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MULTIZYME

MULTIZYME
INR 175 00
NEW PRODUCT
Product location

Anantapur, Andhra Pradesh, India

Product Description

MULTIZYME Cocktail of multiple enzymes With prices of feeding stuff such as soybean meal and grains soaring up every year, even a small percentage of increase in efficiency can mean big savings to the Animal Feed industry. Need of Exogenous Enzymes Poultry naturally produces enzymes to aid the digestion of feed nutrients. However, they do not have enzyme to break down fibre completely and need exogenous enzymes in feed to aid digestion. Ammoniac emissions of Litter Now a day, poultry litter is considered a concern of environment. Ammoniac emissions are causing the farms to closure by the stringent statutory regulations. Minerals in Litter Furthermore the present practice of use of Inorganic minerals forces to go with very excessive levels of inclusions of these minerals, particularly Phosphorous. All these excessive minerals will pass out through Litter. When this poultry litter is used as Manure in Agriculture and Aquaculture these in excess minerals particularly phosphorous ends up in the water table through run-off. Phytate Phytate is the main phosphorus-containing constituent (P content 28.2%) of many seeds and tubers; and its primary physiological role is P storage for germination (Cosgrove, 1980). In general, phytates constitute about 1-2% by weight of many cereals and oilseeds. Approximately 60-90% of total P in these seeds is present in phytate-bound form (Cheryan, 1980). Phytic acid is the primarily source of inositol and the main storage form of phosphorus in plant seeds that are used as animal feed ingredients (oilseed meals, cereal grains, and legumes). There are many applications of phytic acid, including industrial use as a corrosion inhibitor on metals, a rust remover and an additive to lubricating greases, use as a food additive, and medical applications, including use in the prevention of dental caries, use as an imaging agent for organ scintography and an X-ray enhancement contrasting agent, use as a hypocholestromic agent, use to reduce gastric secretion for treatment of gastritis, gastroduodenitis, gastric duodenal ulcers and diarrhea, use as an antidote for toxic metal absorption, therapeutic uses in the prevention and dilution of calcium deposits associated with various diseases and for reducing calcium concentration in urine (thus checking the formation of renal calculi), use as a preventive agent against severe poisoning with pressurized oxygen and preventing thirst during exercise, use as a taste-improving agent in orally administered antibiotics, and use in the treatment of multiple sclerosis (see U.S. Pat. No. 5,217,959 issued to Robert Sabin) Phytates are of very limited digestibility/availability for pigs (Cromwell, 1980; Jongbloed, 1987). It therefore contributes to the P pollution in regions where land and water resources are limited and animal production is intensive such as in The Netherlands. Phytate-protein-starch complex molecule: a potential structure (modified after Thompson, 1986; and Kies, 1998). Phytic acid (myoinositol 1,2,3,4,5,6-hexakis dihydrogen phosphate) is strongly negatively charged (six reactive phosphate groups) over a wide pH range, indicating tremendous potential for complexing or binding positively charged molecules such as cations or proteins below the isoelectric point. The binding is possible within a phosphate group or between two phosphate groups on either the same or different phytic acid molecules; and the resulting structure is said to be a chelate compound (Cheryan, 1980). Usually, phytate-bound nutrients are poorly available in the digestive tract of monogastric animals due to the lack of phytase enzyme required to cleave the phytate molecule (Cosgrove, 1980; Reddy et al., 1982; Jongbloed et al., 1993). Numerous animal experiments have documented the nutritional implications of phytates in binding dietary macro- and microelements (Ca, Mg, Fe, Zn, Cu, Mn, Mo and Co), thus reducing their solubility and bioavailability (Erdman, 1979; Torre et al., 1991). The effect of phytic acid on mineral bioavailability is influenced by pH, amount of phytic acid, mineral concentration, association/configuration of phytic acid with dietary protein/ fiber/starch, heat treatment, pre-feeding processing and the presence of other metal ions in a diet (Cheryan, 1980; Torre et al., 1991). Phytates are generally soluble at low pH, but almost completely insoluble at intestinal pH (Cheryan, 1980). The