메뉴 건너뛰기




Volumn 93, Issue 2, 2014, Pages 326-334

Effects of heat treatment of soy protein isolate on the growth performance and immune function of broiler chickens

Author keywords

Broiler; Growth performance; Heat treated; Immune function; Soy protein isolate

Indexed keywords

SOYBEAN PROTEIN;

EID: 84893817197     PISSN: 00325791     EISSN: 15253171     Source Type: Journal    
DOI: 10.3382/ps.2013-03507     Document Type: Article
Times cited : (26)

References (49)
  • 1
    • 0030070186 scopus 로고    scopus 로고
    • Comparison of the effects of ozone on the modification of amino acid residues in glutamine synthetase and bovine serum albumin
    • Berlett, B. S., R. L. Levine, and E. R. Stadtman. 1996. Comparison of the effects of ozone on the modification of amino acid residues in glutamine synthetase and bovine serum albumin. J. Biol. Chem. 271:4177-4182.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4177-4182
    • Berlett, B.S.1    Levine, R.L.2    Stadtman, E.R.3
  • 2
    • 0019853695 scopus 로고
    • Studies of the mode of action of vitamin e in stimulating T-cell mitogenesis
    • Corwin, L. M., R. K. Gordon, and J. Shloss. 1981. Studies of the mode of action of vitamin E in stimulating T-cell mitogenesis. Scand. J. Immunol. 14:565-571.
    • (1981) Scand. J. Immunol. , vol.14 , pp. 565-571
    • Corwin, L.M.1    Gordon, R.K.2    Shloss, J.3
  • 3
    • 12844278044 scopus 로고    scopus 로고
    • The oxidative environment and protein damage
    • Davies, M. J. 2005. The oxidative environment and protein damage. Biochim. Biophys. Acta 1703:93-109.
    • (2005) Biochim. Biophys. Acta , vol.1703 , pp. 93-109
    • Davies, M.J.1
  • 4
    • 0002415964 scopus 로고    scopus 로고
    • Feeding of oxidized fats to broilers and swine: Effects on enterocyte turnover, hepatocyte proliferation and the gut associated lymphoid tissue
    • Dibner, J. J., C. A. Atwell, M. L. Kitchell, W. D. Shermer, and F. J. Ivey. 1996. Feeding of oxidized fats to broilers and swine: Effects on enterocyte turnover, hepatocyte proliferation and the gut associated lymphoid tissue. Anim. Feed Sci. Technol. 62:1-13.
    • (1996) Anim. Feed Sci. Technol. , vol.62 , pp. 1-13
    • Dibner, J.J.1    Atwell, C.A.2    Kitchell, M.L.3    Shermer, W.D.4    Ivey, F.J.5
  • 5
    • 33646745126 scopus 로고    scopus 로고
    • Protein thiol oxidation in health and disease: Techniques for measuring disulfides and related modifications in complex protein mixtures
    • Eaton, P. 2006. Protein thiol oxidation in health and disease: Techniques for measuring disulfides and related modifications in complex protein mixtures. Free Radic. Biol. Med. 40:1889-1899.
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 1889-1899
    • Eaton, P.1
  • 6
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
    • Esterbauer, H., R. J. Schaur, and H. Zollner. 1991. Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Radic. Biol. Med. 11:81-128.
    • (1991) Free Radic. Biol. Med. , vol.11 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 7
    • 58149498554 scopus 로고    scopus 로고
    • Oxidation of lipid and protein in horse mackerel (Trachurus trachurus) mince and washed minces during processing and storage
    • Eymard, S., C. P. Baron, and C. Jacobsen. 2009. Oxidation of lipid and protein in horse mackerel (Trachurus trachurus) mince and washed minces during processing and storage. Food Chem. 114:57-65.
    • (2009) Food Chem. , vol.114 , pp. 57-65
    • Eymard, S.1    Baron, C.P.2    Jacobsen, C.3
  • 8
    • 0031005562 scopus 로고    scopus 로고
    • Structural characterization of the products of hydroxyl-radical damage to leucine and their detection on proteins
    • Fu, S. L., and R. T. Dean. 1997. Structural characterization of the products of hydroxyl-radical damage to leucine and their detection on proteins. Biochem. J. 324:41-48.
