DOI QR코드

DOI QR Code

Exploration of nutritional and bioactive peptide properties in goat meat from various primal cuts during in vitro gastrointestinal digestion and absorption

  • Pichitpon Luasiri (School of Animal Technology and Innovation, Institute of Agricultural Technology, Suranaree University of Technology) ;
  • Papungkorn Sangsawad (School of Animal Technology and Innovation, Institute of Agricultural Technology, Suranaree University of Technology) ;
  • Jaksuma Pongsetkul (School of Animal Technology and Innovation, Institute of Agricultural Technology, Suranaree University of Technology) ;
  • Pramote Paengkoum (School of Animal Technology and Innovation, Institute of Agricultural Technology, Suranaree University of Technology) ;
  • Chatsirin Nakharuthai (School of Animal Technology and Innovation, Institute of Agricultural Technology, Suranaree University of Technology) ;
  • Saranya Suwanangul (Program in Food Science and Technology, Faculty of Engineering and Agro-industry, Maejo University) ;
  • Sasikan Katemala (Faculty of Agriculture at Kamphaeng Saen, Kasetsart University, Kamphaeng Saen Campus) ;
  • Narathip Sujinda (Faculty of Agriculture at Kamphaeng Saen, Kasetsart University, Kamphaeng Saen Campus) ;
  • Jukkrapong Pinyo (Faculty of Agriculture at Kamphaeng Saen, Kasetsart University, Kamphaeng Saen Campus) ;
  • Jarunan Chainam (Faculty of Agricultural Technology, Valaya Alongkorn Rajabhat University under the Royal Patronage) ;
  • Chompoonuch Khongla (Department of Applied Biology, Faculty of Sciences and Liberal Arts, Rajamangala University of Technology Isan) ;
  • Supaluk Sorapukdee (Office of Administrative Interdisciplinary Program on Agricultural Technology, School of Agricultural Technology, King Mongkut's Institute of Technology Ladkrabang)
  • 투고 : 2023.09.09
  • 심사 : 2024.01.15
  • 발행 : 2024.06.01

초록

Objective: This research aims to explore the nutritional and bioactive peptide properties of goat meat taken from various primal cuts, including the breast, shoulder, rib, loin, and leg, to produce these bioactive peptides during in vitro gastrointestinal (GI) digestion and absorption. Methods: The goat meat from various primal cuts was obtained from Boer goats with an average carcass weight of 30±2 kg. The meat was collected within 3 h after slaughter and was stored at -80℃ until analysis. A comprehensive assessment encompassed various aspects, including the chemical composition, cooking properties, in vitro GI digestion, bioactive characteristics, and the bioavailability of the resulting peptides. Results: The findings indicate that the loin muscles contain the highest protein and essential amino acid composition. When the meats were cooked at 70℃ for 30 min, they exhibited distinct protein compositions and quantities in the sodium dodecyl sulfate-polyacrylamide gel electrophoresis profile, suggesting they served as different protein substrates during GI digestion. Subsequent in vitro simulated GI digestion revealed that the cooked shoulder and loin underwent the most significant hydrolysis during the intestinal phase, resulting in the strongest angiotensin-converting enzyme (ACE) and dipeptidyl peptidase-IV (DPP-IV) inhibition. Following in vitro GI peptide absorption using a Caco-2 cell monolayer, the GI peptide derived from the cooked loin demonstrated greater bioavailability and a higher degree of ACE and DPP-IV inhibition than the shoulder peptide. Conclusion: This study highlights the potential of goat meat, particularly cooked loin, as a functional meat source for protein, essential amino acids, and bioactive peptides during GI digestion and absorption. These peptides promise to play a role in preventing and treating metabolic diseases due to their dual inhibitory effects on ACE and DPP-IV.

키워드

과제정보

This work was supported by Suranaree University of Technology (SUT), Maejo University, Kasetsart University Kamphaeng Saen Campus, Valaya Alongkorn Rajabhat University under the Royal Patronage, Rajamangala University of Technology Isan, King Mongkut's Institute of Technology Ladkrabang, Thailand Science Research and Innovation (TSRI), and the National Science, Research, and Innovation Fund (NSRF) (project codes: FF3-303-65-36-17).