interaction between phytates and minerals leads to formation of complexes that precipitate in the duodenum (Reddy et al., 1982). Since the small intestine is the principal site of divalent cation absorption (Jongbloed et al., 1993), this implies that bioavailability of minerals can be affected by the presence of phytate. The availability of dietary minerals bound to phytate is low, especially when two or more cations are present so that a synergistic binding effect can occur (Maga, 1982). The enzymes that catalyze the conversion of phytic acid to inositol and inorganic phosphate are known as phytases. Phytase is a phosphomonoesterase capable of hydrolyzing phytic acid (myoinositol hexakisphosphate) to yield inorganic orthophosphate that can be absorbed through the gastrointestinal wall of the pig along with a series of lower phosphoric esters of myoinositol. The dephosphorylation is necessary not only for digestibility of phytate P, but also for the utilization of minerals and proteins bound to phytates. The research of phytase spans more than 87 years from its discovery by Suzuki et al. (Tokyo Imp. Univ. Coll. Agr. Bull., 7: 503-512, 1907) until its commercialization in Europe in 1993-1994 by Gist-brocades. Intrinsic phytase present in the seeds of higher plants (e.g. wheat) is recognized by the International Union of Pure and Applied Chemistry and the International Union of Biochemistry as 6-phytase (EC 3.1.3.26). Exogenous phytase produced by microorganisms inhabiting the gastrointestinal tract such as fungi, bacteria, yeasts or intestinal endogenous phytase secreted into the lumen from the intestinal mucosa of some species is recognized as 3-phytase (EC 3.1.3.8; Wise, 1980). However, the endogenous phytase activity in the intestinal mucosa of pigs is negligible (Pointillart et al., 1984). Jongbloed et al. (1992) detected no phytase activity in the ileal digesta, which indicates that phytases from the bacterial flora up to the terminal ileum and intestinal mucosal phytases are negligible. For that reason, the ability of the pig to utilize nutrients bound to phytate complexes is primarily dependent on intrinsic phytase activity of the feed ingredients or enzymatic preparations of microbial phytase added to diets. Schematic mode of action of microbial phytase on dietary phytates. The enzyme cannot stand high temperatures. For instance, by pelleting a pig diet at 70°C, the initial activity is reduced by 15-25% (Schwarz and Hoppe, 1992). Microbial phytases are active over a wide range of pH, with optima at pH 2.5 and 5.5 (Simons et al., 1990). Jongbloed et al. (1992) reported from studies on cannulated pigs (ileal and duodenal cannulae) that hydrolysis of phytate in diets by microbial phytase takes place mainly in the stomach (43%), and decisively less in the small intestine (7%). This indicates that only half of the phytate was hydrolyzed by microbial phytase, which can be explained by the limited retention time in the stomach. Four distinct classes of phytase have been characterized in the literature: histidine acid phosphatases (HAPS), B-propeller phytases, purple acid phosphatases, and most recently, protein tyrosine phosphatase-like phytases (PTP-like phytases). Histidine acid phosphatases (HAPs) Most of the known phytases belong to a class of enzyme called histidine acid phosphatases (HAPs). HAPs have been isolated from filamentous fungi, bacteria, yeast, and plants. All members of this class of phytase share a common active site sequence motif (Arg-His-Gly-X-Arg-X-Pro) and have a two-step mechanism that hydrolyzes phytic acid (as well as some other phosphoesters).[2] The phytase from the fungus Aspergillus niger is a HAP and is well known for its high specific activity and its commercially marketed role as an animal feed additive to increase the bioavailability of phosphate from phytic acid in the grain-based diets of poultry and swine.