Resumen
La industria avícola representa una de las actividades pecuarias más relevantes económicamente en México, sin embargo, genera grandes volúmenes de residuos, entre ellos las plumas. Debido a su alto contenido de queratina, representan una excelente alternativa para su valorización. Este estudio tuvo como objetivo extraer y caracterizar queratina de plumas de pollo mediante un proceso optimizado de hidrólisis alcalina asistida por ultrasonido. Se empleó un diseño de superficie de respuesta con tres factores: temperatura (30, 52.5 y 75 °C), tiempo de sonicación (60, 105 y 150 min) y concentración de NaOH (1, 3.5 y 6 %). Las condiciones óptimas fueron 75 °C, 150 min y 3.5 % de NaOH, alcanzando 3.28 mg de proteína hidrolizada/mL. La temperatura fue el factor más influyente en la extracción. El análisis por SDS-PAGE mostró fragmentos de 5–25 kDa, característicos de queratina hidrolizada, mientras que el análisis por HPLC identificó 16 aminoácidos, siendo glicina, serina y alanina los más abundantes. El análisis in silico reveló péptidos con potencial actividad biológica como inhibidores de la Dipeptidil Peptidasa IV y de la Enzima Convertidora de la Angiotensina. En conjunto, estos resultados demuestran el potencial de los métodos alternativos de extracción para la revalorización sostenible de los desechos avícolas.
Citas
Ai, L., Liu, L., Zheng, L., Liu, Y., Sun, B., Su, G., Xu, J., Chen, Y., & Zhao, M. (2024). An on-line stop-flow RPLC × SEC-MS/DPPH radical scavenging activity analysis system and its application in separation and identification of antioxidant peptides. Food chemistry, 436, 137670. https://doi.org/10.1016/j.foodchem.2023.137670
Alahyaribeik, S., & Ullah, A. (2020). Methods of keratin extraction from poultry feathers and their effects on antioxidant activity of extracted keratin. International journal of biological macromolecules, 148, 449–456. https://doi.org/10.1016/j.ijbiomac.2020.01.144
Arámburo-Gálvez, J. G., Tinoco-Narez-Gil, R., Mora-Melgem, J. A., Sánchez-Cárdenas, C. A., Gracia-Valenzuela, M. H., Flores-Mendoza, L. K., Figueroa-Salcido, O. G., & Ontiveros, N. (2024). In Silico Hydrolysis of Lupin (Lupinus angustifolius L.) Conglutins with Plant Proteases Releases Antihypertensive and Antidiabetic Peptides That Are Bioavailable, Non-Toxic, and Gastrointestinal Digestion Stable. International journal of molecular sciences, 25(23), 12866. https://doi.org/10.3390/ijms252312866
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 sources of biosynthesis. Biochemistry. Biokhimiia, 63(2), 119–124. https://pubmed.ncbi.nlm.nih.gov/9526102/
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. https://doi.org/10.1021/jf904300q
Bilge S., Erkmen C., Yücel A. (2025). A review on keratin-based sensor platforms: Structural properties of keratin, their role in analytical sensing applications, and future perspectives. International Journal of Biological Macromolecules. 321(3):146469. https://doi.org/10.1016/j.ijbiomac.2025.146469
Burge, S., Kelly, E., Lonsdale, D., Mutowo-Muellenet, P., McAnulla, C., Mitchell, A., Sangrador-Vegas, A., Yong, S. Y., Mulder, N., & Hunter, S. (2012). Manual GO annotation of predictive protein signatures: the InterPro approach to GO curation. Database : the journal of biological databases and curation, 2012, bar068. https://doi.org/10.1093/database/bar068
