DOI QR코드

DOI QR Code

Effects of Heat-oxidized Soy Protein Isolate on Growth Performance and Digestive Function of Broiler Chickens at Early Age

  • Chen, X. (College of Animal Science and Technology, Nanjing Agricultural University) ;
  • Chen, Y.P. (College of Animal Science and Technology, Nanjing Agricultural University) ;
  • Wu, D.W. (College of Animal Science and Technology, Nanjing Agricultural University) ;
  • Wen, C. (College of Animal Science and Technology, Nanjing Agricultural University) ;
  • Zhou, Y.M. (College of Animal Science and Technology, Nanjing Agricultural University)
  • Received : 2014.08.11
  • Accepted : 2014.10.14
  • Published : 2015.04.01

Abstract

This study was conducted to investigate effects of heat-oxidized soy protein isolate (HSPI) on growth performance, serum biochemical indices, apparent nutrient digestibility and digestive function of broiler chickens. A total of 320 1-day-old Arbor Acres chicks were randomly divided into 4 groups with 8 replicates of 10 birds, receiving diets containing soy protein isolate (SPI, control group) or the same amount of SPI heated in an oven at $100^{\circ}C$ for 1, 4, or 8 h, for 21 days, respectively. The results indicated that compared with the control group, body weight gain and feed intake of birds fed diet containing SPI heated for 8 h were significantly lower (p<0.05). Serum urea nitrogen concentration was higher in the broilers fed diet containing SPI heated for 4 or 8 h at d 21 (p<0.05). In contrast, serum glucose content was decreased by HSPI substitution at d 21 (p<0.05). The relative pancreas weight in HSPI groups was higher than that in the control group at d 21 (p<0.05). Meanwhile, the opposite effect was observed for relative weight of anterior intestine and ileum in broilers fed a diet containing SPI heated for 8 h (p<0.05). Birds fed diets containing SPI heated for 4 or 8 h had a decreased lipase activity in anterior intestinal content at d 14 and 21 (p<0.05), respectively. In addition, the same effect was also noted in broilers given diets containing SPI heated for 1 h at d 21 (p<0.05). Similarly, amylase, protease and trypsin activity in anterior intestinal content were lower in broilers fed diets containing SPI heated for 8 h at d 21 (p<0.05). The apparent digestibility of dry matter (DM) from d 8 to 10 and DM, crude protein (CP), and ether extract from d 15 to 17 were lower in broilers fed diets containing SPI heated for 8 h (p<0.05). Besides, birds given diets containing SPI heated for 4 h also exhibited lower CP apparent digestibility from d 15 to 17 (p<0.05). It was concluded that HSPI inclusion can exert a negative influence on the growth performance of broilers, which was likely to result from the simultaneously compromised digestive function.

