Peptídeos bioativos da cartilagem e da mucosa intestinal de bovinos como substitutos do plasma bovino desidratado em dietas para leitões em fase de creche
DOI:
https://doi.org/10.5433/1679-0359.2026v47n1p145Palavras-chave:
Desempenho pós-desmame, Eficiência alimentar, Leitões desmamados, Perfil de peptídeos funcionais, Substituição do plasma bovino.Resumo
Peptídeos solúveis da mucosa intestinal e da cartilagem de bovinos (Peptipro®) são obtidos por hidrólise enzimática, sendo coprodutos da extração de heparina e condroitina. Esta hidrólise libera componentes bioativos e resulta em um produto de alta digestibilidade. O objetivo deste estudo foi identificar os peptídeos bioativos contidos no Peptipro®, e avaliar o efeito da sua inclusão na dieta sobre o desempenho e a saúde intestinal de leitões desmamados, comparado com dietas contendo plasma bovino desidratado fornecidas na creche. Uma amostra de Peptipro® foi submetida a sequenciamento de peptídeos por espectrometria de massa. O experimento de desempenho foi realizado em delineamento de blocos ao acaso em arranjo fatorial 3 x 2 com dez repetições. Os fatores foram a dieta e o sexo dos leitões, e os blocos foram definidos com base no peso corporal (PC) inicial. As dietas experimentais foram Plasma bovino (PBov): 6% e 3% de plasma bovino desidratado nas fases Pré-inicial I (primeira semana) e II (segunda semana); Substituição parcial do PBov por Peptipro® (PBov-Pep): 3% de PBov desidratado e 3% de Peptipro® na fase Pré-inicial I, e 1,5% de cada ingrediente na fase Pré-inicial II; e Peptipro®: 3% e 1.5% de Peptipro® nas fases Pré-inicial I e II, respectivamente. Nas fases Inicial I (terceira semana) e Inicial II (últimos 18 dias), a mesma dieta foi fornecida para todos os grupos experimentais. O total de 120 leitões (6,92 ± 0,77 kg PC), sendo 60 machos imunocastrados e 60 fêmeas, foram distribuídos em 30 baias com quatro animais por baia e alimentados à vontade por 39 dias. Um total de 176 peptídeos foram identificados no Peptipro®, dos quais 71 possuem funções bioativas relacionadas à regulação do metabolismo energético (74,6%), regulação da pressão arterial (63,4%), ação antioxidante (8,4%), imunomoduladora (2,8%) e outros processos metabólicos (4,2%). A permeabilidade intestinal, avaliada com o marcador isotiocianato de fluoresceína-dextran (FITC-dextran), não foi influencia pela dieta (P = 0,308). Na fase Pré-inicial II, a dieta Peptipro® aumentou o ganho médio diário em 12,8% em relação a dieta PBov-Pep (0,397 vs. 0,352 kg animal-1 dia-1; P = 0,044) sem afetar o consumo de ração (média de 0,444 kg animal-1 dia-1; P = 0,198), resultando em melhor conversão alimentar (1,08 vs. 1,25 kg de ração kg-1 ganho de peso; P = 0,001). O escore de fezes não foi influenciado pela dieta, pelo sexo ou pela interação entre ambos (P>0,05), apresentando valores médios de 51,5; 35,5 e 13,0% para frequência relativa de fezes normais, pastosas e aquosas. Devido ao bom perfil de aminoácidos, ao amplo espectro de peptídeos bioativos e seu efeito positivo no desempenho animal, o Peptipro® pode substituir o Pbov desidratado em dietas pré-iniciais de leitões na creche.
Downloads
Referências
Arihara, K., Nakashima, Y., Mukai, T., Ishikawa, S., & Itoh, M. (2001). Peptide inhibitors for angiotensin I-converting enzyme from enzymatic hydrolysates of porcine skeletal muscle. Meat Science, 57(3), 319-324. doi: 10.1016/S0309-1740(00)00108-X
Ashmarin, I. P., Karazeeva, E. P., Lyapina, L. A., & Samonina, G. E. (1998). The simplest proline-containing peptides PG, GP, PGP and GPGG: regulatory activity and possible source of biosynthesis. Biochemistry. Bikhimiia, 63(2), 119-124.