Burnett, C. L., Bergfeld, W. F., Belsito, D. V., Hill, R. A., Klaassen, C. D., Liebler, D. C., Marks, J. G., Jr, Shank, R. C., Slaga, T. J., Snyder, P. W., Gill, L. J., & Heldreth, B. (2021). Safety Assessment of Keratin and Keratin-Derived Ingredients as Used in Cosmetics. International journal of toxicology, 40(2_suppl), 36S–51S. https://doi.org/10.1177/10915818211013019
Cain G. A., Christos T. E., Johnson A. L., Pottorf R. S., Tam S., & Schmidt W. K. (1993). Identification of simpler analogs of neurotensin(913) which retain antinociceptive activity. Bioorganic & Medicinal Chemistry Letters., 3, 1767-1772. https://doi.org/10.1016/S0960-894X(00)80059-1
Carre, W., Wang, X., Porter, T. E., Nys, Y., Tang, J., Bernberg, E., Morgan, R., Burnside, J., Aggrey, S. E., Simon, J., & Cogburn, L. A. (2006). Chicken genomics resource: sequencing and annotation of 35,407 ESTs from single and multiple tissue cDNA libraries and CAP3 assembly of a chicken gene index. Physiological genomics, 25(3), 514–524. https://doi.org/10.1152/physiolgenomics.00207.2005
Dąbrowska, M., Sommer, A., Sinkiewicz, I., Taraszkiewicz, A., & Staroszczyk, H. (2022). An optimal designed experiment for the alkaline hydrolysis of feather keratin. Environmental science and pollution research international, 29(16), 24145–24154. https://doi.org/10.1007/s11356-021-17649-2
Dhanda, S., Singh, J., & Singh, H. (2008). Hydrolysis of various bioactive peptides by goat brain dipeptidylpeptidase-III homologue. Cell biochemistry and function, 26(3), 339–345. https://doi.org/10.1002/cbf.1448
Dion, N., Cohen, P., Crine, P., & Boileau, G. (1997). Characterisation of neprilysin (EC 3.4.24.11) S2' subsite. FEBS letters, 411(1), 140–144. https://doi.org/10.1016/s0014-5793(97)00681-9
Fontoura, R., Daroit, D. J., Corrêa, A. P. F., Moresco, K. S., Santi, L., Beys-da-Silva, W. O., Yates, J. R., 3rd, Moreira, J. C. F., & Brandelli, A. (2019). Characterization of a novel antioxidant peptide from feather keratin hydrolysates. New biotechnology, 49, 71–76. https://doi.org/10.1016/j.nbt.2018.09.003
Gałęzowska, G., Ratajczyk, J., & Wolska, L. (2021). Determination of amino acids in human biological fluids by high-performance liquid chromatography: critical review. Amino acids, 53(7), 993–1009. https://doi.org/10.1007/s00726-021-03002-x
Gallego, M., Aristoy, M. C., & Toldrá, F. (2014). Dipeptidyl peptidase IV inhibitory peptides generated in Spanish dry-cured ham. Meat science, 96(2 Pt A), 757–761. https://doi.org/10.1016/j.meatsci.2013.09.014
Ganellin, C. R., Bishop, P. B., Bambal, R. B., Chan, S. M., Law, J. K., Marabout, B., Luthra, P. M., Moore, A. N., Peschard, O., Bourgeat, P., Rose, C., Vargas, F., & Schwartz, J. C. (2000). Inhibitors of tripeptidyl peptidase II. 2. Generation of the first novel lead inhibitor of cholecystokinin-8-inactivating peptidase: a strategy for the design of peptidase inhibitors. Journal of medicinal chemistry, 43(4), 664–674. https://doi.org/10.1021/jm990226g
Goldberg, O., Luini, A., & Teichberg, V. I. (1983). Bicyclic lactones derived from kainic acid as novel selective antagonists of neuroexcitatory amino acids. Journal of medicinal chemistry, 26(1), 39–42. https://doi.org/10.1021/jm00355a009
