Amino acids and protein digestibility and metabolizable energy availability of barley ration in response to Grind[R] enzyme in broiler chickens.
Cereals are the major part of a poultry diet and primary sources of feed energy. Balancing the energy to protein ratio is a fundamental principle of feed formulation (Classen and Stevens, 1995). Birds adjust their feed intake to obtain a constant energy intake (Lesson et al., 1996). However, the energy a bird obtains from a cereal is variable and depends on its availability to the bird and the presence or concentration of anti-nutritive compounds such as soluble non- starch polysaccharide (NSP), especially [beta]-glucan in barley. Effect of age of bird on feedstuffs which contain anti-nutrients, such as [beta]-glucan in barley, is important. Decreasing growth rate by barley [beta]-glucan in young chickens could be reduced by fungal or bacterial enzyme in the diet (Campbell and Bedford, 1992). Determination of nutritive values (available energy and protein) of the diet is critical in the poultry industry. Estimation of chemical energy in feedstuff is relatively easy; however, this estimation in birds is not precise and measurement of metabolizable energy is common (Scott et al., 1998). To improve dietary efficiency, it is necessary to elucidate the exact amino acid requirements of poultry (Ishibashi and Yonemochi, 2002). The quality of a feed protein depends not only on nitrogen content, but also on constituent amino acids and their digestibility (Ravindran and Bryden, 1999). Diet formulation based on digestible amino acids will allow the use of alternative protein sources with low digestibility coefficients, because such formulation will improve the precision of least-cost diets and reduce nitrogen excretion from poultry operations (Perttila et al., 2002; Lemme et al., 2004). Although the advantages of the digestible amino acid system are recognized, diet formulation based on the total amino acid content is still widely used in many parts of the world. Because corn and soybean meal, most commonly used in poultry rations, have a high amino acid digestibility, the benefits of switching to the digestible amino acid system would be relatively small. In the future, however, economic reasons will compel the poultry industry to increase the use of an array of cheaper, alternative protein supplements with low digestibility coefficients in feed formulation. In broiler diet formulation, attention should be given to economical and maximum poultry performance (Schutte and Pack, 1995). Therefore, the main objective of the present study was to evaluate the influence of a commercial enzyme (Grind[R]; Danisco, Finland) and site of sampling (excreta and ileum) on estimation of metabolizable energy, protein and, particularly, amino acid digestibility of barley by marker in broiler chickens.
MATERIAL AND METHODS
In this experiment, 90-day-old unsexed Arbor Acres broiler chicks were transported from a commercial hatchery to the poultry research farm at the Bu-Ali Sina University on January 20 through March 3 2007 (d 1). The animal care committee in Bu-Ali Sina University approved this experiment. Chicks were placed on wood shavings litter in environmentally controlled chambers. The temperature and lighting regime were arranged based on Arbor Acres commercial broiler chicken recommendations. Chicks were fed a commercial starter diet for a 16-d pre-experimental period and, after four h of feed deprivation, were randomly distributed into experimental groups (three treatments, six replicates and five birds in each) in such a way that all groups had a similar average weight. All diets were given in mash form with birds having free access to water and feed throughout the experiment. The basal diet used during the experimental period was based on corn and soybean meal as major ingredients (Table 1). Barley (as test ingredient) was included in the basal diet at level of 40% to form test diets. The crude protein and metabolizable energy contents of basal and experimental diets were 18.26%, 3,025.97 kcal/kg, and 14.62%, 2,859.23 kcal/kg, respectively. The basal diet was calculated to satisfy the chick's requirements according to Arbor Acres recommended requirements. Chromic oxide was included in all diets (0.5%) as an indigestible marker. The test diet divided into two portions and enzyme was supplemented to one of these at 0.5 kg/ton. The crude enzyme preparation used in this study was Grind enzyme (a commercial multienzyme complex produced from a selected strain of Aspergillus niger that hydrolyzes a broad range of carbohydrates). The supplier (Danisco, Finland) reported that the crude enzyme contained endo-1, 3 (4) pglucanase (6,000 U/g), and endo-1,4-p-xylanase (12,000 U/g). The activity of each enzyme was determined by the supplier according
to the Nelson-Somogyi method for the determination of reducing sugar content (Somogyi, 1960). The enzyme preparation was added directly to other ingredients according to the supplier's recommendations.