Bah, C. S. F., Bekhit, A. El-D. A., McConnell, M. A., & Carne, A. (2016). Generation of bioactive peptide hydrolysates from cattle plasma using plant and fungal proteases. Food Chemistry, 213, 98-107. doi: 10.1016/j.foodchem.2016.06.065
Balan, P., Staincliffe, M., & Moughan, P. J. (2021). Effects of spray-dried animal plasma on the growth performance of weaned piglets-A review. Journal of Animal Physiology and Animal Nutrition, 105(4), 699-714. doi: 10.1111/jpn.13435
Balti, R., Nedjar-Arroume, N., Adjé, E. Y., Guillochon, D., & Nasri, M. (2010). Analysis of novel angiotensin I-converting enzyme inhibitory peptides from enzymatic hydrolysates of cuttlefish (Sepia officinalis) muscle proteins. Journal of Agricultural and Food Chemistry, 58(6), 3840-3846. doi: 10.1021/jf904300q
Bella, A. M., Jr., Erickson, R. H., & Kim, Y. S. (1982). Rat intestinal brush border membrane dipeptidyl-aminopeptidase IV: Kinetic properties and substrate specificities of the purified enzyme. Archives of Biochemistry and Biophysics, 218(1), 156-162. doi: 10.1016/0003-9861(82)90330-7
Boonkong, S., Luasiri, P., Pongsetkul, J., Suwanandgul, S., Chaipayang, S., Molee, W., & Sangsawad, P. (2024). Exploring the utilization of bovine blood as a source of antioxidant peptide: production, concentration, identification, and in silico gastrointestinal digestion. Food Science of Animal Resources, 44(6), 1283-1304. doi: 10.5851/kosfa.2024.e45
Brownlee, I. A. (2011). The physiological roles of dietary fibre. Food Hydrocolloids, 25(2), 238-250. doi: 10.1016/j.foodhyd.2009.11.013
Caliendo, G., Greco, G., Grieco, P., Perissutti, E., Santagada, V., Ialenti, A., Maffia, P., Albrizio, S., & Santini, A. (1996). Synthesis and antinociceptive activity of peptides related to interleukin-1b193-195 Lys-Pro-Thr. Peptide Science, 40(5), 479-483. doi: 10.1002/(SICI)1097-0282(1996)40:5<479::AID-BIP5>3.0.CO;2-T
Canibe, N., Hojberg, O., Kongsted, H., Vodolazska, D., Lauridsen, C., Nielsen, T. S., & Schönherz, A. A. (2022). Review on preventive measures to reduce post-weaning diarrhoea in piglets. Animals, 12(19), 2585. doi: 10.3390/ani12192585
Cantú, M. D., Carrilho, E., Wulff, N. A., & Palma, M. S. (2008). Sequenciamento de peptídeos usando espectrometria de massas: um guia prático. Química Nova, 31(3), 669-675. doi: 10.1590/S0100-40422008000300034
Chen, H.-M., Muramoto, K., & Yamauchi, F. (1995). Structural analysis of antioxidative peptides from Soybean beta-conglycinin. Journal of Agricultural and Food Chemistry, 43(3), 574-578. doi: 10.1021/jf00051a004
Cheung, H. S., Wang, F. L., Ondetti, M. A., Sabo, E. F., & Cushman, D. W. (1980). Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence. Journal of Biological Chemistry, 255(2), 401-407. PMID: 6243277
Chi, C. F., Wang, B., Wang, Y. M., Zhang, B., & Deng, S. J. (2015). Isolation and characterization of three antioxidant peptides from protein hydrolysate of bluefin leatherjacket (Navodon septentrionalis) heads. Journal of Functional Foods, 12, 1-10. doi: 10.1016/j.jff.2014.10.027
Crozatti, T. T. S., Miyoshi, J. H., Tonin, A. P. P., Tomazini, L. F., Oliveira, M. A. S., Maluf, J. U., Meurer, E. C., & Matioli, G. (2023). Obtaining of bioactive di- and tripeptides from enzymatic hydrolysis of soybean meal and its protein isolate using Alcalase® and Neutrase®. International Journal of Food Science and Technology, 58(3), 1586-1596. doi: 10.1111/ijfs.15886
Cushman, D. W., Cheung, H. S., Sabo, E. F., & Ondetti, M. A. (1981). Angiotensin converting enzyme inhibitors: evolution of a new class of antihypertensive drugs. In Z. P. Horovitz (Ed.), Angiotensin converting enzyme inhibitors: mechanisms of action and clinical implications (pp. 3-25). Baltimore, Md: Urban & Schwarzenberg.
