{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,18]],"date-time":"2026-09-18T09:07:54Z","timestamp":1789722474624,"version":"4.0.1"},"reference-count":62,"publisher":"MDPI AG","issue":"19","license":[{"start":{"date-parts":[[2025,9,28]],"date-time":"2025-09-28T00:00:00Z","timestamp":1759017600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100012166","name":"National Key R&D Program of China","doi-asserted-by":"publisher","award":["2024YFD2401805"],"award-info":[{"award-number":["2024YFD2401805"]}],"id":[{"id":"10.13039\/501100012166","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"crossref","award":["42076120"],"award-info":[{"award-number":["42076120"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"crossref","award":["41676129"],"award-info":[{"award-number":["41676129"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"crossref"}]},{"name":"Innovation Research and Development Special Funds of the Municipality-province-ministry Co-constructed","award":["GJZX-HYSW-2024-01"],"award-info":[{"award-number":["GJZX-HYSW-2024-01"]}]},{"name":"Special Fund for Promoting High Quality Development of Marine and Fisheries Industry in Fujian Province","award":["FJHYF-L-2023-24"],"award-info":[{"award-number":["FJHYF-L-2023-24"]}]},{"name":"Marine and Fisheries Development Special Fund Youth Science and Technology Innovation Project","award":["23YYST080QCA19"],"award-info":[{"award-number":["23YYST080QCA19"]}]}],"content-domain":{"domain":["www.mdpi.com"],"crossmark-restriction":true},"short-container-title":["Foods"],"abstract":"<jats:p>Fish-derived collagen can reduce the risk of disease transmission and has no religious or cultural restrictions. However, it has limited applications due to its poor thermal stability. In this study, black carp swim bladder collagen (BBC), classified as a type I collagen, was extracted. Amino acid composition analysis revealed that BBC had a higher proline hydroxylation rate of 39.57%. Fourier transform infrared spectroscopy revealed that BBC exhibited a complete triple-helix structure. The fractional viscosity curve and differential scanning calorimetry curves revealed that the thermal denaturation temperature (Td) and the melting temperature (Tm) were 30.85 \u00b0C and 107.19 \u00b0C, respectively. The dynamic rheological analysis showed that as the concentration increased from 5 mg\/mL to 20 mg\/mL at 0.01 Hz, the storage modulus increased from 0.979 Pa to 84.2 Pa. When the temperature exceeded the Td, the BBC solution exhibited viscous behaviour as the frequency increased. The steady-shear analysis showed that the BBC was a shear-thinning fluid. Functional properties analysis revealed that BBC exhibited better emulsification properties, foaming properties, water absorption capacity and oil absorption capacity than land-derived collagen, making it suitable for emulsifiers, bubbling beverages, and frozen meat preservation. Additionally, BBC promoted the growth of MT3C3-E1 cells and maintained the normal morphology of the cells. These results showed that BBC is a promising substitute for terrestrial collagen in functional foods, cosmetics, and biofunctional materials.<\/jats:p>","DOI":"10.3390\/foods14193359","type":"journal-article","created":{"date-parts":[[2025,9,29]],"date-time":"2025-09-29T12:59:46Z","timestamp":1759150786000},"page":"3359","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Thermally Stable Collagen from Black Carp (Mylopharyngodon piceus) Swim Bladder: Preparation, Structure, Rheological, and Functional Properties"],"prefix":"10.3390","volume":"14","author":[{"given":"Lichi","family":"Wei","sequence":"first","affiliation":[{"name":"Fisheries College, Jimei University, Xiamen 361021, China"},{"name":"Technical Innovation Center for Utilization of Marine Biological Resources, Third Institute of Oceanography, Ministry of Natural Resources, Xiamen 361005, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yushuang","family":"Li","sequence":"additional","affiliation":[{"name":"Technical Innovation Center for Utilization of Marine Biological Resources, Third Institute of