Apparent metabolizable energy, corrected by nitrogen, and its availability
At 16 days of age, birds were transferred to metabolism cages. After a 4-d (Kadim and Moughan, 1997) adaptation period to experimental diets (without marker), the birds were deprived of feed for 6 h, then allowed ad libitum feed and water consumption for 3 d. Total excreta was collected during the balance period (3 d) and frozen at -20[degrees]C. Then, chickens were fed experimental diets for a further day and were euthanized and the contents of the ileum (from the Meckel's diverticulum to 4 cm above the ileo-caecal junction) were collected (26 d of age) and frozen at -20[degrees]C for further analysis (Scott et al., 1998). Before analysis, the frozen samples were removed from the freezer, dried and ground. Dry matter and crude protein of diets and excreta were determined by methods according to the Association of Official Analytical Chemists (AOAC, 1990). Chromic oxide was determined spectrophotometrically by the method of Fenton and Fenton (1979). Gross energy contents of diets and excreta were determined using an adiabatic bomb calorimeter. The diet AMEn was multiplied by a factor of 1.0474 to compensate for the test and basal diets having 4.88% of premix (oyster shell, dicalcium phosphate, salt, chromic oxide, vitamin and mineral premix) per 95.12 of macro ingredients (Sibbald and Slinger, 1963; Newkirk et al., 1997; Saki et al., 2008). Therefore, the AMEn of barley was calculated as: AMEn of barley = ((test diet AMEn-basal diet AMEnx0.6)/4)x10).
Diet and barley protein digestibility
Protein digestibility of diets and barley was determined using the procedures described by Ten Doeschate et al. (1993) as follow:
[DC.sub.diet] = 1-[([M.sub.diet]/[M.sub.i,e] x [C.sub.i,e]/[C.sub.diet])]
Where [DC.sub.diet], digestibility coefficient of protein in diet; [M.sub.diet], marker concentration in diet; [M.sub.i,e], marker concentration in ileal digesta (i) or excreta (e); [C.sub.diet], concentration of protein in diet; [C.sub.i,e], concentration of protein in ileal digesta (i) or excreta (e).
[DC.sub.barley] = [[DC.sub.test] X [C.sub.test] - [DC.sub.basal] X [C.sub.basal] X 0.6/ [C.sub.test] - [C.sub.basal] x 0.6]
Where [DC.sub.barley], digestibility coefficient of protein in the barley; [DC.sub.basal], digestibility coefficient of protein in the basal diet; [DC.sub.test], digestibility coefficient of protein in the test diet; [C.sub.basal], digestibility coefficient of protein in basal diet; [C.sub.test], the concentration of protein in the test diet.
Amino acid digestibility
Amino acid concentrations in diets, excreta, and ileal digesta were determined by high performance liquid chromatography (HPLC) by the method of Ravindran and Bryden (1999). Apparent amino acid digestibility of diet was determined by the method described by Ten Doeschate et al. (1993) as follows:
[AD.sub.AA] = 1 [([M.sub.diet]/[M.sub.i,e]) x [A.sub.i,e]/[A.sub.diet])]
Where [AD.sub.AA], apparent digestibility of individual amino acid; [M.sub.diet], marker concentration in diet; [M.sub.i,e], marker concentration in ileal digesta (i) or excreta (e); [A.sub.diet], concentration of each amino acid in diet; [A.sub.i,e], concentration of each amino acid in ileal digesta (i) or excreta (e).
The experiment was designed and statistically analyzed as a 2x2 factorial arrangement of two sites of sampling and two levels of enzyme based on a completely randomized design. Body weight at 16d was used as a covariate. The following statistical model (SAS, 2004) was used to assess the main effect of sampling site (S); the main effect of enzyme (D); and the corresponding interaction S x D:
[Y.sub.ijk] = [mu]+[S.sub.i]+[D.sub.j]+[S.sub.i]x[D.sub.j]+[e.sub.ijk]
Where [Y.sub.ijk], observed trait; [mu], overall mean; [S.sub.i], effect of sampling site; [D.sub.j], effect of enzyme; [S.sub.i][D.sub.j], interaction of [D.sub.j] and [S.sub.i]; and [e.sub.ijk], random error.
Duncan's multiple-range test was used to determine significant difference among treatment means.
Apparent metabolizable energy, corrected by nitrogen, and its availability
Results on AME, AMEn and AME availability are summarized in Table 2. No significant effects of enzyme inclusion were found on AME, AMEn and AME availability (p>0.05). The AME, AMEn and AME availabilities based on ileal measurement were significantly lower than the corresponding measurement based on excreta samples (p<0.05). The interaction of site of sampling by enzyme was not significant for these parameters (p>0.05).
Diet and barley protein digestibility
Results on protein digestibility of diet and barley are summarized in Table 3 and 4, respectively. No reaction was observed on protein digestibility of diets by enzyme inclusion (p>0.05). The ileal protein digestibility of diets was significantly higher than the excreta protein digestibility (p<0.05, Table 3). Barley protein digestibility at the ileum was significantly higher rather than in excreta (p<0.05). No reaction was found by inclusion of enzyme on barley protein digestibility (p>0.05). The sampling sitex enzyme interaction for protein digestibility of diet and barley was also not significant (p = 0.2117, and p = 0.0561, respectively).
