medigraphic.com
ISSN 1561-3011 (Electronic)

2022, Number 1

<< Back Next >>

Rev Cubana Invest Bioméd 2022; 41 (1)

Obtaining collagen from animal tissues by-products of the meat industry

Carvajal OJ, Villegas SJL, Prohías MJ, Figueroa CR, Serrano RY, Valdés MA, Gómez GR, Ameneiros MJM, Sandino BJW

Language: Spanish
References: 34
Page: 34
PDF size: 390.49 Kb.


ABSTRACT

Introduction: Collagen is the most abundant structural protein in the human body, for this reason it is widely used in tissue engineering. When good mechanical performance of the final product is required, an attempt is made to maintain the highest long fiber content. For its characterization, techniques such as electrophoresis and infrared spectroscopy by Fourier transform are used, which allow to determine the purity and protein content of the same.
Objectives: To characterize the collagen obtained from chicken and pork for later use in cardiovascular tissue engineering.
Methods: The dissolution of the collagen source was performed in 5% acetic acid. Collagen was characterized using electrophoresis tests using the SDS-PAGE method and Fourier transform infrared spectrometry using the reflection analysis mode with the SPECAC ATR accessory and range from 600 to 4000 1/cm, to determine purity.
Results: As a result of the work, type I and III collagens are obtained in the mixture of legs plus chicken crest. Also type I collagen in the samples of legs, chicken crests and pig skin.
Conclusions: It was concluded that the raw materials used may be sources of collagen usable for the regeneration of cardiovascular tissue.


REFERENCES

  1. Paredes Puerto A., Camacho Villegas T., Vallejo Cardona A., Esquivel Solís H., Colágenas Recombinantes para Andamios de Ingeniería de Tejidos. Revista Mexicana De Ingeniería. 2017;38(1):103-114. Disponible en: https://dx.doi.org/10.17488/RMIB.38.1.7

  2. Liu DC, Lin YK and Chen MT. Optimum condition of extracting collagen from chicken feet and its characteristics, Asian-Aust J Anim Sci. 2001;14(11):1638-44. DOI: https://10.5713/ajas.2001.1638 8

  3. Copes F, Pien N, Van Vlierberghe S, Boccafoschi F and Mantovani D. Collagen-Based Tissue Engineering Strategies for Vascular Medicine. Front. Bioeng. Biotechnol. (2019) 7:166. Disponible en: DOI: https://10.3389/fbioe.2019.00166

  4. Kazuhisa M. Skin-Moisturizing Effect of Collagen Peptides Taking Orally. J Nutr Food Sci. 2018;8(2):682-90. DOI: https://10.4172/2155-9600.1000682

  5. Robert J, Hartmann DJ, Sengel P. Production of fibronectin and collagen types I and III by chick embryo dermal cells cultured on extracellular matrix substrates. Int. J. Dev. Biol. 1989; 33:267-275.

  6. Wickham A. Multifunctional Biomimetic Scaffolds Tailored for Cardiac Regeneration. 1era ed, Ed. LiU-Tryck. 2015. Consultado en diciembre de 2019. Disponible en: https://www.diva-portal.org/smash/get/diva2:848329/FULLTEXT01.pdf,

  7. Silva Tiago H, Moreira Silva J, Marques AL, Domingues A, Bayon Y and Reis Rui L Marine Origin Collagens and Its Potential Applications. Mar. Drugs. 2014;12:5881-5901. DOI: https://10.3390/md12125881

  8. Belbachir K, Noreen R, Gouspillou G, Petibois C. Collagen types analysis and differentiation by FTIR spectroscopy. Anal Bioanal Chem. 2009;395:829-837. DOI: https://10.1007/s00216-009-3019-y

  9. Cantero Belinchón P, Palacios Lasa M, Urdanoz Izco B. Procedimiento de obtención de colágeno a partir de la piel de un animal- Google Patents”, Publication 2013-01-03, PCT/ES2011/070467, WO2013001103A1. Disponible en: https://patentados.com/2013/obtencion-de-colageno-a-partir

  10. Gómez González R, Figueroa Hernández C, Ameneiros Martínez JM, Prohías J. Obtención de una matriz de colágeno de origen porcino, 19 CCIA CUJAE. 2018. Disponible en: https://www.researchgate.net/publication/329488378