Dhanda, S., Singh, J., & Singh, H. (2008). Hydrolysis of various bioactive peptides by goat brain dipeptidylpeptidase-III homologue. Cell Biochemistry & Function, 26(3), 339-345. doi: 10.1002/cbf.1448
Dias, C. P., Silva, C. A., & Manteca, X. (2014). Bem-estar dos suínos. Midiograf.
Duarte, M. E., & Kim, S. W. (2024). Efficacy of Saccharomyces yeast postbiotics on cell turnover, immune responses, and oxidative stress in the jejunal mucosa of young pigs. Scientific Reports, 14(1), 1-10. doi: 10.1038/s41598-024-70399-2
Everaert, N., Van Cruchten, S., Weström, B., Bailey, M., Van Ginneken, C., Thymann, T., & Pieper, R. (2017). A review on early gut maturation and colonization in pigs, including biological and dietary factors affecting gut homeostasis. Animal Feed Science and Technology, 233, 89-103. doi: 10.1016/j.anifeedsci.2017.06.011
Figueroa, J., Solà-Oriol, D., Guzmán-Pino, S. A., Chetrit, C., Borda, E., & Pérez, J. F. (2016). The use of porcine digestible peptides and their continuity effect in nursery pigs. Journal of Animal Science, 94(4), 1531-1540. doi: 10.2527/jas.2015-0019
Gómez-Ruiz, J. A., Ramos, M., & Recio, I. (2007). Identification of novel angiotensin-converting enzyme-inhibitory peptides from ovine milk proteins by CE-MS and chromatographic techniques. Electrophoresis, 28(22), 4202-4211. doi: 10.1002/elps.200700324
González-Solé, F., Criado-Mesas, L., Villodre, C., García, W. C., Farré, M., Borda, E., Pérez-Cano, F. J., Folch, J. M., Solà-Oriol, D., & Pérez, J. F. (2020). Porcine digestible peptides (Pdp) in weanling diets regulates the expression of genes involved in gut barrier function, immune response and nutrient transport in nursery pigs. Animals, 10(12), 1-21. doi: 10.3390/ani10122368
Hatanaka, T., Inoue, Y., Arima, J., Kumagai, Y., Usuki, H., Kawakami, K., Kimura, M., & Mukaihara, T. (2012). Production of dipeptidyl peptidase IV inhibitory peptides from defatted rice bran. Food Chemistry, 134(2), 797-802. doi: 10.1016/j.foodchem.2012.02.183
He, R., Malomo, S. A., Alashi, A., Girgih, A. T., Ju, X., & Aluko, R. E. (2013). Purification and hypotensive activity of rapeseed protein derived renin and angiotensin converting enzyme inhibitory peptides. Journal of Functional Foods, 5(2), 781-789. doi: 10.1016/j.jff.2013.01.024
Hikida, A., Keisuke, I., Motoyama, T., Kato, R., & Kawarasaki, Y. (2013). Systematic analysis of a dipeptide library for inhibitor development using human dipeptidyl peptidase IV produced by a Saccharomyces cerevisiae expression system. Biochemical and Biophysical Research Communications, 430(4), 1217-1222. doi: 10.1016/j.bbrc.2012.12.073
Huting, A. M. S., Middelkoop, A., Guan, X., & Molist, F. (2021). Using nutritional strategies to shape the gastro-intestinal tracts of suckling and weaned piglets. Animals, 11(2), 1-37. doi: 10.3390/ani11020402
Jayaraman, B., & Nyachoti, C. M. (2017). Husbandry practices and gut health outcomes in weaned piglets: a review. Animal Nutrition, 3(3), 205-211. doi: 10.1016/j.aninu.2017.06.002