Amino acid digestibility
Results of apparent digestibility of amino acids are summarized in Table 5. Apparent digestibilities of diet aspartic acid, glutamic acid, serine, glysine, alanine, valine, tyrosine and methionine were significantly (p<0.05) higher in excreta in comparison to ileal samples. Significant increases in digestibility of tryptophan, proline, methionine, phenylalanine and lysine were achieved by enzyme inclusion (p<0.05). Interaction between sampling site and enzyme was not significant for apparent digestibility of aspartic acid, glutamic acid, histidine, glycine, arginine, phenylalanine, isoleucine, alanine, tryptophan, and serine (p>0.05).
Methionine and glutamic acid digestibility were significantly (p<0.05) higher in excreta collected from chicks fed diet with enzyme than on other treatments. In contrast, tryptophan digestibility in this treatment was significantly lower compared to other treatments (p<0.05). Maximum lysine digestibility between treatments was observed from the ileum of chicks fed enzyme supplemented diet, and a similar trend was observed for phenylalanine.
Treatments effects on digestibility of isoleucine, arginine, and serine were not significant (p>0.05).
AME and AMEn were significantly higher in feces (2,740.5 and 2,634.4kcal/kg) than ileum (2,009.3 and 1,856.8 kcal/kg). These observations may be related to the higher fiber and [beta]-glucan content of barley. The undigested fiber provided a significant feed source for an adaptable gut microflora population. Also, a mature gut (e.g., capacity) and a mature endogenous enzyme system provide other positive conditions in the bird gut to access these fibrous substance (Graham and Aman, 1991; Schutte et al., 1992). The values of AME and AMEn measured in this study were lower than results of Scott et al. (1998). The difference may be related to composition of diet (proportion of test ingredient in diet, 20 versus 40% barley in Scott et al. (1998) and our investigations, respectively). Therefore, this variation may be related to other factors such as [beta]-glucan, variety and seed quality (Slominski et al., 1999), and availability of protein and amino acid (Zhang et al., 1994). Anti-nutritional effects of [beta]-glucan can be decreased by utilization of enzymes. Numerous studies made since the 1960s have confirmed that addition of enzyme preparations containing [beta]-glucanase to diets containing a high proportion of barley increases the AME content (Chesson, 1992). Subsequent works by Broz and Frigg (1986) and Brufau et al. (1991) suggested that these observations can be generalized to the destruction of any gel-forming polysaccharide leached from barley cell wall which depressed AME in the diet. AME content has an adverse relationship with [beta]-glucan level and viscosity in the ileum. Scott et al. (1998) reported that addition of enzymes in the diet increased AME, but in the current study no such outcome was obtained (p>0.05). Differences between AME content of excreta and ileum, were higher in the diet with enzyme than when enzyme was absent. These differences could be due to microbial fermentation in the distal intestine in this experiment. Similar results were achieved by Scott et al. (1998).
Enzyme inclusion had no significant effect on protein digestibility of the diet as well as barley (p>0.05). In recent years, protein digestibility by ileum sampling has been accepted in pigs, since superior estimation of digestibility was obtained rather than from excreta; however, in poultry less attention was given in this respect, because microbial processing effects in the cecum and colon of poultry on nutrient digestibility have less importance. Feed digestibility coefficient is affected by age, sex, genotype and experiment method, and it is necessary to evaluate accurately digestibility coefficients for these factors. Zenella et al. (1999) noted that protein digestibility was reduced by aging while amino acid digestibility increased, but no response was found to sex in this respect. Occasionaly, apparent digestibilities of amino acids in excreta were higher than at the ileum. This means that amino acids have disappeared during passage from the terminal ileum to the end of the digestive tract. Uptake of amino acids and other nitrogenous compounds is not thought to take place after the terminal ileum (Webb, 1990). Therefore, amino acid disappearance may have arisen by some other routes, for instance by microbial fermentation. Microbial metabolism of amino acids in the poultry hindgut comprises the degradation and synthesis of these materials (Ravindran et al., 1999; Kadim et al., 2002). Therefore, the disappearance of amino acids in poultry hindgut is determined by a balance of catabolism and anabolism of amino acids. When the net result is catabolism, the output of amino acids in excreta will be decreased, resulting in the overestimation of amino acid digestibility. But, when the net result is anabolism of amino acids, under-estimation of digestibility may occur. In net catabolism, ammonia may be absorbed but not utilized by the birds and completely excreted in the urine as uric acid (Salter, 1974). In addition, fiber impedes protein