Greenwold, M. J., & Sawyer, R. H. (2010). Genomic organization and molecular phylogenies of the beta (beta) keratin multigene family in the chicken (Gallus gallus) and zebra finch (Taeniopygia guttata): implications for feather evolution. BMC evolutionary biology, 10, 148. https://doi.org/10.1186/1471-2148-10-148
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. https://doi.org/10.1016/j.foodchem.2012.02.183
Hebert, E. M., Mamone, G., Picariello, G., Raya, R. R., Savoy, G., Ferranti, P., & Addeo, F. (2008). Characterization of the pattern of alphas1- and beta-casein breakdown and release of a bioactive peptide by a cell envelope proteinase from Lactobacillus delbrueckii subsp. lactis CRL 581. Applied and environmental microbiology, 74(12), 3682–3689. https://doi.org/10.1128/AEM.00247-08
Heres A., Yokoyama I., Gallego M., Toldrá F., Arihara K., & Mora L. (2021). Antihypertensive potential of sweet Ala-Ala dipeptide and its quantitation in dry-cured ham at different processing conditions. Journal of Functional Foods, 87, 104818. https://doi.org/10.1016/j.jff.2021.104818
Hikida, A., Ito, K., 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. https://doi.org/10.1016/j.bbrc.2012.12.073
Ichimura, T., Yamanaka, A., Otsuka, T., Yamashita, E., & Maruyama, S. (2009). Antihypertensive effect of enzymatic hydrolysate of collagen and Gly-Pro in spontaneously hypertensive rats. Bioscience, biotechnology, and biochemistry, 73(10), 2317–2319. https://doi.org/10.1271/bbb.90197
Jo, D. M., Khan, F., Park, S. K., Ko, S. C., Kim, K. W., Yang, D., Kim, J. Y., Oh, G. W., Choi, G., Lee, D. S., & Kim, Y. M. (2024). From Sea to Lab: Angiotensin I-Converting Enzyme Inhibition by Marine Peptides-Mechanisms and Applications. Marine drugs, 22(10), 449. https://doi.org/10.3390/md22100449
Kamarudin, N. B., Sharma, S., Gupta, A., Kee, C. G., Chik, S. M. S. B. T., & Gupta, R. (2017). Statistical investigation of extraction parameters of keratin from chicken feather using Design-Expert. 3 Biotech, 7(2), 127. https://doi.org/10.1007/s13205-017-0767-9
Kanegawa, N., Suzuki, C., & Ohinata, K. (2010). Dipeptide Tyr-Leu (YL) exhibits anxiolytic-like activity after oral administration via activating serotonin 5-HT1A, dopamine D1 and GABAA receptors in mice. FEBS letters, 584(3), 599–604. https://doi.org/10.1016/j.febslet.2009.12.008
Khan, A. A., Parikh, H., & Qureshi, M. R. N. (2022). A review on chicken feather fiber (CFF) and its application in composites. Journal of Natural Fibers, 19(16), 12565-12585. https://doi.org/10.1080/15440478.2022.2073495
Khumalo, M., Sithole, B., & Tesfaye, T. (2020). Valorisation of waste chicken feathers: Optimisation of keratin extraction from waste chicken feathers by sodium bisulphite, sodium dodecyl sulphate and urea. Journal of environmental management, 262, 110329. https://doi.org/10.1016/j.jenvman.2020.110329
Kumagai, Y., Toji, K., Katsukura, S., Morikawa, R., Uji, T., Yasui, H., Shimizu, T., & Kishimura, H. (2021). Characterization of ACE Inhibitory Peptides Prepared from Pyropia pseudolinearis Protein. Marine drugs, 19(4), 200. https://doi.org/10.3390/md19040200
Lan, V. 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. https://doi.org/10.1016/j.foodchem.2014.11.131
Lee, C. M., & Snyder, S. H. (1982). Dipeptidyl-aminopeptidase III of rat brain. Selective affinity for enkephalin and angiotensin. The Journal of biological chemistry, 257(20), 12043–12050. https://pubmed.ncbi.nlm.nih.gov/6749851/
