), pp 1007-1011.
Lothi et al., Overproduction of an acetylxylan esterase from the extreme thermophile "Caldocellum saccharolyticum" in escherichia coli, Applied Microbiology biotechnology, (1990), pp 214-219.
Eero Sjoestroem, Wood Chemistry, Fundamentals and Applications, (1981), pp 49-67.
Seely et al., The Cyclic-2-3-diphosphoglycerate from Methanobacterium thermoautotrophicum is the D Enantioner, Current Microbiology, vol. 10, (1984), pp 85-88.
Hensel et al., Thermoadaption of methanogenic bacteria by intracellular ion concentration, FEMS Microbiology Letters 49 (1988), pp 75-79.
Scholz et al., Di-myo-inositol-1-1'-phosphate: a new inositol phosphate isolated from Pyrococcus woesei, vol. 306, No. 2,3, (1992), pp 239-242.
Kurr et al., Methanopyrus Kandleri, gen. and sp. nove. represents a novel group of hyperthermophilic methanogens, growing at 110.degree. C*, Archives of Microbiology, (1991), pp 239-247.
Akino et al., Characterization of Three .beta.-Mannanases of an Alkalophilic Bacillus sp., Agric. Biol Chem., 52 (3), (1988), pp 773-779.
Robertson et al., The discovery of new biocatalyst from microbial diversity, vol. 4

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Hemicellulase use in feeds with low caloric content does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Hemicellulase use in feeds with low caloric content, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Hemicellulase use in feeds with low caloric content will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-269217

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.