  11. Baburina MI, Ivankin AN, Stanovova IA. Chemical and biotechnological processing of collagen-containing raw materials into functional components of feed suitable for production of high-quality meat from farm animals; 2017. 59th International Meat Industry Conference MEATCON 2017, IOP Conf. Ser.: Earth Environ. Sci.85 012037. DOI: https://10.1088/1755-1315/85/1/012037

  12. Castro Vargas CD. Obtención de colágeno a partir de crestas de pollos. Tesis de grado. Universidad Industrial de Santander; 2012. Disponible en: https://docplayer.es/30123336-Obtencion-de-colageno-a-partir-de-crestas-de-pollos.html

  13. Mohd Shakrie PA, Mohamed Ibrahim N, Syed Ibrahim Mohd I, Shaik N, Jasamai M, Kok Wai L, Nur Murnisa M, Ahmad Fuad Sh. Physicochemical Evaluation and Spectroscopic Characterisation of Gelatine from Shank and Toes of Gallus gallus domesticus., Sains Malaysiana. 2016;45(3):435-449. Disponible en: www.researchgate.net/publication/291330340_Physicochemical_evaluation_and_spectroscopic_characterisation_of_gelatine_from_shank_and_toes_of_Gallus_gallus_domesticus,

  14. Dhiya Mokhtar N, Abdul Wahab W, Ashima Hamdan N, Abdul Hadi H, Muhamad Shafiq AH, Muhamad Bunnori N. Extraction Optimization and Characterization of Collagen from Chicken (Gallus gallus domesticus) Feet. 5th International Conference on Chemical, Agricultural, Biological and Environmental Sciences (CAFES-17) Kyoto (Japan) April 18-19; 2017- Disponible en: http://irep.iium.edu.my/56704/12/56704_Extraction%20Optimization%20and%20Characterization%20of%20Collagen.pdf

  15. Suparno O, Prasetyo N B. Isolation of collagen from chicken feet with hydro-extraction method and its physico-chemical characterisation, ICDALC 2018 IOP Conf. Series: Earth and Environmental Science 335. 2019;012018 IOP. DOI: https://10.1088/1755-1315/335/1/0120181

  16. Chia Wei L, Loughran M, Tsung Yu T, Shuo Wen T. Evaluation of convenient extraction of chicken skin collagen using organic acid and pepsin combination. J. Chin. Soc. Anim. Sic. 2013;42(1):27-38. Disponible en: https://docplayer.net/57689804-Evaluation-of-convenient-extraction-of-chicken-skin-collagen-using-organic-acid-and-pepsin-combination.html

  17. Huda N, Seow EK, Normawati MN, Nik Aisyah NM. Preliminary Study on Physicochemical Properties of Duck Feet Collagen. International Journal of Poultry Science. 2013;12(10):615-621. Disponible en: https://www.researchgate.net/publication/272964562_Preliminary_Study_on_Physicochemical_Properties_of_Duck_Feet_Collagen

  18. Braz Da Silva Araújo I. , Alves Bezerra T. K., Silva Do Nascimento E., De Almeida Gadelha C.A., Santi-Gadelha T., Suely Madruga M., Optimal conditions for obtaining collagen from chicken feet and its characterization , Food Sci. Technol, Campinas, (2018) 38(1):167-173, disponible en: https://doi.org/10.1590/fst.27517

  19. Fiodorovich Gorlov I, Ivanovich Titov E,Viacheslavovich Semenov G, Ivanovna Slozhenkina M, Yurievich Sokolov A, Saferbegovich Omarov R, Ivanovich Goncharov A, Yurievna Zlobina E, Viktorovna Litvinova E, Vladimirovna Karpenko E. Collagen from porcine skin: a method of extraction and structural properties , International Journal of Food Properties. 2018;21(1):1031-1042. DOI: https://10.1080/10942912.2018.1466324

  20. Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227:680-685.