Lorenzo-Hernando, A., Ruiz-Vegas, J., Vega-Alegre, M., & Bolado-Rodríguez, S. (2019). Recovery of proteins from biomass grown in pig manure microalgae-based treatment plants by alkaline hydrolysis and acidic precipitation. Bioresource Technology, 273, 599–607. https://doi.org/10.1016/j.biortech.2018.11.068
Luzarowski, M., Vicente, R., Kiselev, A., Wagner, M., Schlossarek, D., Erban, A., de Souza, L. P., Childs, D., Wojciechowska, I., Luzarowska, U., Górka, M., Sokołowska, E. M., Kosmacz, M., Moreno, J. C., Brzezińska, A., Vegesna, B., Kopka, J., Fernie, A. R., Willmitzer, L., Ewald, J. C., … Skirycz, A. (2021). Global mapping of protein-metabolite interactions in Saccharomyces cerevisiae reveals that Ser-Leu dipeptide regulates phosphoglycerate kinase activity. Communications biology, 4(1), 181. https://doi.org/10.1038/s42003-021-01684-3
Ma R., Chen Q., Dai Y., Huang Y., Hou Q., Huang Y., Zhong K., Huang Y., Gao H., Bu Q. (2022). Identification of novel antioxidant peptides from sea squirt (Halocynthia roretzi) and its neuroprotective effect in 6-OHDA-induced neurotoxicity. Food & Function, 13, 6008-6021. https://doi.org/10.1039/D2FO00729K
Minkiewicz, P., Iwaniak, A., & Darewicz, M. (2019). BIOPEP-UWM Database of Bioactive Peptides: Current Opportunities. International journal of molecular sciences, 20(23), 5978. https://doi.org/10.3390/ijms20235978
Mokrejš, P., Huťťa, M., Pavlačková, J., & Egner, P. (2017). Preparation of Keratin Hydrolysate from Chicken Feathers and Its Application in Cosmetics. Journal of visualized experiments : JoVE, (129), 56254. https://doi.org/10.3791/56254
Molloy, P. L., Powell, B. C., Gregg, K., Barone, E. D., & Rogers, G. E. (1982). Organisation of feather keratin genes in the chick genome. Nucleic acids research, 10(19), 6007–6021. https://doi.org/10.1093/nar/10.19.6007
Moreno-Mariscal, C., Carrera-Alvarado, G., Mora, L., & Toldrá, F. (2025). Neprilysin (NEP) and Angiotensin Converting Enzyme-I (ACE-I) inhibitory dipeptides from chicken carcass hydrolysates. LWT - Food Science and Technology, 221. https://doi.org/10.1016/j.lwt.2025.117591
Morifuji, M., Koga, J., Kawanaka, K., & Higuchi, M. (2009). Branched-chain amino acid-containing dipeptides, identified from whey protein hydrolysates, stimulate glucose uptake rate in L6 myotubes and isolated skeletal muscles. Journal of nutritional science and vitaminology, 55(1), 81–86. https://doi.org/10.3177/jnsv.55.81
Mullally, M. M., Meisel, H., & FitzGerald, R. J. (1996). Synthetic peptides corresponding to alpha-lactalbumin and beta-lactoglobulin sequences with angiotensin-I-converting enzyme inhibitory activity. Biological chemistry Hoppe-Seyler, 377(4), 259–260. https://doi.org/10.1515/bchm3.1996.377.4.259
Murota, I., Taguchi, S., Sato, N., Park, E. Y., Nakamura, Y., & Sato, K. (2014). Identification of antihyperuricemic peptides in the proteolytic digest of shark cartilage water extract using in vivo activity-guided fractionation. Journal of agricultural and food chemistry, 62(11), 2392–2397. https://doi.org/10.1021/jf405504u
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. https://doi.org/10.1016/j.foodchem.2013.02.115
Onifade, A. A., A1-Sane, N. A., Ai-Musallam, A. A., & Al-Zarban, S. (1998). a review: potentials for biotechnological applications of keratin-degrading microorganisms and their enzymes for nutritional improvement of feathers and other keratins as livestock feed resources. Bioresource Technology (Vol. 66). https://doi.org/10.1016/S0960-8524(98)00033-9