    • (1997) Biochem. J. , vol.324 , pp. 41-48
    • Fu, S.L.1    Dean, R.T.2
  • 9
    • 46249104726 scopus 로고    scopus 로고
    • Effects of yeast culture in broiler diets on performance and immunomodulatory functions
    • Gao, J., H. J. Zhang, S. H. Yu, S. G. Wu, I. Yoon, J. Quigley, and G. H. Qi. 2008. Effects of yeast culture in broiler diets on performance and immunomodulatory functions. Poult. Sci. 87:1377-1384.
    • (2008) Poult. Sci. , vol.87 , pp. 1377-1384
    • Gao, J.1    Zhang, H.J.2    Yu, S.H.3    Wu, S.G.4    Yoon, I.5    Quigley, J.6    Qi, G.H.7
  • 10
    • 84862767862 scopus 로고    scopus 로고
    • Dietary l-arginine supplementation enhances placental growth and reproductive performance in sows
    • Gao, K. G., Z. Y. Jiang, Y. C. Lin, C. T. Zheng, G. L. Zhou, F. Chen, L. Yang, and G. Y. Wu. 2012. Dietary l-arginine supplementation enhances placental growth and reproductive performance in sows. Amino Acids 42:2207-2214.
    • (2012) Amino Acids , vol.42 , pp. 2207-2214
    • Gao, K.G.1    Jiang, Z.Y.2    Lin, Y.C.3    Zheng, C.T.4    Zhou, G.L.5    Chen, F.6    Yang, L.7    Wu, G.Y.8
  • 11
    • 0037421493 scopus 로고    scopus 로고
    • Oxidative stress: New approaches to diagnosis and prognosis in atherosclerosis
    • Heinecke, J. W. 2003. Oxidative stress: New approaches to diagnosis and prognosis in atherosclerosis. Am. J. Cardiol. 91:12A-16A.
    • (2003) Am. J. Cardiol. , vol.91
    • Heinecke, J.W.1
  • 12
    • 0033090173 scopus 로고    scopus 로고
    • Heat processing changes the protein quality of canned cat foods as measured with a rat bioassay
    • Hendriks, W. H., M. M. Emmens, B. Trass, and J. R. Pluske. 1999. Heat processing changes the protein quality of canned cat foods as measured with a rat bioassay. J. Anim. Sci. 77:669-676.
    • (1999) J. Anim. Sci. , vol.77 , pp. 669-676
    • Hendriks, W.H.1    Emmens, M.M.2    Trass, B.3    Pluske, J.R.4
  • 13
    • 14744293446 scopus 로고    scopus 로고
    • Heat induced gelling properties of soy protein isolates prepared from different defatted soybean flours
    • Hua, Y. F., S. W. Cui, Q. Wang, Y. Mine, and V. Poysa. 2005. Heat induced gelling properties of soy protein isolates prepared from different defatted soybean flours. Food Res. Int. 38:377-385.
    • (2005) Food Res. Int. , vol.38 , pp. 377-385
    • Hua, Y.F.1    Cui, S.W.2    Wang, Q.3    Mine, Y.4    Poysa, V.5
  • 14
    • 28444464486 scopus 로고    scopus 로고
    • Soybean protein aggregation induced by lipoxygenase catalyzed linoleic acid oxidation
    • Huang, Y. R., Y. F. Hua, and A. Y. Qiu. 2006. Soybean protein aggregation induced by lipoxygenase catalyzed linoleic acid oxidation. Food Res. Int. 39:240-249.
    • (2006) Food Res. Int. , vol.39 , pp. 240-249
    • Huang, Y.R.1    Hua, Y.F.2    Qiu, A.Y.3
  • 15
    • 0028500763 scopus 로고
    • The avian spleen: A neglected organ
    • John, J. L. 1994. The avian spleen: A neglected organ. Q. Rev. Biol. 69:327-351.
    • (1994) Q. Rev. Biol. , vol.69 , pp. 327-351
    • John, J.L.1
  • 17
    • 34548472673 scopus 로고    scopus 로고
    • Effect of lipoxygenase activity in defatted soybean flour on the gelling properties of soybean protein isolate
    • Kong, X. Z., X. H. Li, H. J. Wang, Y. F. Hua, and Y. R. Huang. 2008. Effect of lipoxygenase activity in defatted soybean flour on the gelling properties of soybean protein isolate. Food Chem. 106:1093-1099.
    • (2008) Food Chem. , vol.106 , pp. 1093-1099
    • Kong, X.Z.1    Li, X.H.2    Wang, H.J.3    Hua, Y.F.4    Huang, Y.R.5
  • 19
    • 0034891783 scopus 로고    scopus 로고
    • Oxidative modification of proteins during aging
    • Levine, R. L., and E. R. Stadtman. 2001. Oxidative modification of proteins during aging. Exp. Gerontol. 36:1495-1502.