Keywords

Broilers;Digestion;Growth Performance;Heat-oxidized Soy Protein Isolate

Acknowledgement

Supported by : Jiangsu province in China

References

  1. AOAC. 1990. Official Methods of Analysis, 15th edn. Association of Official Analytical Chemists, Arlington, VA, USA.
  2. Chen, Y. P., X. Chen, H. Zhang, and Y. M. Zhou. 2013. Effects of dietary concentrations of methionine on growth performance and oxidative status of broiler chickens with different hatching weight. Br. Poult. Sci. 54:531-537. https://doi.org/10.1080/00071668.2013.809402
  3. Deeg, R. and J. Ziegenhorn. 1983. Kinetic enzymatic method for automated determination of total cholesterol in serum. Clin. Chem. 29:1798-1802.
  4. Denli, M., J. C. Blandon, M. E. Guynot, S. Salado, and J. F. Perez. 2009. Effects of dietary AflaDetox on performance, serum biochemistry, histopathological changes, and aflatoxin residues in broilers exposed to aflatoxin $B_1$. Poult. Sci. 88:1444-1451. https://doi.org/10.3382/ps.2008-00341
  5. Fossati, P. and L. Prencipe. 1982. Serum triglycerides determined colorimetrically with an enzyme that produces hydrogen peroxide. Clin. Chem. 28:2077-2080.
  6. Gatellier, P., V. Sante-Lhoutellier, S. Portanguen, and A. Kondjoyan. 2009. Use of meat fluorescence emission as a marker of oxidation promoted by cooking. Meat Sci. 83:651-656. https://doi.org/10.1016/j.meatsci.2009.07.015
  7. Gu, C. and H. Xu. 2010. Effect of oxidative damage due to excessive protein ingestion on pancreas function in mice. Int. J. Mol. Sci. 11:4591-4600. https://doi.org/10.3390/ijms11114591
  8. Headlam, H. A. and M. J. Davies. 2004. Markers of protein oxidation: Different oxidants give rise to variable yields of bound and released carbonyl products. Free Radic. Biol. Med. 36:1175-1184. https://doi.org/10.1016/j.freeradbiomed.2004.02.017
  9. Korhonen, H., A. Pihlanto-Leppala, P. Rantamaki, and T. Tupasela. 1998. Impact of processing on bioactive proteins and peptides. Trends Food Sci. Technol. 9:307-319. https://doi.org/10.1016/S0924-2244(98)00054-5
  10. Liukkonen-Anttila, T. 2001. Nutritional and Genetic Adaptation of Galliform Birds: Implications for Hand-rearing and Restocking. PhD Thesis, University of Oulu, Oulu, Finland. 73.
  11. Mahmood, S., R. Smithard, and M. Sarwar. 1997. Effects of salseed (Shorea robusta) tannins, restricted feed intake and age on relative pancreas weight and activity of digestive enzymes in male broilers. Anim. Feed Sci. Technol. 65:215-230. https://doi.org/10.1016/S0377-8401(96)01076-0
  12. Promeyrat, A., P. Gatellier, B. Lebret, K. Kajak-Siemaszko, L. Aubry, and V. Sante-Lhoutellier. 2010. Evaluation of protein aggregation in cooked meat. Food Chem. 121:412-417. https://doi.org/10.1016/j.foodchem.2009.12.057
  13. Renkema, J. M. S., H. Gruppen, and T. van Vliet. 2002. Influence of pH and ionic strength on heat-induced formation and rheological properties of soy protein gels in relation to denaturation and their protein compositions. J. Agric. Food Chem. 50:6064-6071. https://doi.org/10.1021/jf020061b
  14. Rideau, N., Z. Nitzan, and P. Mongin. 1983. Activities of amylase, trypsin and lipase in the pancreas and small intestine of the laying hen during egg formation. Br. Poult. Sci. 24:1-9. https://doi.org/10.1080/00071668308416707
  15. Sante-Lhoutellier, V., L. Aubry, and P. Gatellier. 2007. Effect of oxidation on in vitro digestibility of skeletal muscle myofibrillar proteins. J. Agric. Food Chem. 55:5343-5348. https://doi.org/10.1021/jf070252k
  16. Shacter, E. 2000. Quantification and significance of protein oxidation in biological samples. Drug Metab. Rev. 32:307-326. https://doi.org/10.1081/DMR-100102336
  17. Smet, K., K. Raes, G. Huyghebaert, L. Haak, S. Arnouts, and S. De Smet. 2008. Lipid and protein oxidation of broiler meat as influenced by dietary natural antioxidant supplementation. Poult. Sci. 87:1682-1688. https://doi.org/10.3382/ps.2007-00384
  18. Stadtman, E. R. 1990. Metal ion-catalyzed oxidation of proteins: biochemical mechanism and biological consequences. Free Radic. Bio. Med. 9: 315-325. https://doi.org/10.1016/0891-5849(90)90006-5
  19. Tang, C. H. and C. Y. Ma. 2009. Effect of high pressure treatment on aggregation and structural properties of soy protein isolate. LWT-Food Sci. Technol. 42:606-611. https://doi.org/10.1016/j.lwt.2008.07.012
  20. Tang, X., Q. Wu, G. Le, J. Wang, K. Yin, and Y. Shi. 2012a. Structural and antioxidant modification of wheat peptides modified by the heat and lipid peroxidation product malondialdehyde. J. Food Sci. 77:H16-H22. https://doi.org/10.1111/j.1750-3841.2011.02500.x
  21. Tang, X., Q. Wu, G. Le, and Y. Shi. 2012b. Effects of heat treatment on structural modification and in vivo antioxidant capacity of soy protein. Nutrition 28:1180-1185. https://doi.org/10.1016/j.nut.2012.03.011
  22. Thomas, L., W. Plischke, and G. Storz. 1982. Evaluation of a quantitative solid phase reagent system for determination of blood analytes. Experiences with the analytes: LDH, bilirubin, BUN, glucose, and uric acid. Ann. Clin. Biochem. 19:214-223. https://doi.org/10.1177/000456328201900403
  23. Witko-Sarsat, V., V. Gausson, and B. Descamps-Latscha. 2003. Are advanced oxidation protein products potential uremic toxins? Kidney Int. 63:S11-S14. https://doi.org/10.1046/j.1523-1755.63.s84.47.x
  24. Wen, C., L. C. Wang, Y. M. Zhou, Z. Y. Jiang, and T. Wang. 2012. Effect of enzyme preparation on egg production, nutrient retention, digestive enzyme activities and pancreatic enzyme messenger RNA expression of late-phase laying hens. Anim. Feed Sci. Technol. 172:180-186. https://doi.org/10.1016/j.anifeedsci.2011.11.012
  25. Wu, D. W., X. Chen, X. Yang, Z. X. Leng, P. S. Yan, and Y. M. Zhou. 2014. Effects of heat treatment of soy protein isolate on the growth performance and immune function of broiler chickens. Poult. Sci. 93:326-334. https://doi.org/10.3382/ps.2013-03507
  26. Zamora, R. and F. J. Hidalgo. 2001. Inhibition of proteolysis in oxidized lipid-damaged proteins. J. Agric. Food Chem. 49: 6006-6011. https://doi.org/10.1021/jf0102719
  27. Zhang, W., S. Xiao, E. J. Lee, and D. U. Ahn. 2011. Efects of dietary oxidation on the quality of broiler breast meat. Anim. Ind. Rep. AS 657, ASL R2624.

Cited by

  1. Digestive evaluation of soy isolate protein as affected by heat treatment and soy oil inclusion in broilers at an early age vol.87, pp.10, 2016, https://doi.org/10.1111/asj.12575
  2. and impairs growth performance and digestive function in broilers vol.58, pp.6, 2017, https://doi.org/10.1080/00071668.2017.1370535
  3. Effect of gut stress induced by oxidized wheat gluten on the growth performance, gut morphology and oxidative states of broilers vol.102, pp.2, 2018, https://doi.org/10.1111/jpn.12845