[4] HAPs have also been overexpressed in several transgenic plants as a potential alternative method of phytase production for the animal feed industry and very recently, the HAP phytase gene from E. coli has been successfully expressed in a transgenic pig. ß-propeller phytases ß-propeller phytases make up a recently discovered class of phytase. This first examples of this class of enzyme were originally cloned from Bacillus species, but numerous microorganisms have since been identified as producing ß-propeller phytases. The three-dimensional structure of ß-propeller phytase is similar to a propeller with six blades. Current research suggests that ß-propeller phytases are the major phytate-degrading enzymes in water and soil, and may play a major role in phytate-phosphorus cycling. Purple acid phosphatases A phytase has recently been isolated from the cotyledons of germinating soybeans that has the active site motif of a purple acid phosphatase (PAP). This class of metalloenzyme has been well studied and searches of genomic databases reveal PAP-like sequences in plants, mammals, fungi, and bacteria. However, only the PAP from soybeans has been found to have any significant phytase activity. The three-dimensional structure, active-site sequence motif and proposed mechanism of catalysis have been determined for PAPs. Protein tyrosine phosphatase-like phytases Only a few of the known phytases belong to a superfamily of enzymes called protein tyrosine phosphatases (PTPs). PTP-like phytases, a relatively newly discovered class of phytase, have been isolated from bacteria that normally inhabit the gut of ruminant animals. All characterized PTP-like phytases share an active site sequence motif (His-Cys-(X)5-Arg), a two-step, acid-base mechanism of dephosphorylation, and activity towards phosphrylated tyrosine residues, characteristics that are common to all PTP superfamily enzymes. Like many PTP superfamily enzymes, the exact biological substrates and roles of bacterial PTP-like phytases have not yet been clearly identified. Interestingly, the characterized PTP-like phytases from ruminal bacteria share sequence and structural homology with the mammalian PTP-like phosphoinositide/-inositol phosphatase PTEN,[3] and significant sequence homology to the PTP domain of a type III-secreted virulence protein from Pseudomonas syringae (HopPtoD2). Biochemical characteristics Substrate specificity Most phytases show a broad substrate specificity, having the ability to hydrolyze many phosphorylated compounds that are not structurally similar to phytic acid such as ADP, ATP, phenyl phosphate, fructose 1,6-bisphosphate, glucose 6-phosphate, glycerophosphate and 3-phosphoglycerate. Only a few phytases have been described as highly specific for phytic acid, such as phytases from Bacillus sp., Aspergillus sp., E. coli and those phytases belonging to the class of PTP-like phytases Pathways of phytic acid dephosphorylation Phytic acid has six phosphate groups that may be released by phytases at different rates and in different order. Phytases hydrolyze phosphates from phytic acid in a stepwise manner, yielding products that again become substrates for further hydrolysis. Most phytases are able to cleave five of the six phosphate groups from phytic acid. Phytases have been grouped based on the first phosphate position of phytic acid that is hydrolyzed. The Enzyme Nomenclature Committee of the International Union of Biochemistry recognizes three types of phytases based on the position of the first phosphate hydrolyzed, those are 3-phytase (EC 3.1.3.8), 4-phytase (EC 3.1.3.26), and 5-phytase (EC 3.1.3.72). To date, most of the known phytases are 3-phytases or 4-phytases, only a HAP purified from lily pollen and a PTP-like phytase from Selenomonas ruminantium subsp. lactilytica have been determined to be 5-phytases. Biological relevance Phytic acid and its metabolites have several important roles in seeds and grains, most notably, phytic acid functions as a phosphorus store, as an energy store, as a source of cations and as a source of myo-inositol (a cell wall precursor). Phytic acid is the principal storage forms of phosphorus in plant seeds and the major source of phosphorus in the grain-based diets used in intensive livestock operations. The organic phosphate found in phytic acid is largely unavailable to the animals that consume it, but the inorganic phosphate that phytases release can be easily absorbed. Ruminant animals can use phytic acid as a source of phosphorus because the bacteria that inhabit their gut are well characterized producers of many types of phytases. However, monogastric animals do not carry bacteria that produce phytase, thus, these animals cannot use phytic acid as a major source of phosphorus and it is excreted in the feces. Phytic acid and its metabolites have several other important roles in Eukaryotic physiological processes. As such, phytases, which hydrolyze phytic acid and its metabolites, also have important roles. Phytic acid and its metabolites have been implicated in DNA repair, clathrin-coated vesicular recycling, control of neurotransmission and cell proliferation. The exact roles of phytases in the regulation of phytic acid and its metabolites and the resulting role in