  21. Xuan Ky, P, Bao Vy P, Viet Ha D, Ho Khanh Hy L, Thu Hong N, Thi Thiet D, Phuong Anh N. Investigation of protein patterns and antioxidant activity of collagen hydrolysates from skin of fanbellied leather jacket monacanthus chinensis by various enzymes. Journal of Marine Science and Technology. 2018;18(4A):141-150. DOI: https://10.15625/1859-3097/18/4A/13642

  22. Wu J, Guo X, Liu H, Chen L. Isolation and Comparative Study on the Characterization of Guanidine Hydrochloride Soluble Collagen and Pepsin Soluble Collagen from the Body of Surf Clam Shell (Coelomactra antiquata). Foods. 2019;8:11. DOI: https://10.3390/foods8010011

  23. Ki Hong J, Yoon Seon H, Young Boong K, Yun Sang Ch, Byoung Mok K, Dong Wook K, Aera J., Jinyoung Ch. Quality Characteristics of Pork Skin Collagen with Enzyme Treatments, Korean J. Food Nutr. 2016;29(5):760-766. Disponible en: http://dx.doi.org/10.9799/ksfan.2016.29.5.760

  24. Knight KR, Mccann JJ, Vanderkolk CA, Coe SA, Mcc O’brien B. Microsurgery The redistribution of collagen in expanded pig skin. British Journal of Plastic Surgery. 1990; 43:565-570. Disponible en: https://www.jprasurg.com/article/0007-1226(90)90121-F/pdf

  25. Yang H, Shu Z. The extraction of collagen protein from pigskin, J. Chem. Pharm. Res. 2014;6(2):683-687. Disponible en http://www.jocpr.com/articles/the-extraction-of-collagen-protein-from-pigskin.pdf

  26. Torres Arreola W, Pacheco Aguilar R, Sotelo Mundo RR, Rouzaud Sández O, Ezquerra Brauer JM. Caracterización parcial del colágeno extraído a partir del manto, aleta y tentáculos de calamar gigante (dosidicusgigas) CYTA. Journal of Food. 2008;6(2):101-108. DOI: https://10.1080/11358120809487634

  27. Gorgieva S, Kokol V. Collagen - vs. Gelatine-Based Biomaterials and Their Biocompatibility: Review and Perspectives. In: Biomaterials Applications for Nanomedicine. Edited by Prof. Rosario Pignatello. Publisher InTech; 2011. Disponible en: https://books.google.com.cu/books?hl=es&lr=&id=b8ePDwAAQBAJ&oi=fnd&pg=PR11&dq=Biomaterials+Applications+for+Nanomedicine&ots=I2_5FVCENW&sig=METtzkMdv6AXjUxQiFdOVOXGcKc&redir_esc=y#v=onepage&q=Biomaterials%20Applications%20for%20Nanomedicine&f=false

  28. Tanaka T, Takahashi K, Tsubaki K, Hirata M, Yamamoto K, Biswas A, Moriyama T, Kawamura Y. Isolation and characterization of acid soluble bluefin tuna (Thunnus orientalis) skin collagen. Fisheries and Aquatic Sciences. 2018;21:7. DOI: https://10.1186/s41240-018-0084-1

  29. Gaurav KP, Suresh PV. Comparative assessment of physic-chemical characteristics and fibril formation capacity of thermostable carp scales collagen, Materials Science and engineering. 2017;70:32-40. DOI: https://10.1016/j.msec.2016.08.047

  30. Meyer M. Processing of collagen based biomaterials and the resulting materials properties, Meyer BioMed Eng OnLine (2019) 18:24, 74pages, https://doi.org/10.1186/s12938-019-0647-0

  31. MERCK. Sodium chloride for analysis EMSURE® ACS ISO Reag. Ph Eur. Disponible en: https://www.merckmillipore.com/INTL/en/product/Sodium-chloride,MDA_CHEM-106404?ReferrerURL=https%3A%2F%2Fwww.google.com%2F#anchor_Specifications

  32. PanReac AppliChem. Ácido Acético glacial (Reag. USP, Ph. Eur.) para análisis, ACS, ISO, https://www.itwreagents.com/iberia/es/product/ga-para-analisis-acs-iso/%C3%81cido+ac%C3%A9tico+glacial+%28reag.+usp%2C+ph.+eur.%29+para+an%C3%A1lisis%2C+acs%2C+iso/131008

  33. Cliche S, Amiot J, Avezard C, Garie´py C. Extraction and Characterization of Collagen with or Without Telopeptides from Chicken Skin, Poultry Science. 2003;82:503-509. disponible en: https://www.sciencedirect.com/science/article/pii/S003257911944978X?via%3Dihub

  34. De Campos Vidal B, Mello ML. Collagen type I amide I band infrared spectroscopy, Micron. 2011;42:283-289. DOI: https://10.106/j.micron.2010.09.010




2020     |     www.medigraphic.com