utilization in the small intestine of poultry. The mechanism of fiber on digestibility of protein is not clear, but the indigestible protein fraction in the feed may be bound to, or encapsulated by fibrous components of the feed (Jensen et al., 1995). Therefore, with lower digestible ingredients such as barley, more undigested nitrogenous substance will reach the hindgut. Grind enzyme also increased apparent digestibility of excreta amino acids in several cases. Ileum digestibility had advantages rather than excreta digestibility in this regard. Nutrient digestibility in feedstuff may aid diet formulation, improve protein utilization and reduce nitrogen excretion. In past years, digestibility of amino acids was obtained by the Sibbald technique (1979) and precise feeding. This procedure is simple but had great problems. Therefore, ileum sampling could remove the undesirable effect of microbial fermentation in the large intestine. However, the influence of hindgut microflora on protein nutrition in chickens is not clearly established. In contrast to our results, Papadopoulos (1985) reported that the influence of the avian hindgut on protein nutrition is insignificant and that there is little advantage, over conventional excreta analysis, in using other methods to determine amino acid digestibility in chickens. Commonly adult roosters were used for digestibility assay, and results were used for diet formulation in chickens; however, roosters are physiologically different from chicks. Thus, it is better to use chicks in digestibility assays. In barley, anti-nutritional factors are important agents in reduction of apparent protein digestibility. Inclusion of enzyme in broiler diets could increase apparent digestibility of amino acids and destroy anti-nutritional factors of feedstuffs. Increased endogenous enzymes and diminished fermentation in the gastrointestinal tract were achieved by [beta]-glucanase and thereby increased nutrient absorption. These outcomes are in agreement with the results of Perttila et al. (2001), Biadoo et al. (1998) and Ten Doeschate et al. (1993).
According to results of the current study, Grind enzyme addition can increase apparent digestibility of some amino acids. In contrast, no improvements were achieved in AME, AMEn, and protein digestibility of diets and barley by enzyme inclusion. Sampling site is important to estimate digestibility of protein and amino acids that is dependent on type of animal and diet. Apparent digestibility of aspartic acid, glutamic acid, serine, glycine, alanine, tyrosine, valine and methionine were greater in feces than ileum. However in other amino acids, there were no differences between digestibility coefficients achieved by ileum or excreta samples. Values of AME and AMEn in feces are more valid than in the ileum; on the other hand, estimation of protein digestibility in the ileum shows better results than feces in poultry.
Our special thanks to Bu-Ali Sina University for providing facilities and financial support for this study. We also wish to thank to the staff of the Department of Animal Science of this university for their excellent scientific collaboration.
AOAC. 1990. Official Methods of Analysis. 15th edn. Association of Official Analytical Chemists. Arlington, Virginia.
Biadoo, S. K., Y. G. Lui and D. Yungbiut. 1998. Effect of microbial enzyme supplementation on energy, amino acid digestibility and performance of pigs fed hulless barley based diets. Can. J. Anim. Sci. 78:625-631.
Borin, K., B. Ogle and J. E. Lindberg. 2002. Methods and techniques for the determination of amino acid digestibility: A Review. Livest. Res. Rural Dev. 14(6).
Broiler Manual for Arbor Acres. 2006. Feed Specifications for As Hatched Broilers grown. Arbor Acres service bulletin.
Broz, J. and M. Frigg. 1986. Effects of beta-glucanase on the feeding of broiler diets based on barley or oats. Arch. Gefluegelkd. 50:41-47.
Brufau, J., C. Nogareda, A. Perez-Vendrell, M. Franncesch and E. Esteve-Garcia. 1991. Effects of Trichoderma viride enzymes in pelleted broiler diets based on barley. Anim. Feed Sci. Technol. 34:193-202.
Campbell, G. L. and M. R. Bedford. 1992. Enzyme applications for monogastric feeds: A review. Can. J. Anim. Sci. 72:449-466.
Chesson, A. 1992. Effects of supplementary enzymes in barley diets. Options Mediterr., Ser. A. 20:55-62.
Classen, H. L. and J. P. Stevens. 1995. Poultry production. In: Nutrition and growth. (Ed. P. Hunton) Elsevier. pp. 79-99.
Fenton, T. W. and M. Fenton. 1979. An improved procedure for the determination of chromic oxide in feed and feces. Can. J. Anim. Sci. 59:631-634.
Graham, H. and P. Aman. 1991. Nutrition aspects of dietary fibres. Anim. Feed Sci. Technol. 32:143-158.
Ishibashi, T. and C. Yonemochi. 2002. Possibility of amino acid nutrition in broiler. Anim. Sci. J. 73:155-165.
Jensen, S. K., Y. G. Liu and B. O. Eggum. 1995. The effect of heat treatment on glucosinolates and nutritional value of rapeseed meal in rats. Anim Feed Sci. Technol. 53:17-28.
Kadim, I. T. and P. J. Moughan. 1997. Development of an ileal amino acid digestibility assay for the growing chiken- effect of time after feeding and site of sampling. Br. Poult. Sci. 38:89-95.