Pourjavaheri, F., Ostovar Pour, S., Jones, O. A. H., Smooker, P. M., Brkljača, R., Sherkat, F., Blanch, E. W., Gupta, A., & Shanks, R. A. (2019). Extraction of keratin from waste chicken feathers using sodium sulfide and L-cysteine. Process Biochemistry, 82, 205–214. https://doi.org/10.1016/j.procbio.2019.04.010
Presland, R. B., Gregg, K., Molloy, P. L., Morris, C. P., Crocker, L. A., & Rogers, G. E. (1989). Avian keratin genes. I. A molecular analysis of the structure and expression of a group of feather keratin genes. Journal of molecular biology, 209(4), 549–559. https://doi.org/10.1016/0022-2836(89)90593-7
Rahman, M. M., & Lamsal, B. P. (2021). Ultrasound-assisted extraction and modification of plant-based proteins: Impact on physicochemical, functional, and nutritional properties. Comprehensive Reviews in Food Science and Food Safety (Vol. 20, Issue 2, pp. 1457–1480). Blackwell Publishing Inc. https://doi.org/10.1111/1541-4337.12709
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, 1721(1-3), 89–97. https://doi.org/10.1016/j.bbagen.2004.10.005
Rouse, J. G., & Van Dyke, M. E. (2010). A review of keratin-based biomaterials for biomedical applications. Materials, 3(2), 999–1014. https://doi.org/10.3390/ma3020999
Sharma, S., Gupta, A., Chik, S. M. S. T., Gek, K. C., Podde, P. K., Thraisingam, J., & Subramaniam, M. (2016, December). Extraction and characterization of keratin from chicken feather waste biomass: a study. In Proceedings of the national conference for postgraduate research (NCON-PGR 2016), Universiti Malaysia Pahang (UMP), Pekan (pp. 693-699). https://www.researchgate.net/publication/311843895
Sinkiewicz, I., Śliwińska, A., Staroszczyk, H., & Kołodziejska, I. (2017). Alternative Methods of Preparation of Soluble Keratin from Chicken Feathers. Waste and Biomass Valorization, 8(4), 1043–1048. https://doi.org/10.1007/s12649-016-9678-y
Soffer R. L. (1973). Peptide acceptors in the leucine, phenylalanine transfer reaction. The Journal of biological chemistry, 248(24), 8424–8428. https://doi.org/10.1016/S0021-9258(19)43150-5
Sonklin, C., Alashi, A. M., Laohakunjit, N., & Aluko, R. E. (2021). Functional Characterization of Mung Bean Meal Protein-Derived Antioxidant Peptides. Molecules, 26(6), 1515. https://doi.org/10.3390/molecules26061515
Suetsuna, K., Ukeda, H., & Ochi, H. (2000). Isolation and characterization of free radical scavenging activities peptides derived from casein. The Journal of nutritional biochemistry, 11(3), 128–131. https://doi.org/10.1016/s0955-2863(99)00083-2
Tang, H., Finn, R. D., & Thomas, P. D. (2019). TreeGrafter: phylogenetic tree-based annotation of proteins with Gene Ontology terms and other annotations. Bioinformatics (Oxford, England), 35(3), 518–520. https://doi.org/10.1093/bioinformatics/bty625
Tesfaye, T., Sithole, B., & Ramjugernath, D. (2017). Valorisation of chicken feathers: a review on recycling and recovery route—current status and future prospects. Clean Technologies and Environmental Policy, 19(10), 2363-2378. https://doi.org/10.1007/s10098-017-1443-9
Van Platerink, C. J., Janssen, H. G., & 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. https://doi.org/10.1007/s00216-008-1990-3

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