the physiological processes described above are still largely unknown and the subject of much research. Phytase has been reported to cause hypersensitivity pneumonitis in a human exposed while adding the enzyme to cattle feed. Dietary factors affecting efficacy of microbial phytase A prerequisite for a good evaluation of microbial phytase efficacy is that the animals be fed below their P requirement. This is due to intestinal regulation of P absorption when animals are fed above their P requirement. There is little information available on dietary factors affecting efficacy of microbial phytase. It is commonly known that higher dietary Ca levels decrease apparent absorption of P (Jongbloed, 1987). However in most experiments dietary treatments with different Ca levels were implemented only in diets with microbial phytase and not simultaneously in diets without microbial phytase (Lei et al., 1994; Lantzsch et al., 1995). Mostly a linear decrease of P absorption is observed. In two experiments we studied whether a possible interaction could be demonstrated between dietary Ca level and microbial phytase supplementation on P absorption (Mroz et al., 1994b; Jongbloed et al., 1995). We observed a linear decrease in apparent digestibility of P at higher Ca levels, but no interaction with microbial phytase could be demonstrated. Another dietary factor is the amount and source of phytate. In two experiments we studied the effect of phytate amount and source on the efficacy of microbial phytase (Dekker et al., 1992). For this purpose we used diets based on either corn or sunflower seed meal at two inclusion levels (and so two levels of phytate P). The concentrations of phytate P were 1.2 and 1.8 g/kg; and phytase activities in the corn and sunflower-based diets were 450 and 340 FTU/kg, respectively. We observed that in the cornbased diet the higher level of phytate generated substantially more digestible P, while in the sunflower-based diet slightly more digestible P was generated at the higher phytate level. It was concluded firstly that in both diets the lower level of phytate was too low to get maximal effect of the enzyme; and secondly that phytate in corn is more readily available than phytate in sunflower seed meal. Lack of substrate (phytate) may occur in piglet diets formulated with large proportions of animal products as a protein or P source or with diets that already contain a high oncentration of intrinsic phytase like wheat, wheat bran, barley, rye or triticale (Düngelhoef et al., 1994; Eeckhout and De Paepe, 1992). Jongbloed et al. (2000) performed two experiments in which diets were supplemented with or without microbial phytase and/or lactic acid and formic acid. Supplementary lactic acid and formic acid exerted a synergistic effect on apparent digestibility of P. This means that efficacy of microbial phytase could be further enhanced by some organic acids. APPARENT ILEAL DIGESTIBILITY There is a limited number of reports on the apparent ileal digestibility of crude protein in pigs in relation to phytase supplementation. Ileal digestibility of N and amino acids is usually considered a proper criterion of dietary protein value (Low, 1989). Officer and Batterham (1992) reported that ileal digestibility of crude protein and essential amino acids increased by 7-12 percentage units. Also, Khan and Cole (1993) observed an increase in ileal nitrogen digestibility of 12.8 percentage units (P<0.077) when feeding a high-phytate barley-based diet with Aspergillus niger phytase (1000 FTU/ kg) to six cannulated gilts. Mroz et al. (1994a) observed a lower ffect (+3.5 percentage units); and in a second experiment Kemme et al. (1999) showed a significantly higher ileal digestibility for several amino acids (Table 3). However, there are a few reports showing that microbial phytase exerted no effect on apparent ileal digestibility of crude protein or amino acids (Lantzsch et al., 1995; Valaja et al., 1998). Effect of management factors on efficacy of microbial phytase In practice, pigs are raised under a wide variety of housing and feeding conditions. Therefore, it is important to know the effects of different feeding regimens and housing conditions on the efficacy of microbial phytase. In one study we could not show any effect of feeding level (2.3 and 2.8 times maintenance requirement for metabolizable energy) on the efficacy of microbial phytase (Mroz et al., 1994a). In the same experiment no effect on phytase efficacy was noted between feeding two and seven times a day, while efficacy was slightly decreased when pigs