Kadim, I. T., P. J. Moughan and V. Ravindran. 2002. Ileal amino acid digestibility assay for the growing meat chicken comparison of ileal and excreta amino acid digestibility in the chicken. Br. Poult. Sci. 43(4):587-597.
Lesson, S., L. Caston and J. D. Summers. 1996. Broiler response to diet energy. Poult. Sci. 75:529-535.
Lemme, A., V. Ravindran and W. L. Bryden. 2004. Ileal digestibility of amino acids in feed ingredients for broilers. World's Poult. Sci. J. 60:514-517.
Newkirk, R. W., H. L. Classen and R. T. Tyler. 1997. Nutritional evaluation of low glucosinolate mustard meals (Brassica juncea) in broiler diets. Poult. Sci. 76:1272-1277.
Papadopoulos, M. C. 1985. Estimation of amino acid digestibility and availability in feedstuffs for poultry. World's Poult. Sci. J. 41:64-71.
Perttila, S., J. Valaja, K. Partanet, T. Jalava and E. Venalainen. 2002. Apparent ileal digestibility of amino acids in protein feedstuffs and diet formulation based on total vs digestible lysin for poultry. Anim. Feed Sci. Technol. 98:203-218.
Perttila, S., J. Valaja, K. Partanet, T. Jalava, T. Kiskinen and S. Palander. 2001. Effect of preservation method and [beta]-glucanase supplementation on ileal amino acid digestibility and feeding value of barley for poultry. Br. Poult. Sci. 42:218-229.
Ravindran, V., L. I. Hew, G. Ravindran and W. L. Bryden. 1999. Acomparison of ileal digesta and excreta analysis for the determination of amino acid digestibility in food ingredients for poultry. Br. Poult. Sci. 40:266-274.
Ravindran, V. and W. L. Bryden. 1999. Amino acid availability in poultry-in vitro and in vivo measurements. Aust. J. Agric. Res. 50:889-908.
Saki, A. A., H. Mahmoudi, M. M. Tabataei and A. Ahmadi. 2008. The availability of energy and protein, respect to uric acid, of yellow-seeded rapeseed meal in broiler diets. Asian-Aust. J. Anim. Sci. 21(11):1624-1628.
Salter, D. N., M. E. Coates and D. Hewitt. 1974. The influence of gut microflora on the digestion of dietary and endogenous protein studies on the amino acid composition of the excreta of germ-free and conventional animals. Br. J. Nutr. 31:307-318.
SAS Institute Inc. 2004. SAS/STAT User's Guide: Version9. 8th edn. SAS Institute Inc., Cary, North Carolina.
Schutte, J. B., J. De Jong, E. J. Van Weerden and M. J. Van Baaik. 1992. Nutrition value of D-xylose and L-arabinose for broiler chicks. Br. Poult. Sci. 33:89-100.
Schutte, J. B. and M. pack. 1995. Effects of dietary sulfur containing amino acids on performance and breast deposition of broiler chicks during growing and finishing phases. Br. Poult. Sci. 36:747-762.
Scott, T. A., F. G. Silversides, H. L. Classen, M. L. Swift and M. R. Bedford. 1998. Comparison of sample source (excreta or ileal digesta) and age of broiler chick on measurement of apparent digestible energy of wheat and barley. Poult. Sci. 77:456-463.
Sibbald, I. R. 1979. Passage of food through the adult rooster. Poult. Sci. 58:446-459.
Sibbald, I. R. and S. J. Slinger. 1963. A biological assay for metabolizable energy in poultry feed ingredients together with findings which demonstrate some of the problems associated with the evaluation of fats. Poult. Sci. 42:313-325.
Somogyi, M. 1960. Modification of two methods for the assay of amylase. Clin. Chem. 6:23-35.
Slominski, B. A., J. Simbaya, L. D. Campbell, G. Rakow and W. Guenter. 1999. Nutritive value for broilers of meals derived from newly developed varieties of yellow-seeded canola. Anim. Feed Sci. Technol. 78:249-262.
Ten Doeschate, R. A. H. M., C. W. Scheele, V. V. A. M. Schreurs and J. D. Vanderklis. 1993. Digestibility studies in broiler chickens: Influence of genotype, age, sex and method of determination. Br. Poult. Sci. 34:131-146.
Webb, K. E. 1990. Intestinal absorbtionof protein hydrolysis products. A review. J. Anim. Sci. 6:3011-3022.
Zanella, I., N. K. Sakomura, F. G. Silversides, A. Fiqueird and M. pack. 1999. Effect of enzyme supplementation of broiler diets based on corn and soybeans. Poult. Sci. 78:561-568.