Oceanography, Ministry of Natural Resources, Xiamen 361005, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cong","family":"Ke","sequence":"additional","affiliation":[{"name":"Technical Innovation Center for Utilization of Marine Biological Resources, Third Institute of Oceanography, Ministry of Natural Resources, Xiamen 361005, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0632-1609","authenticated-orcid":false,"given":"Junde","family":"Chen","sequence":"additional","affiliation":[{"name":"Technical Innovation Center for Utilization of Marine Biological Resources, Third Institute of Oceanography, Ministry of Natural Resources, Xiamen 361005, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jing","family":"Zhang","sequence":"additional","affiliation":[{"name":"Fisheries College, Jimei University, Xiamen 361021, China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,9,28]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Laasri, I., Bakkali, M., Mejias, L., and Laglaoui, A. (2023). Marine collagen: Unveiling the blue resource-extraction techniques and multifaceted applications. Int. J. Biol. Macromol., 253.","DOI":"10.1016\/j.ijbiomac.2023.127253"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"e25194","DOI":"10.1016\/j.heliyon.2024.e25194","article-title":"Development of films based on chitosan, gelatin and collagen extracted from bocachico scales (Prochilodus magdalenae)","volume":"10","year":"2024","journal-title":"Heliyon"},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Zheng, Y., Li, Y.S., Ke, C., Gao, X.Y., Liu, Z.Y., and Chen, J.D. (2024). Comparison of structural and physicochemical characteristics of skin collagen from chum salmon (cold-water fish) and Nile tilapia (warm-water fish). Foods, 13.","DOI":"10.3390\/foods13081213"},{"key":"ref_4","doi-asserted-by":"crossref","unstructured":"Jelsma, T., Wijnker, J.J., Smid, B., Verheij, E., Van der Poel, W.H.M., and Wisselink, H.J. (2019). Salt inactivation of classical swine fever virus and African swine fever virus in porcine intestines confirms the existing in vitro casings model. Vet. Microbiol., 238.","DOI":"10.1016\/j.vetmic.2019.108424"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"616","DOI":"10.1016\/j.foodchem.2007.11.017","article-title":"Isolation and characterisation of collagens from the skin, scale and bone of deep-sea redfish (Sebastes mentella)","volume":"108","author":"Wang","year":"2008","journal-title":"Food Chem."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/j.procbio.2017.08.003","article-title":"Characterization of pacific cod (Gadus macrocephalus) skin collagen and fabrication of collagen sponge as a good biocompatible biomedical material","volume":"63","author":"Sun","year":"2017","journal-title":"Process Biochem."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"138723","DOI":"10.1016\/j.molstruc.2024.138723","article-title":"Preliminarily revealing rheological behaviors of mesoscale collagen fibrils in suspension","volume":"1311","author":"Li","year":"2024","journal-title":"J. Mol. Struct."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"104402","DOI":"10.1016\/j.arabjc.2022.104402","article-title":"Double-spotted pufferfish (Takifugu bimaculatus) skin collagen: Preparation, structure, cytocompatibility, rheological, and functional properties","volume":"16","author":"Gao","year":"2023","journal-title":"Arab. J. Chem."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"100746","DOI":"10.1016\/j.focha.2024.100746","article-title":"Characterization of acid-soluble collagen (ASC) derived from walleye pollock and silver carp skin and comparison them with the collagen from pig and duck skin","volume":"4","author":"He","year":"2024","journal-title":"Food Chem. Adv."},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Guan, Y.X., He, J.L., Chen, J.D., Li, Y.S., Zhang, X.K., Zheng, Y., and Jia, L.Y. (2022). Valorization of fish processing by-products: Microstructural, rheological, functional, and properties of silver carp skin type I collagen. Foods, 11.","DOI":"10.3390\/foods11192985"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"112518","DOI":"10.1016\/j.lwt.2021.112518","article-title":"Structural, functional, rheological, and biological properties of the swim bladder collagen extracted from grass carp (Ctenopharyngodon idella)","volume":"153","author":"Li","year":"2022","journal-title":"LWT-Food Sci. Technol."