    • (2001) Exp. Gerontol. , vol.36 , pp. 1495-1502
    • Levine, R.L.1    Stadtman, E.R.2
  • 20
    • 0034489803 scopus 로고    scopus 로고
    • Dietary oxidized oil influences the levels of type 2 T-helper cell-related antibody and inflammatory mediators in mice
    • Lin, B. F., C. C. Lai, K. W. Lin, and B. L. Chiang. 2000. Dietary oxidized oil influences the levels of type 2 T-helper cell-related antibody and inflammatory mediators in mice. Br. J. Nutr. 84:911-917.
    • (2000) Br. J. Nutr. , vol.84 , pp. 911-917
    • Lin, B.F.1    Lai, C.C.2    Lin, K.W.3    Chiang, B.L.4
  • 21
    • 0031041248 scopus 로고    scopus 로고
    • Effects of dietary oxidized frying oil on immune responses of spleen cells in rats
    • Lin, B. F., Y. J. Wu, B. L. Chiang, J. F. Liu, and C. J. Huang. 1997. Effects of dietary oxidized frying oil on immune responses of spleen cells in rats. Nutr. Res. 17:729-740.
    • (1997) Nutr. Res. , vol.17 , pp. 729-740
    • Lin, B.F.1    Wu, Y.J.2    Chiang, B.L.3    Liu, J.F.4    Huang, C.J.5
  • 22
    • 0033827809 scopus 로고    scopus 로고
    • Chemical, physical, and gel-forming properties of oxidized myofibrils and whey- and soy - Protein isolates
    • Liu, G., Y. L. Xiong, and D. A. Butterfield. 2000. Chemical, physical, and gel-forming properties of oxidized myofibrils and whey- and soy - protein isolates. J. Food Sci. 65:811-818.
    • (2000) J. Food Sci. , vol.65 , pp. 811-818
    • Liu, G.1    Xiong, Y.L.2    Butterfield, D.A.3
  • 24
    • 0037451636 scopus 로고    scopus 로고
    • Protection against oxidative protein damage induced by metal-catalyzed reaction or alkylperoxyl radicals: Comparative effects of melatonin and other antioxidants
    • Mayo, J. C., D. X. Tan, R. M. Sainz, M. Natarajan, S. Lopez-Burillo, and R. J. Reiter. 2003. Protection against oxidative protein damage induced by metal-catalyzed reaction or alkylperoxyl radicals: Comparative effects of melatonin and other antioxidants. Biochim. Biophys. Acta 1620:139-150.
    • (2003) Biochim. Biophys. Acta , vol.1620 , pp. 139-150
    • Mayo, J.C.1    Tan, D.X.2    Sainz, R.M.3    Natarajan, M.4    Lopez-Burillo, S.5    Reiter, R.J.6
  • 26
    • 84893780141 scopus 로고
    • NRC, 9th rev. ed. Natl. Acad. Press, Washington, DC
    • NRC. 1994. Nutrient Requirements of Poultry. 9th rev. ed. Natl. Acad. Press, Washington, DC.
    • (1994) Nutrient Requirements of Poultry
  • 27
    • 0041765653 scopus 로고    scopus 로고
    • How stress influences the immune response
    • Padgett, D. A., and R. Glaser. 2003. How stress influences the immune response. Trends Immunol. 24:444-448.
    • (2003) Trends Immunol. , vol.24 , pp. 444-448
    • Padgett, D.A.1    Glaser, R.2
  • 28
    • 0034659164 scopus 로고    scopus 로고
    • Myeloperoxidase-generated oxidants and atherosclerosis
    • Podrez, E. A., H. M. Abu-Soud, and S. L. Hazen. 2000. Myeloperoxidase-generated oxidants and atherosclerosis. Free Radic. Biol. Med. 28:1717-1725.
    • (2000) Free Radic. Biol. Med. , vol.28 , pp. 1717-1725
    • Podrez, E.A.1    Abu-Soud, H.M.2    Hazen, S.L.3
  • 29
    • 33745222784 scopus 로고    scopus 로고
    • ESR and NMR spectroscopy studies on protein oxidation and formation of dityrosine in emulsions containing oxidised methyl linoleate
    • Saeed, S., D. Gillies, G. Wagner, and N. K. Howell. 2006. ESR and NMR spectroscopy studies on protein oxidation and formation of dityrosine in emulsions containing oxidised methyl linoleate. Food Chem. Toxicol. 44:1385-1392.
