Acknowledgement
The authors would like to thank the staff of the Baima Experimental Base of Nanjing Agricultural University for their help with the experimental site.
References
- Selle PH, Dorigam JCD, Lemme A, Chrystal PV, Liu SY. Synthetic and crystalline amino acids: alternatives to soybean meal in chicken-meat production. Animals (Basel) 2020;10:729. https://doi.org/10.3390/ani10040729
- Noblet J, Wu SB, Choct M. Methodologies for energy evaluation of pig and poultry feeds: a review. Anim Nutr 2022;9:378. https://doi.org/10.1016/j.aninu.2022.05.002
- Duque-Estrada PK, Kyriakopoulou W, de Groot AJ, van der Goot AJ, Berton-Carabin CC. Oxidative stability of soy proteins: from ground soybeans to structured products. Food Chem 2020;318:126499. https://doi.org/10.1016/j.foodchem.2020.126499
- Shacter E. Quantification and significance of protein oxidation in biological samples. Drug Metab Rev 2000;32:307-26. https://doi.org/10.1081/DMR-100102336
- Estevez MS, Diaz-Velasco, Martinez R. Protein carbonylation in food and nutrition: a concise update. Amino Acids 2022;54:559-73. https://doi.org/10.1007/s00726-021-03085-6
- Lu P, Xue WY, Zhang XL, et al. Heat-induced protein oxidation of soybean meal impairs growth performance and antioxidant status of broilers. Poult Sci 2019;98:276-86. https://doi.org/10.3382/ps/pey344
- Chen ZQ, Wang C, Gao XD, et al. Interaction characterization of preheated soy protein isolate with cyanidin-3-O-glucoside and their effects on the stability of black soybean seed coat anthocyanins extracts. Food Chem 2019;271:266-73. https://doi.org/10.1016/j.foodchem.2018.07.170
- Carbonaro MP, Maselli P, Nucara A. Relationship between digestibility and secondary structure of raw and thermally treated legume proteins: a Fourier transform infrared (FT-IR) spectroscopic study. Amino Acids 2012;43:911-21. https://doi.org/10.1007/s00726-011-1151-4
- Dzurec DJ, Zall RR. Effect of heating, cooling, and storing milk on casein and whey proteins. J Dairy Sci 1985;68:273-80. https://doi.org/10.3168/jds.S0022-0302(85)80822-5
- Zhang XL, Lu P, Xue WY, Wu D, Wen C, Zhou Y. Digestive evaluation of soy isolate protein as affected by heat treatment and soy oil inclusion in broilers at an early age. Anim Sci J 2016;87:1291-7. https://doi.org/10.1111/asj.12575
- Tang X, Wu Q, Le G, Shi Y. Effects of heat treatment on structural modification and in vivo antioxidant capacity of soy protein. Nutrition 2012;28:1180-5. https://doi.org/10.1016/j.nut.2012.03.011
- Gu Y, Chen Y, Jin R, Wang C, Wen C, Zhou Y. Protective effects of curcumin on laying hens fed soybean meal with heat-induced protein oxidation. Ital J Anim Sci 2021;20:1069-78. https://doi.org/10.1080/1828051X.2021.1913653
- Levine RL, Garland D, Oliver CN, et al. Determination of carbonyl content in oxidatively modified proteins. Method Enzymol 1990;186:464-78. https://doi.org/10.1016/0076-6879(90)86141-h
- Smith PK, Krohn RI, Hermanson GT, et al. Measurement of protein using bicinchoninic acid. Anal Biochem 1985;150:76-85. https://doi.org/10.1016/0003-2697(85)90442-7
- Hoshi Y, Yamauchi F. Determination of sulfhydryl and disulfide contents of soybean 11S globulin and their change by lyophilization. Agric Biol Chem 1983;47:2435-40. https://doi.org/10.1080/00021369.1983.10865976
- Lo WMY and Li-Chan ECY. Angiotensin I converting enzyme inhibitory peptides from in vitro pepsin-pancreatin digestion of soy protein. J Agric Food Chem 2005;53:3369-76. https://doi.org/10.1021/jf048174d
- Anderson ME. Determination of glutathione and glutathione disulfide in biological samples. Method Enzymol 1985;113:548-55. https://doi.org/10.1016/s0076-6879(85)13073-9
- Benzie IFF, Strain JJ. The ferric reducing ability of plasma (FRAP) as a measure of "antioxidant power": the FRAP assay. Anal Biochem 1996;239:70-6. https://doi.org/10.1006/abio.1996.0292
- Goth LA. simple method for determination of serum catalase activity and revision of reference range. Clin Chim Acta 1991;196:143-51. https://doi.org/10.1016/0009-8981(91)90067-M