},{"key":"ref_12","doi-asserted-by":"crossref","unstructured":"Yu, L.X., Lin, J.Q., Chen, D.Q., Duan, X.B., Peng, Q.D., and Liu, S.P. (2018). Ecological flow assessment to improve the spawning habitat for the four major species of carp of the yangtze river: A study on habitat suitability based on ultrasonic telemetry. Water, 10.","DOI":"10.3390\/w10050600"},{"key":"ref_13","first-page":"102764","article-title":"Effects of feeding pattern on growth, immunity and intestinal flora of GIFT tilapia (Oreochromis niloticus) and largemouth bass (Micropterus salmoides)","volume":"42","author":"Wang","year":"2025","journal-title":"Aquacult. Rep."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/j.lwt.2017.11.060","article-title":"Quality parameters of black carp (Mylopharyngodon piceus) raised in lotic and lentic freshwater systems","volume":"90","author":"Harimana","year":"2018","journal-title":"LWT-Food Sci. Technol."},{"key":"ref_15","unstructured":"Ministry of Agriculture and Rual Affairs of the People\u2019s China (2024). China Fishery Statistical Yearbook, China Agriculture Press."},{"key":"ref_16","doi-asserted-by":"crossref","unstructured":"Chen, J.D., Wang, G.Y., and Li, Y.S. (2021). Preparation and characterization of thermally stable collagens from the scales of lizardfish (Synodus macrops). Mar. Drugs, 19.","DOI":"10.3390\/md19110597"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"264","DOI":"10.1016\/j.foodchem.2014.01.076","article-title":"Characteristics of collagens from the swim bladders of yellowfin tuna (Thunnus albacares)","volume":"155","author":"Kaewdang","year":"2014","journal-title":"Food Chem."},{"key":"ref_18","first-page":"100984","article-title":"Physicochemical and biological properties of collagens obtained from tuna tendon by using the ultrasound-assisted extraction","volume":"15","author":"Chanmangkang","year":"2024","journal-title":"J. Sci. Food Agric."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1016\/j.foodchem.2004.10.026","article-title":"Isolation and characterisation of acid and pepsin-solubilised collagens from the skin of brownstripe red snapper (Lutjanus vitta)","volume":"93","author":"Jongjareonrak","year":"2005","journal-title":"Food Chem."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"105875","DOI":"10.1016\/j.foodhyd.2020.105875","article-title":"Fabrication and characterization of acid soluble collagen stabilized Pickering emulsions","volume":"106","author":"Zhu","year":"2020","journal-title":"Food Hydrocoll."},{"key":"ref_21","doi-asserted-by":"crossref","unstructured":"Ma, H.Z., Zhang, L.N., Niu, X.R., Zhang, Y.N., Yang, X.Y., and Li, L. (2025). Soy protein-gellan gum noncovalent complexes stabilized emulsion: Effect of heating and pH on emulsion stability. Int. J. Biol. Macromol., 301.","DOI":"10.1016\/j.ijbiomac.2025.140067"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"592","DOI":"10.1016\/j.jfoodeng.2006.02.018","article-title":"Functional properties of rice bran protein concentrates","volume":"79","author":"Chandi","year":"2007","journal-title":"J. Food Eng."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"1441","DOI":"10.1016\/j.foodchem.2012.02.032","article-title":"Extraction and characterisation of pepsin-solubilised collagen from fins, scales, skins, bones and swim bladders of bighead carp (Hypophthalmichthys nobilis)","volume":"133","author":"Liu","year":"2012","journal-title":"Food Chem."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"101593","DOI":"10.1016\/j.tice.2021.101593","article-title":"Comparison of collagen characteristic from the skin and swim bladder of gulf corvina (Cynoscion othonopterus)","volume":"72","year":"2021","journal-title":"Tissue Cell"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"128139","DOI":"10.1016\/j.foodchem.2020.128139","article-title":"Characterization and comparison of collagen extracted from the skin of the nile tilapia by fermentation and chemical pretreatment","volume":"340","author":"Song","year":"2021","journal-title":"Food Chem."