were fed once daily. The efficacy of microbial phytase (500 FTU/kg) is increased by soaking a phytate-rich diet (maize, tapioca, beans, phytase-inactivated wheat bran and extracted sunflower meal) for 8-15 hrs prior to feeding (Kemme and Jongbloed, 1993). Some results of this treatment in a trial with growing pigs from 30 to 70 kg body weight are presented in Table 4. Soaking a barleysoybean meal diet supplemented with microbial phytase for 3 hrs, however, did not result in a higher P digestibility (Näsi and Helander, 1994). This may have been due to the short soaking time and the rather high dietary Ca content. In a second experiment of Näsi et al. (1995), soaking a barleyrapeseed meal diet for 3 hrs with dried whey at 40°C increased P digestibility by 4%. Environmental impact of microbial phytase In the absence of microbial phytase only ~16% of P in corn and ~38% of P in soybean meal is digested by pigs. Because of the large amount of undigested dietary P, a substantial amount of P is excreted via feces. Based on the estimates of Cromwell et al. (1993), a dose of microbial phytase equal to 1000 FTU/g converted approximately one-third of the unavailable P to an available form. About 500 FTU/kg of diet generates approximately 0.8 g digestible P/kg, which is equivalent to 1.0 g P from monocalcium phosphate or 1.23 g P from dicalcium phosphate, which is often used in the United States. This is illustrated in Table 6. This table shows that with supplementation of 500 FTU/kg of feed, total P content is 1.3 g/kg lower. With the same performance as the control diet between 20 and 50 kg live weight and a feed conversion ratio of 2.5, it can be calculated that P excretion per kg growth is 4.75 instead of 8.0 g, which is 40% lower. (http://en.engormix.com/MA-pig-industry/nutrition/articles/efficacy-use-application-microbial-t182/p0.htm) Phytase is used as an animal feed supplement - often in poultry and swine - to enhance the nutritive value of plant material by liberation of inorganic phosphate from phytic acid (myo-inositol hexakisphosphate). Phytase can be purified from transgenic microbes and has been produced recently in transgenic canola, alfalfa and rice plants. Phytase can also be produced on a large scale through cellulosic biomass fermentation using genetically modified (GM) yeast. Phytase can also be isolated from basidiomycetes fungi. A strain of transgenic pig can produce phytase, thus reducing their environmental impact. All vegetable matters, particularly grains, cereals and pulses or most of the components of animal feed, contains Phytic acid. This Phytic acid has the ability to adsorb all the minerals like phosphate, calcium, magnesium, iron etc. because of the electrical chares present in them. Phytase enzyme has the ability to completely breakdown Phytic acid into simpler substances and prevents the adsorption of minerals present in the feed. Hence, it is a great boon to the animal system and all the mineral components present in the feed are made available for the animals for absorption and for further metabolism. However, tests have shown that the power to release digestible P out of plant phytate is not linear. This means that the first 250 FTU of phytase will release more digestible P than the second 250 FTU you include in a compound. This ‘non-linear behaviour’ forms special challenges for feed formulation programs, as these are based on linear programming. 3-Phytase EC [3.1.3.8] Aspergillus niger 6-Phytase EC [3.1.3.26] Aspergillus oryzae, containing the gene for 6-phytase isolated from Peniophora lycii Non-starch polysaccharides Poultry lack the digestive capacity of ruminant animals and the presence of non-starch polysaccharides (NSP) in the diet increases intestinal viscosity resulting in decreased digestibility of the diet. The use of non-starch polysaccharide (NSP) degrading enzymes as feed additives has consolidated around their application to barley- and wheat-based diets for broiler chicks. Only with this application has a good understanding of their mode of action been developed and reasons for their effectiveness established. Most of the effect of NSP degrading enzymes can be ascribed to reversing the increase in digesta viscosity caused by polysaccharides leached from grain cell walls. Because digesta viscosity is greatest in the youngest birds and decreases with age, the value of supplementary enzymes for older birds is limited to secondary and less well defined effects. These include the release of nutrients otherwise entrapped in the cellular matrix of the feed. Maize alone