Kazimierska, K., & Biel, W. (2023). Chemical composition and functional properties of spray-dried animal plasma and its contributions to livestock and pet health: a review. Animals, 13(15), 2484. doi: 10.3390/ani13152484
Kohmura, M., Nio, N., & Ariyoshi, Y. (1990). Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins. Agriculture and Biological Chemistry, 54(4), 1101-1102. doi: 10.1080/00021369.1990.10870065
Lafarga, T., O’Connor, P., & Hayes, M. (2014). Identification of novel dipeptidyl peptidase-IV and angiotensin-I-converting enzyme inhibitory peptides from meat proteins using in silico analysis. Peptides, 59, 53-62. doi: 10.1016/j.peptides.2014.07.005
Lan, V. T. T., Ito, K., Ohno, M., Motoyama, T., Ito, S., & Kawarasaki, Y. (2015). Analyzing a dipeptide library to identify human dipeptidyl peptidase IV inhibitor. Food Chemistry, 175, 66-73. doi: 10.1016/j.foodchem.2014.11.131
Lange, C. F. M., Pluske, J., Gong, J., & Nyachoti, C. M. (2010). Strategic use of feed ingredients and feed additives to stimulate gut health and development in young pigs. Livestock Science, 134(1-3), 124-134. doi: 10.1016/j.livsci.2010.06.117
Lee, C. M., & Snyder, S. H. (1982). Dipeptidyl-aminopeptidase III of rat brain selective affinity for enkephalin and angiotensin. Journal of Biological Chemistry, 257(20), 12043-12050. PMID: 6749851
Li, C.-H., Matsui, T., Matsumoto, K., Yamasaki, R., & Kawasaki, T. (2002). Latent production of angiotensin I-converting enzyme inhibitors from buckwheat protein. Journal of Peptide Science, 8(6), 267-274. doi: 10.1002/psc.387
Li, J., Li, Q., Li, J., & Zhou, B. (2014). Peptides derived from Rhopilema esculentum hydrolysate exhibit angiotensin converting enzyme (ACE) inhibitory and antioxidant abilities. Molecules, 19(9), 13587-13602. doi: 10.3390/molecules190913587
Luzarowski, M., Vicente, R., Kiselev, A., Wagner, M., Schlossarek, D., Erban, A., Souza, L. P., Childs, D., Wojciechowska, I., Luzarowska, U., Górka, M., Sokolowska, E. M., Kosmacz, M., Moreno, J. C., Brzezinska, A., Vegesna, B., Kopka, J., Fernie, A. R., Willmitzer, L., … Skirycz, A. (2021). Global mapping of protein-metabolite interactions in Saccharomyces cerevisiae reveals that Ser-Leu dipeptide regulates phosphoglycerate kinase activity. Communications Biology, 10(4), 181. doi: 10.1038/s42003-021-01684-3
Manoharan, S., Shuib, A. S., Abdullah, N., Bin Mohamad, S., & Aminudin, N. (2017). Characterisation of novel angiotensin-I-converting enzyme inhibitory tripeptide, Gly-Val-Arg derived from mycelium of Pleurotus pulmonarius. Process Biochemistry, 62, 215-222. doi: 10.1016/j.procbio.2017.07.020
Maruyama, S., Miyoshi, S., & Tanaka, H. (1989). Angiotensin I-converting enzyme inhibitors derived from Ficus carica. Agricultural and Biological Chemistry, 53(10), 2763-2767. doi: 10.1080/00021369.1989.10869725
Meisel, H., Walsh, D. J., Murray, B., & FitzGerald, R. J. (2016). ACE inhibitory peptides. In Y. Mine, & F. Shahidi F. (Eds.), Nutraceutical proteins and peptides in health and disease (pp. 269-315). Boca Raton, London, New York: CRC Taylor & Francis Group.