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"130061","DOI":"10.1016\/j.foodchem.2021.130061","article-title":"Collagens made from giant salamander (Andrias davidianus) skin and their odorants","volume":"361","author":"Chen","year":"2021","journal-title":"Food Chem."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"1507","DOI":"10.1016\/j.foodhyd.2011.02.011","article-title":"Isolation and characterization of acid and pepsin-solubilized collagens from the skin of balloon fish (Diodon holocanthus)","volume":"25","author":"Huang","year":"2011","journal-title":"Food Hydrocoll."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"107748","DOI":"10.1016\/j.foodhyd.2022.107748","article-title":"Collagen and its derivatives: From structure and properties to their applications in food industry","volume":"131","author":"Tang","year":"2022","journal-title":"Food Hydrocoll."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"106129","DOI":"10.1016\/j.ultsonch.2022.106129","article-title":"Impact of ultrasound on extractability of native collagen from tuna by-product and its ultrastructure and physicochemical attributes","volume":"89","author":"Pezeshk","year":"2022","journal-title":"Ultrason. Sonochem."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"804","DOI":"10.1016\/j.foodres.2015.07.018","article-title":"Comparative study on characteristics and in vitro fibril formation ability of acid and pepsin soluble collagen from the skin of catla (Catla catla) and rohu (Labeo rohita)","volume":"76","author":"Kumar","year":"2015","journal-title":"Food Res. Int."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1016\/j.ijbiomac.2017.09.022","article-title":"Comparison of characteristics and fibril-forming ability of skin collagen from barramundi (Lates calcarifer) and tilapia (Oreochromis niloticus)","volume":"107","author":"Liao","year":"2018","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"100454","DOI":"10.1016\/j.scp.2021.100454","article-title":"Extraction, characterization and biocompatibility evaluation of collagen from silver carp (Hypophthalmichthys molitrix) skin by-product","volume":"22","author":"Faralizadeh","year":"2021","journal-title":"Sustain. Chem. Pharm."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"2435","DOI":"10.1016\/j.foodchem.2012.11.136","article-title":"Comparative Study on Molecular characteristics of acid soluble collagens from skin and swim bladder of seabass (Lates calcarifer)","volume":"138","author":"Sinthusamran","year":"2013","journal-title":"Food Chem."},{"key":"ref_34","doi-asserted-by":"crossref","unstructured":"Stani, C., Vaccari, L., Mitri, E., and Birarda, G. (2020). FTIR investigation of the secondary structure of type I collagen: New insight into the amide III band. Spectrochim. Acta A Mol. Biomol. Spectrosc., 229.","DOI":"10.1016\/j.saa.2019.118006"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"106576","DOI":"10.1016\/j.foodhyd.2020.106576","article-title":"Study of the thermodynamics and conformational changes of collagen molecules upon self-assembly","volume":"114","author":"Zhu","year":"2020","journal-title":"Food Hydrocoll."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"107111","DOI":"10.1016\/j.foodhyd.2021.107111","article-title":"Compositional and structural characteristics of pepsin-soluble type I collagen from the scales of red drum fish, Sciaenops ocellatus","volume":"123","author":"Chen","year":"2022","journal-title":"Food Hydrocoll."