참고문헌

  1. Gawat M, Boland M, Singh J, Kaur L. Goat meat: production and quality attributes. Foods 2023;12:3130. https://doi.org/10.3390/foods12163130 
  2. Pralomkarn W, Supakorn C, Boonsanit D. Knowledge in goats in Thailand. Walailak J Sci Technol 2011;9:93-105. 
  3. Corazzin M, Del Bianco S, Bovolenta S, Piasentier E. Carcass characteristics and meat quality of sheep and goat. In: Lorenzo JM, Munekata PES, Barba FJ, Toldra F. More than beef, pork and chicken-the production, processing, and quality traits of other sources of meat for human diet. Cham, Switzerland; Springer: 2019. pp. 119-65. https://doi.org/10.1007/978-3-030-05484-7_6 
  4. Sangsawad P, Katemala S, Pao D, Suwanangul S, Jeencham R, Sutheerawattananonda M. Integrated evaluation of dual-functional DPP-IV and ACE inhibitory effects of peptides derived from sericin hydrolysis and their stabilities during in vitro-simulated gastrointestinal and plasmin digestions. Foods 2022;11:3931. https://doi.org/10.3390/foods11233931 
  5. Sangsawad P, Roytrakul S, Yongsawatdigul J. Angiotensin converting enzyme (ACE) inhibitory peptides derived from the simulated in vitro gastrointestinal digestion of cooked chicken breast. J Funct Foods 2017;29:77-83. https://doi.org/10.1016/j.jff.2016.12.005 
  6. Martini S, Conte A, Tagliazucchi D. Comparative peptidomic profile and bioactivities of cooked beef, pork, chicken and turkey meat after in vitro gastro-intestinal digestion. J Proteom 2019;208:103500. https://doi.org/10.1016/j.jprot.2019.103500 
  7. Brodkorb A, Egger L, Alminger M, et al. INFOGEST static in vitro simulation of gastrointestinal food digestion. Nat Protoc 2019;14:991-1014. https://doi.org/10.1038/s41596-018-0119-1 
  8. Vermeirssen V, Van Camp J, Verstraete W. Bioavailability of angiotensin I converting enzyme inhibitory peptides. Br J Nutr 2004;92:357-66. https://doi.org/10.1079/BJN20041189 
  9. Xu Q, Hong H, Wu J, Yan X. Bioavailability of bioactive peptides derived from food proteins across the intestinal epithelial membrane: a review. Trends Food Sci Technol 2019;86:399-411. https://doi.org/10.1016/j.tifs.2019.02.050 
  10. Liu R, Cheng J, Wu H. Discovery of food-derived dipeptidyl peptidase IV inhibitory peptides: a review. Int J Mol Sci 2019;20:463. https://doi.org/10.3390/ijms20030463 
  11. Miralles B, Amigo L, Recio I. Critical review and perspectives on food-derived antihypertensive peptides. J Agric Food Chem 2018;66:9384-90. https://doi.org/10.1021/acs.jafc.8b02603 
  12. Bhat Z, Kumar S, Bhat HF. Bioactive peptides of animal origin: a review. J Food Sci Technol 2015;52:5377-92. https://doi.org/10.1007/s13197-015-1731-5 
  13. Liu F, Meng L, Gao X, Li X, Luo H, Dai R. Effect of end point temperature on cooking losses, shear force, color, protein solubility and microstructure of goat meat. J Food Process Preserv 2013;37:275-83. https://doi.org/10.1111/j.1745-4549.2011.00646.x 
  14. Biyikli M, Akoglu A, Kurhan S, Akoglu IT. Effect of different Sous Vide cooking temperature-time combinations on the physicochemical, microbiological, and sensory properties of turkey cutlet. Int J Gastron Food Sci 2020;20:100204. https://doi.org/10.1016/j.ijgfs.2020.100204 
  15. Taethaisong N, Paengkoum S, Nakharuthai C, et al. Effect of purple neem foliage as a feed supplement on nutrient apparent digestibility, nitrogen utilization, rumen fermentation, microbial population, plasma antioxidants, meat quality and fatty acid profile of goats. Animals 2022;12:2985. https://doi.org/10.3390/ani12212985 
  16. Purba RAP, Suong NTM, Paengkoum S, Schonewille JT, Paengkoum P. Dietary inclusion of anthocyanin-rich black cane silage treated with ferrous sulfate heptahydrate reduces oxidative stress and promotes tender meat production in goats. Front Vet Sci 2022;9:969321. https://doi.org/10.3389/fvets.2022.969321 