Zhang, W. G., L. D. Campbell and S. C. Stothers. 1994. An investigation of the feasibility of the predicting nitrogen-corrected true metabolisable energy content in barley from chemical composition. Can. J. Anim. Sci. 74:335-360.
A. A. Saki *, S. Mirzayi (1), Sh. Ghazi (1), M. M. Moini1 and R. Naseri Harsini
Department of Animal Science, Faculty of Agriculture, Bu-Ali Sina University, Hamedan, Iran
* Corresponding Author: Ali Asghar Saki. Tel: +98-918-3139775, Fax: +98-811-8273126, E-mail: firstname.lastname@example.org
(1) Department of Animal Science, Faculty of Agriculture, Razi University, Kermanshah-Iran.
Received June 12, 2009; Accepted September 23, 2009
Table 1. Formulation of rations and diet composition (%) Barley- Barley+ Basal Ingredients (%) enzyme enzyme diet Corn 63.58 36.60 36.60 Soybean meal 29.22 16.15 16.15 Barley -- 40 40 Soybean oil 2.39 2.39 2.39 Oyster shell 1.50 1.50 1.50 Dicalcium phosphate (1) 1.91 1.91 1.91 Sodium chloride 0.33 0.33 0.33 Vitamin mix (2) 0.25 0.25 0.25 Mineral mix (3) 0.25 0.25 0.25 DL-met (98.5%) 0.07 0.07 0.07 enzyme -- 0.05 -- Chrome oxide 0.5 0.5 0.5 Calculated analysis ME (Kcal/kg) 3,025.97 2,859.23 2,859.23 CP (%) 18.26 14.62 14.62 Ca (4) (%) 1.08 1.12 1.12 NPP (5) (%) 0.47 0.49 0.49 Na (%) 0.15 0.22 0.22 Met (%) 0.37 0.31 0.31 Lys (%) 1.03 0.73 0.73 Met+cys (%) 0.70 0.59 0.59 (1) Contains 18.7% P and 22% Ca. (2) Supplied per kg of vitamin mixture: Vitamin A, 7.2 g; Vitamin D, 7.0 g; Vitamin E, 14.4 g; Vitamin [K.sub.3], 1.6 g; Vitamin [B.sub.1], 0.72 g; Riboflavin, 3.3 g; Pantothenic acid, 12 g; niacin, 12,160 mg; Vitamin [B.sub.6], 6.2 mg; Biotin, 0.2 g; Vitamin [B.sub.12], 0.6 g; choline chloride, 440 mg. (3) Supplied per kg of mineral mixture: manganese (oxide), 64 g; iron (FeS[O.sub.4]), 100 g; zinc (oxide), 44 g; copper (CuS[O.sub.4]), 16 g; iodine (calcium iodate), 64 g; selenium (1%), 8 g; cobalt, 0.2 g. (4) Calculated from tabular values (NRC, 1994). (5) NPP, nonphytate P. Table 2. Comparison of AME, AMEn and availability of AME AME (1) AMEn (2) Source of variation (kcal/kg) (kcal/kg) Sample source (S) ileum 2,009.3 (b) 1,856.8 (b) excreta 2,740.5 (a) 2,634.4 (a) p <0.0001 <0.0001 Enzyme level (D) 0 2,369.7 (a) 2,236.9 (a) (kg/ton) 0.5 2,380.2 (a) 2,254.3 (a) p 0.6244 0.4020 S x D p 0.0744 0.0918 Combination effects Sample source x 0.5 x ileum 2,084.21 [+ or 1,933.1 [+ or enzyme level -] 326 (b) -] 0.31 (b) 0 x ileum 1,934.43 [+ or 1,780.4 [+ or -] 216 (b) -] 0.21 (b) 0.5 x excreta 2,804.91 [+ or 2,693.4 [+ or -] 167 (a) -] 0.14 (a) 0 x excreta 2,676.12 [+ or 2,575.4 [+ or -] 125 (a) -] 0.12 (a) p 0.0031 0.0015 MSE 4,943.27 4,480.65 Source of variation AME availability (%) Sample source (S) ileum 0.48 (b) excreta 0.65 (a) p <0.0001 Enzyme level (D) 0 0.56 (a) (kg/ton) 0.5 0.56 (a) p 0.4815 S x D p 0.0635 Combination effects Sample source x 0.5 x ileum 0.49 [+ or -] 0.07 (b) enzyme level 0 x ileum 0.46 [+ or -] 0.05 (b) 0.5 x excreta 0.67 [+ or -] 0.04 (a) 0 x excreta 0.63 [+ or -] 0.03 (a) p 0.0031 MSE 0.0028 Means with common superscripts in same column are not significantly different (p<0.05). (1) Apparent metabolizable energy. (2) Apparent