},{"key":"ref_37","doi-asserted-by":"crossref","unstructured":"Chen, J.D., Li, J.Y., Li, Z.B., Yi, R.Z., Shi, S.J., Wu, K.Y., Li, Y.S., and Wu, S.J. (2019). Physicochemical and functional properties of type I collagens in red stingray (Dasyatis akajei) skin. Mar. Drugs, 17.","DOI":"10.3390\/md17100558"},{"key":"ref_38","doi-asserted-by":"crossref","unstructured":"Wu, K.Y., Li, Y.S., and Chen, J.D. (2024). Effect of pH on the structure, functional properties and rheological properties of collagen from greenfin horse-faced filefish (Thamnaconus septentrionalis) skin. Mar. Drugs, 22.","DOI":"10.3390\/md22010045"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"1581","DOI":"10.1016\/j.foodchem.2007.10.027","article-title":"Characterization of acid-soluble collagen from the skin of walleye pollock (Theragra chalcogramma)","volume":"107","author":"Yan","year":"2008","journal-title":"Food Chem."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"1592","DOI":"10.1016\/j.procbio.2013.07.011","article-title":"Isolation and characterization of thermostable collagen from the marine eel-fish (Evenchelys macrura)","volume":"48","author":"Veeruraj","year":"2013","journal-title":"Process Biochem."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"665","DOI":"10.5851\/kosfa.2016.36.5.665","article-title":"Isolation and characterization of pepsin-soluble collagens from bones, skins, and tendons in duck feet","volume":"36","author":"Kim","year":"2016","journal-title":"Korean J. Food Sci. Anim. Resour."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"8046","DOI":"10.1021\/jf051040v","article-title":"Conformational study of globulin from common buckwheat (Fagopyrum esculentum Moench) by fourier transform infrared spectroscopy and differential scanning calorimetry","volume":"53","author":"Choi","year":"2005","journal-title":"J. Agric. Food Chem."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"244","DOI":"10.1016\/j.foodchem.2005.06.053","article-title":"Comparison of physical\u2013chemical properties of type I collagen from different species","volume":"99","author":"Lin","year":"2006","journal-title":"Food Chem."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"142972","DOI":"10.1016\/j.molstruc.2025.142972","article-title":"Physicochemical studies of asarylaldehyde crosslinked type-I collagen fibrils","volume":"1344","author":"Banerjee","year":"2025","journal-title":"J. Mol. Struct."},{"key":"ref_45","doi-asserted-by":"crossref","unstructured":"Salvatore, L., Russo, F., Natali, M.L., Rajabimashhadi, Z., Bagheri, S., Mele, C., Lionetto, F., Sannino, A., and Gallo, N. (2024). On the effect of pepsin incubation on type I collagen from horse tendon: Fine tuning of its physico-chemical and rheological properties. Int. J. Biol. Macromol., 256.","DOI":"10.1016\/j.ijbiomac.2023.128489"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"110347","DOI":"10.1016\/j.foodhyd.2024.110347","article-title":"Rheological properties of the swim bladder colloid from Atlantic cod (Gadus morhua) and its digestive characteristics","volume":"156","author":"Zhang","year":"2024","journal-title":"Food Hydrocoll."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"145920","DOI":"10.1016\/j.foodchem.2025.145920","article-title":"Colloidal structural characteristics and variation patterns of chicken skin gelatin during thermal processing","volume":"493","author":"Xu","year":"2025","journal-title":"Food Chem."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"140266","DOI":"10.1016\/j.foodchem.2024.140266","article-title":"Effect of psyllium husk powder on the gelation behavior, microstructure, and intermolecular interactions in myofibrillar protein gels from Andrias davidianus","volume":"458","author":"Huang","year":"2024","journal-title":"Food Chem."},{"key":"ref_49","doi-asserted-by":"crossref","unstructured":"Sozeri Atik, S., Ozt\u00fcrk, H.I., and Ak\u0131n, N. (2024). Perspectives on the yogurt rheology. Int. J. Biol. Macromol., 263.","DOI":"10.1016\/j.ijbiomac.2024.130428"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1007\/s13367-015-0028-6","article-title":"Rheological behavior of acylated pepsin-solubilized collagen solutions: Effects of concentration","volume":"27","author":"Li","year":"2015","journal-title":"Korea-Aust. Rheol. J."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1016\/j.foodhyd.2014.07.024","article-title":"Structural and functional characterization of kidney bean and field pea protein isolates: A comparative study","volume":"43","author":"Shevkani","year":"2015","journal-title":"Food Hydrocoll."