Miguel, M., Gómez-Ruiz, J. A., Recio, I., & Aleixandre, A. (2010). Changes in arterial blood pressure after single oral administration of milk-casein-derived peptides in spontaneously hypertensive rats. Molecular Nutrition & Food Research, 54(10), 1422-1427. doi: 10.1002/mnfr.200900448
Minkiewicz, P., Iwaniak, A., & Darewicz, M. (2019). BIOPEP-UWM database of bioactive peptides: current opportunities. International Journal of Molecular Sciences, 20(23), 5978. doi: 10.3390/ijms20235978
Miyoshi, S., Ishikawa, H., Kaneko, T., Fukui, F., Tanaka, H., & Maruyama, S. (1991). Structure and activity of angiotensin-converting enzyme inhibitors in an alpha-zein hydrolysate. Agricultural and Biological Chemistry, 55(5), 1313-1318. doi: 10.1080/00021369.1991.10870760
Mora, L., González-Rogel, D., Heres, A., & Toldrá, F. (2020). Iberian dry-cured ham as a potential source of α-glucosidase-inhibitory peptides. Journal of Functional Foods, 67, 103840. doi: 10.1016/j.jff.2020.103840
Morifuji, M., Koga, J., Kawanaka, K., & Higuchi, M. (2009). Branched-chain amino acid-containing dipeptides, identified from whey protein hydrolysates, stimulate glucose uptake in L6 myotubes and isolated skeletal muscles. Journal of Nutritional Science and Vitaminology, 55(1), 81-86. doi: 10.1016/10.3177/jnsv.55.81
Murray, B. A., & FitzGerald, R. J. (2007). Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production. Current Pharmaceutical Design, 13(8), 773-791. doi: 10.2174/138161207780363068
Nogata, Y., Nagamine, T., Yanaka, M., & Ohta, H. (2009). Angiotensin I converting enzyme inhibitory peptides produced by autolysis reactions from wheat bran. Journal of Agricultural and Food Chemistry, 57(15), 6618-6622. doi: 10.1021/jf900857w
Nongonierma, A. B., Mooney, C., Shields, D. C., & FitzGerald, R. J. (2013). Inhibition of dipeptidyl peptidase IV and xanthine oxidase by amino acids and dipeptides. Food Chemistry, 141(1), 644-653. doi: 10.1016/j.foodchem.2013.02.115
O'Reilly, P. J., Hardison, M. T., Jackson, P. L., Xu, X., Snelgrove, R. J., Gaggar, A., Galin, F. S., & Blalock, J. E. (2009). Neutrophils contain prolyl endopeptidase and generate the chemotactic peptide, PGP, from collagen. Journal of Neuroimmunology, 217(1), 51-54. doi: 10.1016/j.jneuroim.2009.09.020
Pihlanto-Leppälä, A., Koskinen, P., Piilola, K., Tupasela, T., & Korhonen, H. (2000). Angiotensin I-converting enzyme inhibitory properties of whey protein digests: concentration and characterization of active peptides. Journal of Dairy Research, 67(1), 53-64. doi: 10.1017/s0022029999003982
Poliseli, C. B., Meurer, E. C., Ribeiro, M. A. S., Tonin, A. P. P., Sartori, F. F., Poliseli, C. L., & Ribeiro, V. M. S. (2020). Identification of bioactive peptides in protein hydrolysates by liquid chromatography-tandem mass spectrometry. Journal of Mass Spectrometry, 55(12), e4701. doi: 10.1002/jms.4701