  17. Paengkoum P, Lukkananukool A, Bureenok S, et al. Effect of feeding systems on meat goat CLA. Int J Nutr Food Eng 2013;7:894-6. https://doi.org/10.5281/zenodo.1087734 
  18. Das AK, Rajkumar V. Comparative study on carcass characteristics and meat quality of three Indian goat breeds. Indian J Anim Sci 2010;80:1014-8. 
  19. Latimer GW Jr. Official methods of analysis of AOAC international. Gaithersburg, MD, USA: AOAC International; 2016. 
  20. Hamzeh A, Noisa P, Yongsawatdigul J. Characterization of the antioxidant and ACE-inhibitory activities of Thai fish sauce at different stages of fermentation. J Funct Foods 2020;64:103699. https://doi.org/10.1016/j.jff.2019.103699 
  21. Sangsawad P, Kiatsongchai R, Chitsomboon B, Yongsawatdigul J. Chemical and cellular antioxidant activities of chicken breast muscle subjected to various thermal treatments followed by simulated gastrointestinal digestion. J Food Sci 2016;81:C2431-8. https://doi.org/10.1111/1750-3841.13418 
  22. Adler-Nissen J. Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid. J Agric Food Chem 1979;27:1256-62. https://doi.org/10.1021/jf60226a042 
  23. Liang N, Kim BJ, Dallas DC. Bioavailability of peptides derived from the in vitro digestion of human milk assessed by caco-2 cell monolayers. J Agric Food Chem 2022;70:7077-84. https://doi.org/10.1021/acs.jafc.2c01246 
  24. Sangsawad P, Roytrakul S, Choowongkomon K, et al. Transepithelial transport across Caco-2 cell monolayers of angiotensin converting enzyme (ACE) inhibitory peptides derived from simulated in vitro gastrointestinal digestion of cooked chicken muscles. Food Chem 2018;251:77-85. https://doi.org/10.1016/j.foodchem.2018.01.047 
  25. Mohammed HHH, Jin G, Ma M, et al. Comparative characterization of proximate nutritional compositions, microbial quality and safety of camel meat in relation to mutton, beef, and chicken. LWT 2020;118:108714. https://doi.org/10.1016/j.lwt.2019.108714 
  26. Shija DS, Mtenga LA, Kimambo AE, et al. Chemical composition and meat quality attributes of indigenous sheep and goats from traditional production system in Tanzania. Asian-Australas J Anim Sci 2013;26:295-302. https://doi.org/10.5713/ajas.2012.12432 
  27. Sen AR, Santra A, Karim SA. Carcass yield, composition and meat quality attributes of sheep and goat under semiarid conditions. Meat Sci 2004;66:757-63. https://doi.org/10.1016/S0309-1740(03)00035-4 
  28. Utrera M, Morcuende D, Estevez M. Temperature of frozen storage affects the nature and consequences of protein oxidation in beef patties. Meat Sci 2014;96:1250-7. https://doi.org/10.1016/j.meatsci.2013.10.032 
  29. Rotola-Pukkila MK, Pihlajaviita ST, Kaimainen MT, Hopia AI. Concentration of umami compounds in pork meat and cooking juice with different cooking times and temperatures. J Food Sci 2015;80:C2711-6. https://doi.org/10.1111/1750-3841.13127 
  30. Gorska-Warsewicz H, Laskowski W, Kulykovets O, Kudlinska-Chylak A, Czeczotko M, Rejman K. Food products as sources of protein and amino acids-the case of Poland. Nutrients 2018;10:1977. https://doi.org/10.3390/nu10121977 
  31. Gannon NP, Schnuck JK, Vaughan RA. BCAA metabolism and insulin sensitivity-dysregulated by metabolic status? Mol Nutr Food Res 2018;62:1700756. https://doi.org/10.1002/mnfr.201700756 
  32. Potue P, Chiangsaen P, Maneesai P, et al. Effects of Thai native chicken breast meat consumption on serum uric acid level, biochemical parameters, and antioxidant activities in rats. Sci Rep 2022;12:14056. https://doi.org/10.1038/s41598-022-18484-2 
