COMPARISON OF COLLAGEN EXTRACTION METHODS

Year 2019, , 383 - 395, 15.05.2019

Özge Ata , Şebnem Tavman

https://doi.org/10.15237/gida.GD18112

Abstract

Collagen is the most abundant protein in mammals.
Collagen, commonly used in the food, pharmaceutical, cosmetic and leather
industries, is commercially derived from by-products of mammals, such as pig
and bovine. There are at least 20 different types of collagen detected so far.
Most of the collagen in the body belongs to type 1, type 2 and type 3. Collagen
properties vary according to the pre-treatment and extraction method. Salting
out, acid hydrolysis and enzymatic hydrolysis methods are used for collagen
extraction. In addition, recent studies have shown that the use of ultrasound is
effective in increasing the extraction efficiency. In this review, studies on
the effect of pre-treatment and different extraction methods on collagen yield
were investigated.

Keywords

Collagen, extraction, ultrasound

KOLAJEN EKSTRAKSİYON YÖNTEMLERİNİN KARŞILAŞTIRILMASI

Abstract

Kolajen, memelilerde en bol bulunan proteindir. Gıda,
ilaç, kozmetik ve deri endüstrisinde yaygın olarak kullanılan kolajen, ticari
olarak, domuz ve sığır gibi memelilerin yan ürünlerinden elde edilmektedir.
Şimdiye kadar tespit edilen en az 20 farklı kolajen tipi vardır. Vücuttaki
kolajenlerin çoğu tip 1, tip 2 ve tip 3 grubuna aittir. Kolajen özellikleri,
uygulanan ön işlem ve ekstraksiyon yöntemine göre değişmektedir. Tuzla
çöktürme, asitle hidroliz ve enzimatik hidroliz yöntemleri kolajen ekstraksiyonu
için kullanılmaktadır. Bununla beraber, son yıllarda yapılan çalışmalar,
ultrason kullanımının ekstraksiyon verimini artırmada etkili olduğunu
göstermiştir. Bu derlemede, ön işlemlerin ve farklı ekstraksiyon yöntemlerinin
kolajen verimine etkisi ile ilgili yapılan çalışmalar incelenmiştir.