Pujols, J., Blázquez, E., Segalés, J., Rodríguez, F., Chang, C. Y., Argilaguet, J., Bosch-Camós, L., Rosell, R., Pailler-García, L., Gavrilov, B., Campbell, J., & Polo, J. (2023). Feeding spray-dried porcine plasma to pigs improves the protection afforded by the African Swine Fever Virus (ASFV) BA71∆CD2 vaccine prototype against experimental challenge with the pandemic ASFV—Study 2. Vaccines, 11(4), 1-13. doi: 10.3390/vaccines11040825
Rawendra, R. D. S., Aisha, Chen, S.-H., Chang, C.-I., Shih, W.-L., Huang, T.-C., Liao, M.-H., & Hsu, J.-L. (2014). Isolation and characterization of a novel angiotensin-converting enzyme-inhibitory tripeptide from enzymatic hydrolysis of soft-shelled turtle (Pelodiscus sinensis) egg white: in vitro, in vivo, and in silico study. Journal of Agricultural and Food Chemistry, 62(5), 12178-12185. doi: 10.1021/jf504734g
Ringseis, R., Matthes, B., Lehmann, V., Becker, K., Schöps, R., Ulbrich-Hofmann, R., & Eder, K. (2005). Peptides and hydrolysates from casein and soy protein modulate the release of vasoactive substances from human aortic endothelial cells. Biochimica et Biophysica Acta - General Subjects, 1721(1-3), 89-97. doi: 10.1016/j.bbagen.2004.10.005
Rostagno, H. S., Albino, L. F. T., Hannas, M. I., Donzele, J. L., Sakomura, N. S., Perazzo, F. G., Saraiva, A., Teixeira, M. L., Rodrigues, P. B., Oliveira, R. F., Barreto, S. L. T., & Brito, C. O. (2017). Tabelas brasileiras para aves e suínos (4a ed.). Universidade Federal de Viçosa.
Ruckman, L. A., Petry, A. L., Gould, S. A., & Patience, J. F. (2020). The impact of porcine spray-dried plasma protein and dried egg protein harvested from hyper-immunized hens, provided in the presence or absence of subtherapeutic levels of antibiotics in the feed, on growth and indicators of intestinal function and physio. Translational Animal Science, 4(3), 1-16. doi: 10.1093/tas/txaa095
Sedaghati, M., Ezzatpanah, H., Boojar, M. M., Ebrahimi, M. T., & Aminafshar, M. (2014). Plasmin digest of kappa-casein as a source of antibacterial peptides. Journal of Dairy Research, 81(2), 245-251. 10.1017/S0022029914000120
Sentandreu, M. A., & Toldrá, F. (2007). Evaluation of ACE inhibitory activity of dipeptides generated by the action of porcine muscle dipeptidyl peptidases. Food Chemistry, 101(2), 511-515. doi: 10.1016/j.foodchem.2006.04.018
Sharma, S., Singh, R., & Rana, S. (2011). Bioactive peptides: a review. International Journal Bioautomation, 15(4), 223-250. doi: 10.1093/fqs/fyx006
Silva, G. F., Silva, B. A. N., Sanglard, D., Domingos, R. L., Gonçalves, M. F., Cardoso, H. M. C., Cardoso, L. A., Pereira, T. S. B., Maia, B. C. A., Brito, S. K., Martins, L. T. S., Miranda, A. L., Haupenthal, L. A., Hirtenlehner, S., & Abreu, M. L. T. (2023). Performance and gut permeability of post-weaned piglets are influenced by different sources of lignocellulose fiber. Livestock Science, 274, 105274. doi: 10.1016/j.livsci.2023.105274
Sobestiansky, J., & Barcellos, D. (2007). Doenças dos suínos. Cânone Editorial.