amongst the commonly used cereals does not appear to release soluble NSPs in amounts sufficient to produce a detectable depression in performance. However, maize is not a homogeneous commodity and for some samples this may not be the case. Use of NSP degrading enzymes with legume seeds can improve nitrogen retention but effects are generally small. The structures of the soyabean NSPs, particularly the pectic polysaccharides, appear unique and existing commercial formulations are not recognised to contain enzymes capable of their degradation. With the present knowledge of soyabean polysaccharide structure, more informed formulation of enzyme products for use with soyabean should enable better responses to be achieved. When coupled with the lesser response from maize, this could allow the effective use of enzyme additives with maize-soyabean diets. (http://journals.cambridge.org/action/displayAbstract?fromPage=online&aid=622688) Multizyme is conceived to solve at a time many complex problems that may arise when feed manufacturer employs more than one problematic feeding stuff like a combination of Guar Meal Korma, Cotton Seed Cake, Soy Extractions, Fish Meal which contain Anti Nutritional Factors. Matrix Value of Multizyme Matrix Value of Enzymes = nutrient-equivalent values assigned to enzyme products in least-cost formulation Feed Formulation with Enzymes The improvements in nutrient digestibility must be considered to effectively use enzymes in formulation. The nutrients affected and the actual improvements in digestibility may be based on research or expected results for the enzyme in use. A summary of estimated changes to specifications of corn-soy layer diets is given in Table 6. This table was compiled from available information and provides a range for each enzyme class. More specific information is available from enzyme suppliers. Two techniques to use enzymes in formulation involve a) altering the formula nutrient specifications or b) assigning nutrient specifications to the enzyme in the ingredient matrix. Examples of these techniques are given in Tables 7 and 8. A theoretical "Enzyme A" which improves digestibility of protein, energy, calcium and phosphorus is used for this example. The changes to the specifications and the ingredient matrix values for theoretical "Enzyme A" are shown in Table 7. These values would be supplied by the enzyme manufacturer and verified by research. Table 8 shows composition of high-density layer formulas with and without the enzyme. The standard formula was set to contain a minimum of 1320 Kcal ME/lb. and utilized 47 lbs. of fat to meet this requirement. In the second formula the enzyme was forced in at 1 lb. /ton and the formula specifications were decreased by the amount suggested on Table 7. Minimum specifications for metabolizable energy, protein, amino acids, calcium and phosphorus were decreased because of the enzyme’s effects in making these nutrients more available. The least cost formula used less soybean meal, limestone, dical and fat resulting in a lower formula cost. In the last column, the enzyme was given the nutrient specifications in Table 7. The formula and cost savings are the same but the nutrient levels assigned to the enzyme inflate the reported nutrient levels. The actual nutrient values in the last column are those that would be measured by analysis. A possible solution is to add additional nutrients and update ingredients to reflect these changes. Table 1. Enzymes for Corn-Soy Layer Diets Enzyme Type Product Manufacturer Active Enzyme Components Targeted Feed Components Hemicellulases Hemicell ChemGen Corp. B -Mannanase Galactomannan polymers in soybean meal Lodestar EN140 Loders Croklaan A -Galactosidase Galacto-oligosaccharides (raffinose,stachyose, etc.) in soybean meal Vegpro Alltech , Inc Protease, cellulase, pentosanase, A -galactosidase, amylase Oligosaccharides in soybean meal Phytases Allzyme Phytase Alltech, Inc Phytase Phytin in plant materials Natuphos BASF Phytase Phytin in plant materials Enzyme Blends Avizyme 1500 Finnfeeds Xylananse, protease, amylase Non-starch polysaccharides, starches, proteins in corn and soybean meal Multizyme Karyotica Amylase, Beta Glucanase, Cellulase, Pectinase, Phytase, Protease, Xylanase Non-starch polysaccharides, starches, proteins in corn and soybean meal; Phytin in plant materials Table 2. Effect of B-Mannanase Supplementation on Laying Hen Performance % HD Production Egg Weight, g Age, Weeks: 18-30 31-42 43-54 55-66 18-30 31-42 43-54 55-66 ME Level1 Enzyme Low --- 70.33 85.64a 78.69a 73.92a 51.31a 