metabolizable energy corrected by nitrogen. Table 3. A comparison of in vivo diet protein digestibility (%) Source of variation Diet protein digestibility Sample source (S) ileum 60.24 (a) excreta 41.80 (b) p 0.0004 Enzyme level (D) 0 52.20 (a) (kg/ton) 0.5 50.20 (a) p 0.4889 SxD p 0.2117 Combination effects Sample source 0.5 x ileum 59.96 [+ or -] 0.06 (a) x enzyme level 0 x ileum 60.52 [+ or -] 0.03 (a) 0.5 x excreta 43.88 [+ or -] 0.07 (b) 0 x excreta 39.71 [+ or -] 0.02 (b) p 0.0024 MSE 0.0028 Means with common superscripts in same column are not significantly different (p<0.05). Table 4. A comparison of in vivo barley protein digestibility (%) Source of variation Barley's protein digestibility Sample source (S) ileum 52.77 (a) excreta 41.79 (b) p 0.0001 Enzyme level (D) 0 44.26 (a) (kg/ton) 0.5 50.30 (a) p 0.4889 SxD p 0.0561 Combination effects Sampling site 0.5 x ileum 60.90 [+ or -] 1.85 (a) x enzyme level 0 x ileum 44.64 [+ or -] 8.48 (b) 0.5 x excreta 39.71 [+ or -] 2.23 (b) 0 x excreta 43.88 [+ or -] 7.61 (b) p 0.2544 MSE 0.0112 Means with common superscripts in same column are not significantly different (p<0.05). Table 5. i) Amino acid digestibility of diets (%) Source of variation Aspartic acid Glutamic acid Sample source (S) ileum 65.06 (b) 73.24 (b) excreta 71.17 (a) 83.63 (a) p 0.0001 <0.0001 Enzyme level (D) 0 66.14 (a) 76.72 (a) (kg/ton) 0.5 70.09 (a) 80.15 (a) p 0.0884 0.3681 SxD p 0.0741 0.6423 Combination effects Sample source 0.5 x ileum 67.44 [+ or -] 73.66 [+ or -] x enzyme level 1.07 (ab) 1.61 (c) 0 x ileum 62.69 [+ or -] 72.83 [+ or -] 3.06 (b) 0.26 (c) 0.5 x excreta 72.75 [+ or -] 86.65 [+ or -] 0.55 (a) 0.77 (a) 0 x excreta 69.60 [+ or -] 80.62 [+ or -] 3.39 (a) 3.39 (b) p 0.2168 0.8760 MSE 16.38 23.01 Source of variation Histidine Glycine Sample source (S) ileum 76.02 (a) 68.66 (b) excreta 73.64 (a) 76.27 (a) p 0.0061 0.0001 Enzyme level (D) 0 73.09 (a) 72.19 (a) (kg/ton) 0.5 76.57 (a) 72.74 (a) p 0.2436 0.9923 SxD p 0.4330 0.3679 Combination effects Sample source 0.5 x ileum 78.08 [+ or -] 69.75 [+ or -] x enzyme level 1.29 (a) 1.76 (b) 0 x ileum 73.97 [+ or -] 67.57 [+ or -] 0.02 (ab) 1.29 (b) 0.5 x excreta 75.07 [+ or -] 75.74 [+ or -] 1.45 (ab) 0.79 (a) 0 x excreta 72.22 [+ or -] 76.81 [+ or -] 3.39 (b) 3.39 (a) p 0.1472 0.4759 MSE 3.82 40.7 Source of variation Arginine Sample source (S) ileum 67.59 (a) excreta 71.41 (a) p 0.0005 Enzyme level (D) 0 69.83 (a) (kg/ton) 0.5 69.17 (a) p 0.6724 SxD p 0.9264 Combination effects Sample source 0.5 x ileum 66.80 [+ or -] 0.27 (a) x enzyme level 0 x ileum 68.39 [+ or -] 2.84 (a) 0.5 x excreta 71.55 [+ or -] 0.63 (a) 0 x excreta 71.28 [+ or -] 3.29 (a) p 0.7605 MSE 8.49 Means with common superscripts in same column are not significantly different (p<0.05). Table 5. ii) Amino acid digestibility of diets (%) Source of variation Tyrosine Methionine Sample source (S) ileum 67.78 (b) 64.30 (b) excreta 72.47 (a) 81.35 (a) p 0.0031 0.0001 Enzyme level (D) 0 71.89 (a) 62.37 (b) (kg/ton) 0.5 68.36 (a) 83.28 (a) p 0.3679 0.0023 SxD p 0.0286 <0.0001 Combination effects Sample source 0.5 x ileum 69.50 [+ or 79.15 [+ or x enzyme level -] 