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"125742","DOI":"10.1016\/j.ijpharm.2025.125742","article-title":"Application of rheology to hot melt extrusion: Theory and practice","volume":"680","author":"Wang","year":"2025","journal-title":"Int. J. Pharm."},{"key":"ref_53","doi-asserted-by":"crossref","unstructured":"Mollaheydaralimoazzen, M., Sheikholeslam, M., Poursamar, S.L., Farzan, M., Farzan, M., and Rafienia, M. (2025). 3D-printing of shear-thinning and self-healing gelatin\/starch\/halloysite-nanotube hydrogels for soft tissue engineering: An in vitro and in vivo assessment. Int. J. Biol. Macromol., 315.","DOI":"10.1016\/j.ijbiomac.2025.144502"},{"key":"ref_54","doi-asserted-by":"crossref","unstructured":"Ahmad, M.I., Li, Y.H., Pan, J.F., Liu, F., Dai, H.J., Fu, Y., Huang, T., Farooq, S., and Zhang, H. (2024). Collagen and gelatin: Structure, properties, and applications in food industry. Int. J. Biol. Macromol., 254.","DOI":"10.1016\/j.ijbiomac.2023.128037"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"29555","DOI":"10.1039\/D0RA03731A","article-title":"Structural, physicochemical and functional properties of semen ziziphi spinosae protein","volume":"10","author":"Zhang","year":"2020","journal-title":"RSC Adv."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"111967","DOI":"10.1016\/j.foodres.2022.111967","article-title":"Collagen extracted from rabbit: Meat and by-products: Isolation and physicochemical assessment","volume":"162","author":"Toniasso","year":"2022","journal-title":"Food Res. Int."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"852","DOI":"10.1016\/j.foodchem.2009.01.011","article-title":"Functional properties of protein concentrates and isolates produced from cashew (Anacardium occidentale L.) nut","volume":"115","author":"Ogunwolu","year":"2009","journal-title":"Food Chem."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"1733","DOI":"10.1007\/s11947-018-2138-x","article-title":"Structural, functional, and sensorial properties of protein isolate produced from salmon, cod, and herring by-products","volume":"11","author":"Abdollahi","year":"2018","journal-title":"Food Bioprocess Technol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"1602","DOI":"10.1016\/j.ijbiomac.2017.03.011","article-title":"Effect of ultrasound assisted extraction on the physicochemical and functional properties of collagen from soft-shelled turtle calipash","volume":"105","author":"Zou","year":"2017","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/j.fbio.2018.03.003","article-title":"Optimization of collagen extraction from chicken feet by papain hydrolysis and synthesis of chicken feet collagen based biopolymeric fibres","volume":"23","author":"Dhakal","year":"2018","journal-title":"Food Biosci."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"394","DOI":"10.1016\/j.foodhyd.2018.12.028","article-title":"Effects of pretreatments on the structure and functional properties of okara protein","volume":"90","author":"Tao","year":"2019","journal-title":"Food Hydrocoll."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"246","DOI":"10.17221\/128\/2018-CJFS","article-title":"The effect of drying temperature on the properties of gelatin from carps (Cyprinus carpio) skin","volume":"37","author":"Tkaczewska","year":"2019","journal-title":"Czech J. Food Sci."}],"container-title":["Foods"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2304-8158\/14\/19\/3359\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,9,30]],"date-time":"2025-09-30T04:15:27Z","timestamp":1759205727000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2304-8158\/14\/19\/3359"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,9,28]]},"references-count":62,"journal-issue":{"issue":"19","published-online":{"date-parts":[[2025,10]]}},"alternative-id":["foods14193359"],"URL":"https:\/\/doi.org\/10.3390\/foods14193359","relation":{},"ISSN":["2304-8158"],"issn-type":[{"value":"2304-8158","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,9,28]]}}}