- Hafeman DG, Sunde RA, Hoekstra WG. Effect of dietary selenium on erythrocyte and liver glutathione peroxidase in the rat. J Nutr 1974;104:580-7. https://doi.org/10.1093/jn/104.5.580
- Huang Y, Haley CS, Wu F, et al. Genetic mapping of quantitative trait loci affecting carcass and meat quality traits in Beijing ducks (Anas platyrhynchos). Anim Genet 2007;38:114-9. https://doi.org/10.1111/j.1365-2052.2007.01571.x
- Kim JR, Yoon HW, Kwo KS, Lee SR, Rhee SG. Identification of proteins containing cysteine residues that are sensitive to oxidation by hydrogen peroxide at neutral pH. Anal Biochem 2000;283:214-21. https://doi.org/10.1006/abio.2000.4623
- Wu W, Hua Y, Lin Q, Xiao H. Effects of oxidative modification on thermal aggregation and gel properties of soy protein by peroxyl radicals. Int J Food Sci Technol 2011;46:1891-7. https://doi.org/10.1111/j.1365-2621.2011.02698.x
- Narayan M. The formation of native disulfide bonds: treading a fine line in protein folding. Protein J 2021;40:134-9. https://doi.org/10.1007/s10930-021-09976-7
- Swaisgood HE, Catignani GL. Protein digestibility: in vitro methods of assessment. Adv Food Nutr Res 1991;35:185-236. https://doi.org/10.1016/S1043-4526(08)60065-0
- Long GH, Ji Y, Pan HB, Sun Z, Li Y, Qin G. Characterization of thermal denaturation structure and morphology of soy glycinin by FTIR and SEM. Int J Food Prop 2015;18:763-74. https://doi.org/10.1080/10942912.2014.908206
- Zhao X, Zhao Q, Chen H, Xiong H. Distribution and effects of natural selenium in soybean proteins and its protective role in soybean β-conglycinin (7S globulins) under AAPH-induced oxidative stress. Food Chem 2019;272:201-9. https://doi.org/10.1016/j.foodchem.2018.08.039
- Li Z, Mo L, Le G, Shi Y. Oxidized casein impairs antioxidant defense system and induces hepatic and renal injury in mice. Food Chem Toxicol 2014;64:86-93. https://doi.org/10.1016/j.fct.2013.10.039
- Yuksel M, Ates I, Kaplan M, et al. Is oxidative stress associated with activation and pathogenesis of inflammatory bowel disease? J Med Biochem 2017;36:341-8. https://doi.org/10.1515/jomb-2017-0013
- Alqhtani AH, Qaid MM, Al-Mufarrej SI, Al-Garadi MA, Ali ABA. Serum biochemistry indices, leukogram, carcass variables and intestinal measurements of Eimeria tenellainfected or non-infected broilers treated with dietary Cinnamomum verum bark. J Appl Anim Res 2023;51:40-51. https://doi.org/10.1080/09712119.2022.2150630
- Malila Y. In vivo oxidative stress associated with growth-related myopathies in chicken and potential health impact: an opinion paper. Front Physiol 2023;14:1291323. https://doi.org/10.3389/fphys.2023.1291323
- Zhang X, Lu P, Xue W, Wu D, Wen C, Zhou Y. An evaluation of heat on protein oxidation of soy protein isolate or soy protein isolate mixed with soybean oil in vitro and its consequences on redox status of broilers at early age. Asian-Australas J Anim Sci 2017;30:1135-42. https://doi.org/10.5713/ajas.16.0683
- Frame CA, Johnson EL, Kilburn E, Huff-Lonergan E, Kerr BJ, Serao MR. Impact of dietary oxidized protein on oxidative status and performance in growing pigs. J Anim Sci 2020;98:skaa097. https://doi.org/10.1093/jas/skaa097
- Offer G. Modeling of the formation of pale, soft and exudative meat-effects of chilling regime and rate and extent of glycolysis. Meat Sci 1991;30:157-84. https://doi.org/10.1016/0309-1740(91)90005-B
- Thanatsang KV, Malila Y, Arayamethakorn S, et al. Nutritional properties and oxidative indices of broiler breast meat affected by wooden breast abnormality. Animals (Basel) 2020;10:2272. https://doi.org/10.3390/ani10122272
- E-Senousey HK, Fouad AM, Yao JH, Zhang ZG, Shen QW. Dietary alpha lipoic acid improves body composition, meat quality and decreases collagen content in muscle of broiler chickens. Asian-Australas J Anim Sci 2013;26:394-400. https://doi.org/10.5713/ajas.2012.12430
- Savell JW, Cross HR, Francis JJ, et al. National consumer retail beef study - Interaction of trim level, price and grade on consumer acceptance of beef steaks and roasts. J Food Qual 1989;12:251-74. https://doi.org/10.1111/j.1745-4557.1989.tb00328.x