  33. Alekseeva E, Kolchina V. Amino acid composition of beef obtained from the specialized meat cattle. IOP Conf Ser Earth Environ Sci 2019;341:012136. https://doi.org/10.1088/1755-1315/341/1/012136 
  34. Liu Y, Zhang L, Gao S, et al. Effect of protein oxidation in meat and exudates on the water holding capacity in bighead carp (Hypophthalmichthys nobilis) subjected to frozen storage. Food Chem 2022;370:131079. https://doi.org/10.1016/j.foodchem.2021.131079 
  35. Domian E, Manko-Jurkowska D. The effect of homogenization and heat treatment on gelation of whey proteins in emulsions. J Food Eng 2022;319:110915. https://doi.org/10.1016/j.jfoodeng.2021.110915 
  36. Ganapathy V, Ganapathy ME, Leibach FH. Protein digestion and assimilation. In: Yamada T, editors. Textbook of gastroenterology. Oxford, UK: Blackwell Publishing Ltd; 2008. p. 464-77. https://doi.org/10.1002/9781444303254.ch19 
  37. Hong SM, Tanaka M, Koyanagi R, Shen W, Matsui T. Structural design of oligopeptides for intestinal transport model. J Agric Food Chem 2016;64:2072-9. https://doi.org/10.1021/acs.jafc.6b00279 
  38. Ketnawa S, Suwal S, Huang JY, Liceaga AM. Selective separation and characterization of dual ACE and DPP-IV inhibitory peptides from rainbow trout (Oncorhynchus mykiss) protein hydrolysates. Int J Food Sci Technol 2019;54:1062-73. https://doi.org/10.1111/ijfs.13939 
  39. Hernandez-Olivas E, Munoz-Pina S, Garcia-Hernandez J, Andres A, Heredia A. Impact of common gastrointestinal disorders in elderly on in vitro meat protein digestibility and related properties. Food Biosci 2022;46:101560. https://doi.org/10.1016/j.fbio.2022.101560 
  40. Fleury L, Deracinois B, Dugardin C, et al. In vivo and in vitro comparison of the DPP-IV Inhibitory potential of food proteins from different origins after gastrointestinal digestion. Int J Mol Sci 2022;23:8365. https://doi.org/10.3390/ijms23158365 
  41. Cross ML, Gill HS. Modulation of immune function by a modified bovine whey protein concentrate. Immunol Cell Biol 1999;77:345-50. https://doi.org/10.1046/j.1440-1711.1999.00834.x 
  42. Lacroix IME, Chen XM, Kitts DD, Li-Chan ECY. Investigation into the bioavailability of milk protein-derived peptides with dipeptidyl-peptidase IV inhibitory activity using Caco-2 cell monolayers. Food Funct 2017;8:701-9. https://doi.org/10.1039/C6FO01411A 
  43. Sangsawad P, Choowongkomon K, Kitts DD, Chen XM, Li-Chan ECY, Yongsawatdigul J. Transepithelial transport and structural changes of chicken angiotensin I-converting enzyme (ACE) inhibitory peptides through Caco-2 cell monolayers. J Funct Foods 2018;45:401-8. https://doi.org/10.1016/j.jff.2018.04.020 
  44. Gallego M, Grootaert C, Mora L, Aristoy MC, Camp JV, Toldra F. Transepithelial transport of dry-cured ham peptides with ACE inhibitory activity through a Caco-2 cell monolayer. J Funct Foods 2016;21:388-95. https://doi.org/10.1016/j.jff.2015.11.046 
  45. Miguel M, Gomez-Ruiz JA, Recio I, Aleixandre A. Changes in arterial blood pressure after single oral administration of milk-casein-derived peptides in spontaneously hypertensive rats. Mol Nutr Food Res 2010;54:1422-7. https://doi.org/10.1002/mnfr.200900448 
  46. Garzon AG, Ferreira MdR, Cian RE, Oliva ME, D'Alessandro ME, Drago SR. Microencapsulated bioactive peptides from brewer's spent grain promotes antihypertensive and antidiabetogenic effects on a hypertensive and insulin-resistant rat model. J Food Biochem 2022;46:e14283. https://doi.org/10.1111/jfbc.14283 
  47. Pei J, Liu Z, Pan D, Zhao Y, Dang Y, Gao X. Transport, stability, and in vivo hypoglycemic effect of a broccoli-derived DPP-IV inhibitory peptide VPLVM. J Agric Food Chem 2022;70:4934-41. https://doi.org/10.1021/acs.jafc.1c08191