Keywords

Kolajen, ekstraksiyon, ultrason

References

• Ali, A. M. M., Benjakul, S., Kishimura, H. (2017). Molecular characteristics of acid and pepsin soluble collagens from the scales of golden carp (Probarbus jullieni). Emir J Food Agric, 29(6): 450-457.
• Ali, A. M. M., Kishimura, H., Benjakul, S. (2018). Extraction efficiency and characteristics of acid and pepsin soluble collagens from the skin of golden carp (Probarbus Jullieni) as affected by ultrasonication. Process Biochem, 66: 237-244.
• Arumugam, G. K. S., Sharma, D., Balakrishnan, R. M., Ettiyappan, J. B. P. (2018). Extraction, optimization and characterization of collagen from sole fish skin. Sustainable Chem Pharm, 9: 19-26.
• Avila Rodríguez, M. I., Rodríguez Barroso, L. G., Sánchez, M. L. (2018). Collagen: A review on its sources and potential cosmetic applications. J Cosmet Dermatol, 17: 20–26.
• Balasubramanian, P., Prabhakaran, M. P., Sireesha, M., Ramakrishna, S. (2012). Collagen in human tissues: structure, function, and biomedical implications from a tissue engineering perspective. In: Polymer Composites–Polyolefin Fractionation–Polymeric Peptidomimetics–Collagens, Pasch, H.(chief ed.), Springer, Berlin, Heidelberg, pp. 173-206.
• Chemat, F., Rombaut, N., Sicaire, A. G., Meullemiestre, A., Fabiano-Tixier, A. S., Abert-Vian, M. (2017). Ultrasound assisted extraction of food and natural products. Mechanisms, techniques, combinations, protocols and applications. A review. Ultrason Sonochem, 34: 540-560.
• Chen, J., Li, L., Yi, R., Xu, N., Gao, R., Hong, B. (2016). Extraction and characterization of acid-soluble collagen from scales and skin of tilapia (Oreochromis niloticus). LWT-Food Sci Technol, 66: 453-459.
• Cheng, F.Y., Hsu, F.W., Chang, H.S., Lin, L.C., Sakata, R. (2009). Effect of different acids on the extraction of pepsin-solubilised collagen containing melanin from silky fowl feet. Food Chem, 113(2): 563–567.
• Chuaychan, S., Benjakul, S., Kishimura, H. (2015). Characteristics of acid-and pepsin-soluble collagens from scale of seabass (Lates calcarifer). LWT-Food Sci Technol, 63(1): 71-76.
• De Moraes, M. C., Cunha, R. L. (2013). Gelation property and water holding capacity of heat-treated collagen at different temperature and pH values. Food Res Int, 50(1): 213-223.
• Dhakal, D., Koomsap, P., Lamichhane, A., Sadiq, M. B., Anal, A. K. (2018). Optimization of collagen extraction from chicken feet by papain hydrolysis and synthesis of chicken feet collagen based biopolymeric fibres. Food Biosci, 23:23-30.
• Dong, X. B., Li, X., Zhang, C. H., Wang, J. Z., Tang, C. H., Sun, H. M., Jia, W., Li, Y., Chen, L. L. (2014). Development of a novel method for hot-pressure extraction of protein from chicken bone and the effect of enzymatic hydrolysis on the extracts. Food Chem 157: 339-346.
• Duan, L., Li, J., Li, C., Li, G. (2013). Effects of NaCl on the rheological behavior of collagen solution. Korea-Aust Rheol J, 25(3): 137-144.
• Dun, R., Jackson, H. T., Smith, Y. (2008). Methods for processing and utilization of low cost fishes: a critical appraisal. J Food Sci Technol, 32: 1-12.
• Ehrlich, H., Wysokowski, M., Zółtowska-Aksamitowska, S., Petrenko, I., Jesionowski, T. (2018). Collagens of Poriferan Origin. Mar Drugs, 16(3): 1-21.
• Ferraro, V., Martinie, B.G., Sayd, T., Chambon, C., Anton, M., Lhoutellier, V.S. (2017). Collagen type I from bovine bone. Effect of animal age, bone anatomy and drying methodology on extraction yield, self-assembly, thermal behaviour and electrokinetic potential. Int J Biol Macromol, 97: 55–66.
• Gao, L. L., Wang, Z. Y., Li, Z., Zhang, C. X., Zhang, D. Q. (2017). The characterization of acid and pepsin soluble collagen from ovine bones (Ujumuqin sheep). J Integr Agr,17(3): 704-711.
• Gelse, K., Pöschl, E., Aigner, T. (2003). Collagens – structure, function, and biosynthesis. Adv Drug Delivery Rev, 55: 1531-1546.
• Gómez-Guillén, M. C., Giménez, B., López-Caballero, M. E., Montero, M. P. (2011). Functional and bioactive properties of collagen and gelatin from alternative sources: A review. Food Hydrocolloids, 25(8): 1813-1827.