    • (2006) Food Chem. Toxicol. , vol.44 , pp. 1385-1392
    • Saeed, S.1    Gillies, D.2    Wagner, G.3    Howell, N.K.4
  • 30
    • 34447301257 scopus 로고    scopus 로고
    • Effect of oxidation on in vitro digestibility of skeletal muscle myofibrillar proteins
    • 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.
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 5343-5348
    • Sante-Lhoutellier, V.1    Aubry, L.2    Gatellier, P.3
  • 31
    • 34249007019 scopus 로고
    • A syndrome produced by diverse nocuous agents
    • Selye, H. 1936a. A syndrome produced by diverse nocuous agents. Nature 138:32.
    • (1936) Nature , vol.138 , pp. 32
    • Selye, H.1
  • 32
    • 0000668139 scopus 로고
    • Thymus and adrenals in the response of the organism to injuries and intoxications
    • Selye, H. 1936b. Thymus and adrenals in the response of the organism to injuries and intoxications. Br. J. Exp. Pathol. 17:234-248.
    • (1936) Br. J. Exp. Pathol. , vol.17 , pp. 234-248
    • Selye, H.1
  • 33
    • 0034545719 scopus 로고    scopus 로고
    • Quantification and significance of protein oxidation in biological samples
    • Shacter, E. 2000. Quantification and significance of protein oxidation in biological samples. Drug Metab. Rev. 32:307-326.
    • (2000) Drug Metab. Rev. , vol.32 , pp. 307-326
    • Shacter, E.1
  • 34
    • 0032622470 scopus 로고    scopus 로고
    • Introduction to poultry vaccines and immunity
    • Sharma, J. M. 1999. Introduction to poultry vaccines and immunity. Adv. Vet. Med. 41:481-494.
    • (1999) Adv. Vet. Med. , vol.41 , pp. 481-494
    • Sharma, J.M.1
  • 35
    • 0025674536 scopus 로고
    • Metal ion-catalyzed oxidation of proteins: Biochemical mechanism and biological consequences
    • Stadtman, E. R. 1990. Metal ion-catalyzed oxidation of proteins: Biochemical mechanism and biological consequences. Free Radic. Biol. Med. 9:315-325.
    • (1990) Free Radic. Biol. Med. , vol.9 , pp. 315-325
    • Stadtman, E.R.1
  • 36
    • 33750710080 scopus 로고    scopus 로고
    • Protein oxidation and aging
    • Stadtman, E. R. 2006. Protein oxidation and aging. Free Radic. Res. 40:1250-1258.
    • (2006) Free Radic. Res. , vol.40 , pp. 1250-1258
    • Stadtman, E.R.1
  • 38
    • 55549102634 scopus 로고    scopus 로고
    • Effect of high pressure treatment on aggregation and structural properties of soy protein isolate
    • Tang, C. H., and C. Y. Ma. 2009. Effect of high pressure treatment on aggregation and structural properties of soy protein isolate. Lebenson. Wiss. Technol. 42:606-611.
    • (2009) Lebenson. Wiss. Technol. , vol.42 , pp. 606-611
    • Tang, C.H.1    Ma, C.Y.2
  • 39
    • 84867218581 scopus 로고    scopus 로고
    • Effects of heat treatment on structural modification and in vivo antioxidant capacity of soy protein
    • Tang, X., Q. P. Wu, G. W. Le, and Y. H. Shi. 2012a. Effects of heat treatment on structural modification and in vivo antioxidant capacity of soy protein. Nutrition 28:1180-1185.
    • (2012) Nutrition , vol.28 , pp. 1180-1185
    • Tang, X.1    Wu, Q.P.2    Le, G.W.3    Shi, Y.H.4
  • 40
    • 84856032175 scopus 로고    scopus 로고
    • Structural and antioxidant modification of wheat peptides modified by the heat and lipid peroxidation product malondialdehyde
    • Tang, X., Q. P. Wu, G. W. Le, J. Wang, K. J. Yin, and Y. H. Shi. 2012b. Structural and antioxidant modification of wheat peptides modified by the heat and lipid peroxidation product malondialdehyde. J. Food Sci. 77:H16-H22.