Suetsuna K. (1999). Separation and identification of antioxidant peptides from proteolytic digest of dried bonito. Nippon Suisan Gakkaishi, 65(1), 92-96. doi: 10.2331/suisan.65.92
Suetsuna, K. (1998). Isolation and characterization of angiotensin I-converting enzyme inhibitor dipeptides derived from Allium sativum L (garlic). Journal of Nutritional Biochemistry, 9(7), 415-419. doi: 10.1016/S0955-2863(98)00036-9
Sun, Y., & Kim, S. W. (2017). Intestinal challenge with enterotoxigenic Escherichia coli in pigs, and nutritional intervention to prevent postweaning diarrhea. Animal Nutrition, 3(4), 322-330. doi: 10.1016/j.aninu.2017.10.001
Theysgeur, S., Cudennec, B., Deracinois, B., Perrin, C., Guiller, I., Lepoudère, A., Flahaut, C., & Revallec, R. (2021). New bioactive peptides identified from a tilapia byproduct hydrolysate exerting effects on DPP-IV activity and intestinal hormones regulation after canine gastrointestinal simulated digestion. Molecules, 26(1), 136. doi: 10.3390/molecules26010136
Torrallardona, D. (2010). Spray dried animal plasma as an alternative to antibiotics in weanling pigs. Asian-Australasian Journal of Animal Sciences, 23(1), 131-148. doi: 10.5713/ajas.2010.70630
Turner, G., Du, F., & Varshavsky, A. (2000). Peptides accelerate their uptake by activating a ubiquitin-dependent proteolytic pathway. Nature, 405(6786), 579-583. doi: 10.1038/35014629
Udenigwe, C., Li, H., & Aluko, R. E. (2012). Quantitative structure-activity relationship modeling of renin-inhibiting dipeptides. Amino Acids, 42(4), 1379-1386. doi: 10.1007/s00726-011-0833-2
Van Dijk, A. J., Everts, H., Nabuurs, M. J. A., Margry, R. J. C. F., & Beynen, A. C. (2001). Growth performance of weanling pigs fed spray-dried animal plasma: a review. Livestock Production Science, 68(2-3), 263-274. doi: 10.1016/S0301-6226(00)00229-3
Van Platerink, C. J., Janssen, H.-G. M., & Haverkamp, J. (2008). Application of at-line two-dimensional liquid chromatography-mass spectrometry for identification of small hydrophilic angiotensin I-inhibiting peptides in milk hydrolysates. Analytical and Bioanalytical Chemistry, 391(1), 299-307. doi: 10.1007/s00216-008-1990-3
Vicuña, E. A., Kuttappan, V. A., Tellez, G., Hernandez-Velasco, X., Seeber-Galarza, R., Latorre, J. D., Faulkner, O. B., Wolfenden, A. D., Hargis, B. M., & Bielke, L. R. (2015). Dose titration of FITC-D for optimal measurement of enteric inflammation in broiler chicks. Poult Science, 94(6), 1353-1359. doi: 10.3382/ps/pev111
Vidal, A. R., Cansian, R. L., Mello, R. O., Demiate, I. M., Kempka, A. P., Dornelles, R. C. P., Rodriguez, J. M. L., & Campagnol, P. C. B. (2022). Production of collagens and protein hydrolysates with antimicrobial and antioxidant activity from sheep slaughter by-products. Antioxidants, 11(6), 1173. doi: 10.3390/antiox11061173
Wang, W., & Mejia, E. G. (2006). A new frontier in soy bioactive peptides that may prevent age-related chronic diseases. Comprehensive Reviews in Food Science and Food Safety, 4(4), 63-78. doi: 10.1111/j.1541-4337.2005.tb00075.x
Wei, D., Fan, W., & Xu, Y. (2021). Identification of water-soluble peptides in distilled spent grain and its angiotensin converting enzyme (ACE) inhibitory activity based on UPLC-Q-TOF-MS and proteomics analysis. Food Chemistry, 353, 129521. 10.1016/j.foodchem.2021.129521
Wijtten, P. J. A., Meulen, J. van der, & Verstegen, M. W. A. (2011). Intestinal barrier function and absorption in pigs after weaning: a review. British Journal of Nutrition, 105(7), 967-981. doi: 10.1017/S0007114510005660