59.17a 62.98a 64.09 Low + 69.89 86.57b 79.92b 75.58b 51.37a 59.39a 62.89a 64.11 High --- 71.16 86.78b 79.89b 74.08a 51.48a 59.76b 63.28b 64.08 High + 71.83 87.26c 80.68c 75.41b 51.91b 59.71b 63.39b 64.06 1 Low ME, 1266-1285 Kcal/lb.; High ME, 1311-1330 Kcal/lb. Means within columns not sharing a common superscript are significantly different (p<.05) Table 3. Effect of Enzyme Supplementation on Molted Hen Performance, 72-100 Weeks of Age, Average ME Enzyme1 % HD Production Egg Weight, g Feed Consumption, lbs/100/day None 68.73b 66.57b 24.60 A 68.94ab 66.47b 24.82 B 69.80a 66.59b 25.39 1 A - protease, amylase, xylanase B – protease, cellulase, xylanase, B-glucanase Means within columns not sharing a common superscript are significantly different (p<.05) Table 4. Effect of B-Mannanase Supplementation on Laying Hen Performance at Four Amino Acid Densities, 17-37 Weeks of Age Lysine, % Enzyme % HD Production Egg Weight, g Feed Consumption, g/hen/day 0.70 --- 72.92a 53.40a 93.44 0.70 + 73.98b 52.91b 93.64 0.78 --- 75.20 54.02 94.48 0.78 + 75.51 53.80 94.08 0.87 --- 77.18 54.77j 95.44 0.87 + 76.50 53.87k 94.53 0.96 --- 76.72 54.57 93.99a 0.96 + 76.59 54.86 92.13b Means within columns not sharing a common superscript are significantly different (p<.05) Table 5. Effect of Enzyme1 Supplementation on Performance of W-36 and B-300 Layers at Two Metabolizable Energy Levels 20-40 weeks of age Diet ME Enzyme Feed Cons, g % HD Egg Production Egg Weight, g W-36 1 Normal --- 96.5 91.6 57.7 2 Normal + 95.6 90.9 57.4 3 Low --- 98.4 90.2 58.2 4 Low + 99.5 91.7 58.6 B-300 1 Normal --- 99.1 86.1 61.3 2 Normal + 102.0 89.3 60.4 3 Low --- 103.2 88.8 59.4 4 Low + 100.3 88.4 58.8 1 xylanase, protease and amylase enzymes Table 6. Estimated Changes to Corn-Soy Layer Ration Specifications with Various Enzymes Enzyme Class: Hemicellulases Phytases Enzyme Blends ME, Kcal/lb. Decrease 10-40 Kcal Decrease 10-15 Kcal Decrease 10-20 Kcal Protein, % Decrease 0.4-0.5 points Decrease 0.4-0.5 points Decrease 0.0-0.5 points Lysine, % Decrease 0.00-0.05 points Decrease 0.01-0.02 points Decrease 0.00-0.02 points Methionine, % Decrease 0.000-0.005 points Decrease 0.002-0.005 points Decrease 0.000-0.005 points Available, Phos, % No Change Decrease 0.10-0.13 points No Change Calcium, % No Change Decrease 0.2-0.3 points No Change Table 7. Feed Formulation with Theoretical "Enzyme A" "Enzyme A" – Hemicellulose, phytase blend. Use rate 1lb/ton (0.05%). Cost - $1.50/lb Nutrient Change to Nutrient Specifications with "Enzyme A"1 Ingredient Matrix Values for "Enzyme A" used at 0.45 Kg/ton2 ME, Kcal/lb. Decrease 20 Kcal 40,000 Kcal/lb. Protein, Decrease 0.50 points 1000% Lysine, % Decrease 0.02 points 40% Methionine, % Decrease 0.01 points 20% Threonine, % Decrease 0.01 points 20% Calcium, % Decrease 0.2 points 400% Available Phosphorus, % Decrease 0.05 points 100% 1 Based on expected improvements in nutrient digestibility, "Enzyme A" allows us to change our nutrient specifications by these amounts and achieve results similar to a ration without the enzyme. 2 These values must be assigned to ‘Enzyme A" in the ingredient nutrient matrix based on expected improvements in nutrient digestibility. Enzyme use must be restricted to 1 lb./ton Table 8. Comparison of Formulation Methods with Theoretical "Enzyme A" "Enzyme A": --- + + Formulation Method: Standard Specification Change "Enzyme A" as an Ingredient Ingredient Kg/ton Kg/ton Lbs/ton Corn 559.2 588.3 588.3 48% Soy 219.3 209.3 209.3 Limestone 82.2 79 79 18.5% Dical 18.6 15.9 15.9 Salt 3.6 3.6 3.6 Layer Premix 2.7 2.7 2.7 dl-Methionine 1.5 1.45 1.45 "Enzyme A" --- 0.45 0.45 Fat 21.3 7.3 7.3 Calculated Nutrients Protein, % 17.20 17.00 (17.50)1 17.002 ME, Kcal/lb 1320 1300 (1320) 1300 Calcium, % 4.00 3.80 (4.00) 3.80 Avail. Phos, % 0.48 0.43 (0.48) 0.43 Lysine, % 0.92 0.90 (0.92) 0.90 Methionine, % 0.46 0.45 (0.46) 0.45 Threonine, % 0.68 0.67 (0.68) 0.67 1 Values reported on formula sheet based on values assigned to the enzyme 2 Nutrient values that would be determined by analysis Dosage: 750-1500 grams per ton in the compound feed. Direction: Mix the cocktail enzyme with premix evenly and then add the premix into complete feed and evenly mix again. Use the product once opening and fasten it after its using. Package and Storage: 25 Kg per kraft bag. Keep it at a dry, well-ventilated place at room temperature away from direct sunshine and rain & avoid touch with toxic and harmful substances during transportation and storage. Shelf Life: 12 Months after manufactured.

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