    • (2012) J. Food Sci. , vol.77
    • Tang, X.1    Wu, Q.P.2    Le, G.W.3    Wang, J.4    Yin, K.J.5    Shi, Y.H.6
  • 41
    • 0034890121 scopus 로고    scopus 로고
    • Aging and oxidation of reactive protein sulfhydryls
    • Thomas, J. A., and R. J. Mallis. 2001. Aging and oxidation of reactive protein sulfhydryls. Exp. Gerontol. 36:1519-1526.
    • (2001) Exp. Gerontol. , vol.36 , pp. 1519-1526
    • Thomas, J.A.1    Mallis, R.J.2
  • 42
    • 34548313953 scopus 로고    scopus 로고
    • Lipid and protein deterioration during the chilled storage of minced sea salmon (Pseudopercis semifasciata)
    • Tironi, V. A., M. C. Tomas, and M. C. Anon. 2007. Lipid and protein deterioration during the chilled storage of minced sea salmon (Pseudopercis semifasciata). J. Sci. Food Agric. 87:2239-2246.
    • (2007) J. Sci. Food Agric. , vol.87 , pp. 2239-2246
    • Tironi, V.A.1    Tomas, M.C.2    Anon, M.C.3
  • 44
    • 0031925483 scopus 로고    scopus 로고
    • Functional stability of antioxidantwashed, cryoprotectant-treated beef heart surimi during frozen storage
    • Wang, B., and Y. L. Xiong. 1998. Functional stability of antioxidantwashed, cryoprotectant-treated beef heart surimi during frozen storage. J. Food Sci. 63:293-298.
    • (1998) J. Food Sci. , vol.63 , pp. 293-298
    • Wang, B.1    Xiong, Y.L.2
  • 45
    • 84893754913 scopus 로고    scopus 로고
    • Effects of soybean protein modified by heat or malondialdehyde on the level of free radicals and antioxidant capability in mice
    • Wu, Q. P., J. Wang, G. W. Le, Y. J. Shui, and Y. H. Shi. 2011. Effects of soybean protein modified by heat or malondialdehyde on the level of free radicals and antioxidant capability in mice. Ying Yang Xue Bao 33:14-18.
    • (2011) Ying Yang Xue Bao , vol.33 , pp. 14-18
    • Wu, Q.P.1    Wang, J.2    Le, G.W.3    Shui, Y.J.4    Shi, Y.H.5
  • 46
    • 70349096756 scopus 로고    scopus 로고
    • Structural modification of soy protein by the lipid peroxidation product acrolein
    • Wu, W., X. J. Wu, and Y. F. Hua. 2010. Structural modification of soy protein by the lipid peroxidation product acrolein. Lebenson. Wiss. Technol. 43:133-140.
    • (2010) Lebenson. Wiss. Technol. , vol.43 , pp. 133-140
    • Wu, W.1    Wu, X.J.2    Hua, Y.F.3
  • 47
    • 67249118991 scopus 로고    scopus 로고
    • Structural modification of soy protein by the lipid peroxidation product malondialdehyde
    • Wu, W., C. M. Zhang, and Y. F. Hua. 2009a. Structural modification of soy protein by the lipid peroxidation product malondialdehyde. J. Sci. Food Agric. 89:1416-1423.
    • (2009) J. Sci. Food Agric. , vol.89 , pp. 1416-1423
    • Wu, W.1    Zhang, C.M.2    Hua, Y.F.3
  • 48
    • 64449084784 scopus 로고    scopus 로고
    • Oxidative modification of soy protein by peroxyl radicals
    • Wu, W., C. M. Zhang, X. Z. Kong, and Y. F. Hua. 2009b. Oxidative modification of soy protein by peroxyl radicals. Food Chem. 116:295-301.
    • (2009) Food Chem. , vol.116 , pp. 295-301
    • Wu, W.1    Zhang, C.M.2    Kong, X.Z.3    Hua, Y.F.4
  • 49
    • 0036493406 scopus 로고    scopus 로고
    • Defects in leukocyte-mediated initiation of lipid peroxidation in plasma as studied in myeloperoxidase-deficient subjects: Systematic identification of multiple endogenous diffusible substrates for myeloperoxidase in plasma
    • Zhang, R., Z. Shen, W. M. Nauseef, and S. L. Hazen. 2002. Defects in leukocyte-mediated initiation of lipid peroxidation in plasma as studied in myeloperoxidase-deficient subjects: Systematic identification of multiple endogenous diffusible substrates for myeloperoxidase in plasma. Blood 99:1802-1810.
    • (2002) Blood , vol.99 , pp. 1802-1810
    • Zhang, R.1    Shen, Z.2    Nauseef, W.M.3    Hazen, S.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.