Wu, H., He, H.-L., Chen, X.-L., Sun, C.-Y., Zhang, Y.-Z., & Zhou, B.-C. (2008). Purification and identification of novel angiotensin I-converting enzyme inhibitory peptides from shark meat hydrolysate. Process Biochemistry, 43(4), 457-461. doi: 10.1016/j.procbio.2008.01.018
Wu, J., Aluko, R. E., & Nakai, S. (2006). Structural requirements of angiotensin I-converting enzyme inhibitory activity: quantitative structure-activity relationship study of di- and tripeptides. Journal of Agricultural Food Chemistry, 54(3), 732-738. doi: 10.1021/jf051263l
Wylensek, D., Hitch, T. C. A., Riedel, T., Afrizal, A., Kumar, N., Wortmann, E., Liu, T., Devendran, S., Lesker, T. R., Hernández, S. B., Heine, V., Buhl, E. M., D’Agostino, P. M., Cumbo, F., Fischöder, T., Wyschkon, M., Looft, T., Parreira, V. R., Abt, B., … Clavel, T. (2020). A collection of bacterial isolates from the pig intestine reveals functional and taxonomic diversity. Nature Communications, 11(1), 1-26. doi: 10.1038/s41467-020-19929-w
Xiong, X., Tan, B., Song, M., Ji, P., Kim, K., Yin, Y., & Liu, Y. (2019). Nutritional intervention for the intestinal development and health of weaned pigs. Frontiers in Veterinary Science, 6(46), 1-14. doi: 10.3389/fvets.2019.00046
Xu, B., Fu, J., Zhu, L., Li, Z., Jin, M., & Wang, Y. (2021). Overall assessment of antibiotic substitutes for pigs: a set of meta-analyses. Journal of Animal Science and Biotechnology, 12(1), 1-15. doi: 10.1186/s40104-020-00534-2
Yano, S., Suzuki, K., & Funatsu, G. (1996). Isolation from alpha-zein of thermolysin peptides with angiotensin I-converting enzyme inhibitory activity. Bioscience Biotechnology & Biochemistry, 60(4), 661-663. doi: 10.1271/bbb.60.661
Yokomizo, A., Takenaka, Y., & Takenaka, T. (2002). Antioxidative activity of peptides prepared from Okara protein. Food Science and Technology Research, 8(4), 357-359. doi: 10.3136/fstr.8.357
Zhu, Q., Wang, Y., Liu, Y., Yu, B., He, J., Zheng, P., Mao, X., Huang, Z., Luo, J., Luo, Y., Yan, H., & Yu, J. (2022). Effects of a novel protease on growth performance, nutrient digestibility and intestinal health in weaned piglets. Animals, 12(20), 1-15. doi: 10.3390/ani12202803
Downloads
Publicado
Como Citar
Edição
Seção
Licença
Copyright (c) 2026 Geraldo Camilo Alberton, José Luciano Andriguetto, Eduardo César Meurer, Sergio Rodrigo Fernandes, Gizele Fonseca Silva, Marcio Paschoalloto, Álvaro Henrique Rocha, Marcos Paulo Beuron, Évelin Lemos Oliveira, Anderson Ferreira Cunha

Este trabalho está licenciado sob uma licença Creative Commons Attribution-NonCommercial 4.0 International License.
Semina: Ciências Agrárias adota para suas publicações a licença CC-BY-NC, sendo os direitos autorais do autor, em casos de republicação recomendamos aos autores a indicação de primeira publicação nesta revista.
Esta licença permite copiar e redistribuir o material em qualquer meio ou formato, remixar, transformar e desenvolver o material, desde que não seja para fins comerciais. E deve-se atribuir o devido crédito ao criador.
As opiniões emitidas pelos autores dos artigos são de sua exclusiva responsabilidade.
A revista se reserva o direito de efetuar, nos originais, alterações de ordem normativa, ortográfica e gramatical, com vistas a manter o padrão culto da língua e a credibilidade do veículo. Respeitará, no entanto, o estilo de escrever dos autores. Alterações, correções ou sugestões de ordem conceitual serão encaminhadas aos autores, quando necessário.