0.70 (b) -] 1.20 (b) 0 x ileum 66.06 [+ or 49.45 [+ or -] 0.66 (b) -] 3.39 (c) 0.5 x excreta 67.22 [+ or 84.41 [+ or -] 1.09 (b) -] 0.83 (a) 0 x excreta 77.73 [+ or 75.29 [+ or -] 3.39 (a) -] 0.31 (b) p 0.0105 0.0001 MSE 3.41 3.44 Source of variation Isoleucine Phenylalanine Sample source (S) ileum 73.08 (a) 74.45 (a) excreta 75.32 (a) 79.77 (a) p 0.06318 0.0566 Enzyme level (D) 0 72.76 (a) 71.61 (b) (kg/ton) 0.5 75.64 (a) 82.61 (a) p 0.2895 0.0001 SxD p 0.8442 0.0539 Combination effects Sample source 0.5 x ileum 75.13 [+ or 83.05 [+ or x enzyme level -] 1.23 (a) -] 1.34 (a) 0 x ileum 71.03 [+ or 65.85 [+ or -] 3.39 (a) -] 3.39 (b) 0.5 x excreta 76.15 [+ or 82.17 [+ or -] 1.20 (a) -] 1.17 (a) 0 x excreta 74.50 [+ or 77.37 [+ or -] 2.45 (a) -] 7.84 (ab) p 0.2669 0.0503 MSE 5.12 19.04 Source of variation Lysine Sample source (S) ileum 74.37 (a) excreta 74.72 (a) p 0.5942 Enzyme level (D) 0 71.49 (b) (kg/ton) 0.5 77.59 (a) p 0.0311 SxD p 0.0454 Combination effects Sample source 0.5 x ileum 77.06 [+ or -] 1.32 (a) x enzyme level 0 x ileum 69.68 [+ or -] 3.39 (b) 0.5 x excreta 76.12 [+ or -] 1.23 (a) 0 x excreta 73.31 [+ or -] 1.83 (ab) p 0.0447 MSE 4.53 Means with common superscripts in same column are not significantly different (p<0.05). Table 5. iii) Amino acid digestibility of diets (%) Source of variation Serine Tryptophan Sample source (S) ileum 68.71 (b) 70.42 (a) excreta 72.49 (a) 63.69 (b) p 0.0052 0.0004 Enzyme level (D) 0 70.11 (a) 63.42 (b) (kg/ton) 0.5 71.09 (a) 70.69 (a) p 0.2391 0.0001 S x D p 0.5626 0.0638 Combination effects Sample source 0.5 x ileum 69.45 [+ or 72.78 [+ or x enzyme level -] 0.77 (a) -] 0.44 (a) 0 x ileum 67.97 [+ or 68.06 [+ or -] 0.85 (a) -] 1.63 (a) 0.5 x excreta 72.73 [+ or 54.06 [+ or -] 0.52 (a) -] 1.32 (b) 0 x excreta 72.26 [+ or 73.33 [+ or -] 3.39 (a) -] 3.39 (a) p 0.1484 0.0019 MSE 3.28 4.03 Source of variation Alanine Proline Sample source (S) ileum 70.49 (b) 79.64 (a) excreta 77.99 (a) 82.89 (a) p 0.0001 0.0652 Enzyme level (D) 0 72.37 (a) 76.56 (b) (kg/ton) 0.5 76.11 (a) 85.97 (a) p 0.1517 0.0001 S x D p 0.08291 0.0138 Combination effects Sample source 0.5 x ileum 71.75 [+ or 83.45 [+ or x enzyme level -] 3.18 (b) -] 0.77 (ab) 0 x ileum 69.23 [+ or 75.84 [+ or -] 1.08 (b) -] 3.39 (b) 0.5 x excreta 80.47 [+ or 88.50 [+ or -] 0.74 (a) -] 2.12 (a) 0 x excreta 75.51 [+ or 77.29 [+ or -] 3.39 (ab) -] 5.86 (b) p 0.0351 0.0696 MSE 5.84 12.76 Source of variation Valine Sample source (S) ileum 65.09 (b) excreta 74.64 (a) p 0.0001 Enzyme level (D) 0 69.41 (a) (kg/ton) 0.5 70.32 (a) p 0.2834 S x D p 0.0095 Combination effects Sample source 0.5 x ileum 67.27 [+ or -] 1.03 (bc) x enzyme level 0 x ileum 62.92 [+ or -] 4.13 (c) 0.5 x excreta 73.37 [+ or -] 0.88 (ab) 0 x excreta 75.91 [+ or -] 1.28 (a) p 0.0148 MSE 5.15 Means with common superscripts in same column are not significantly different (p<0.05).
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|Author:||Saki, A.A.; Mirzayi, S.; Ghazi, Sh.; Moini, M.M.; Harsini, R. Naseri|
|Publication:||Asian - Australasian Journal of Animal Sciences|
|Date:||May 1, 2010|
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