• Gómez-Guillén, M. C., Montero, P. (2001). Extraction of gelatin from megrim (Lepidorhombus boscii) skins with several organic acids. J Food Sci, 66(2): 213-216.
• Hashim, P., Ridzwan, M. M., Bakar, J. (2014). Isolation and characterization of collagen from chicken feet. International Journal of Bioengineering and Life Sciences, 8(3): 250-254.
• Iltchenco, S., Kempka, A. P., Prestes, R. C. (2017). Profiles of enzymatic hydrolysis of different collagens and derivatives over time. R Bras Tecnol Agroindustr, 11(1): 2165-2185.
• Jeevithan, E., Jingyi, Z., Wang, N., He, L., Bao, B., Wu, W. (2015). Physico-chemical, antioxidant and intestinal absorption properties of whale shark type-II collagen based on its solubility with acid and pepsin. Process Biochem, 50(3): 463-472.
• Jeevithan, E., Wu, W., Nanping, W., Lan, H., Bao, B. (2014). Isolation, purification and characterization of pepsin soluble collagen isolated from silvertip shark (Carcharhinus albimarginatus) skeletal and head bone. Process Biochem, 49(10): 1767-1777.
• Jung, K. H., Choi, Y. C., Chun, J. Y., Min, S. G., Hong, G. P. (2014). Effects of concentration and reaction time of trypsin, pepsin, and chymotrypsin on the hydrolysis efficiency of porcine placenta. Korean J Food Sci Anim Resour, 34(2): 151-157.
• Kadler, K. E., Baldock, C., Bella, J., Boot-Handford, R. P. (2007). Collagens at a glance. J Cell Sci, 120(12): 1955–1958.
• Kaewdang, O., Benjakul, S., Kaewmanee, T., Kishimura, H. (2014). Characteristics of collagens from the swim bladders of yellowfin tuna (Thunnus albacares). Food Chem, 155: 264-270.
• Karsdal, M. A., Mortensen, J. H. (2016). Type VII collagen. In: Biochemistry of collagens, laminins and elastin: structure, function and biomarkers, Karsdal, M. A. (chief ed.), Academic Press, Denmark, pp. 57-60.
• Kittiphattanabawon, P., Nalinanon, S., Benjakul, S., Kishimura, H. (2015). Characteristics of pepsin-solubilised collagen from the skin of splendid squid (Loligo formosana). J Chem, 2015: 1-8.
• Krishnamoorthi, J., Ramasamy, P., Shanmugam, V., Shanmugam, A. (2017). Isolation and partial characterization of collagen from outer skin of Sepia pharaonis (Ehrenberg, 1831) from Puducherry coast. Biochem biophys rep, 10: 39-45.
• Lafarga, T., Hayes, M. (2014). Bioactive peptides from meat muscle and by-products: generation, functionality and application as functional ingredients. Meat Sci, 98(2): 227-239.
• Li, P., Wu, G. (2018). Roles of dietary glycine, proline, and hydroxyproline in collagen synthesis and animal growth. Amino Acids, 50(1): 29-38.
• Liang, Q., Wang, L., Sun, W., Wang, Z., Xu, J., Ma, H. (2014). Isolation and characterization of collagen from the cartilage of Amur sturgeon (Acipenser schrenckii). Process Biochem, 49(2): 318–323.
• Lin, C. W., Loughran, M., Tsai, T. Y., Tsai, S. W. (2013). Evaluation of convenient extraction of chicken skin collagen using organic acid and pepsin combination. J. Chin. Soc. Anim. Sic, 42(1): 27-38.
• Liu, D. C., Lin, Y. K., Chen, M. T. (2001). Optimum Condition of Extracting Collagen from Chicken Feet and its Characteristics. Asian-Australas J Anim Sci, 14(11): 1638-1644.
• Liu, D., Wei, G., Li, T., Hu, J., Lu, N., Regenstein, J. M., Zhou, P. (2015a). Effects of alkaline pretreatments and acid extraction conditions on the acid-soluble collagen from grass carp (Ctenopharyngodon idella) skin. Food Chem, 172:836-843.
• Liu, D., Zhang, X., Li, T., Yang, H., Zhang, H., Regenstein, J. M., Zhou, P. (2015b). Extraction and characterization of acid-and pepsin-soluble collagens from the scales, skins and swim-bladders of grass carp (Ctenopharyngodon idella). Food Biosci, 9: 68-74.
• Liu, H., Huang, K. (2016). Structural Characteristics of Extracted Collagen from Tilapia (Oreochromis mossambicus) Bone: Effects of Ethylenediaminetetraacetic Acid Solution and Hydrochloric Acid Treatment. Int J Food Prop, 19(1): 63-75.
• Liu, Y., Andarawis-Puri, N., & Eppell, S. J. (2016). Method to extract minimally damaged collagen fibrils from tendon. J Biol Methods, 3(4): e54.
• Lodish, H., Berk, A., Zipursky, S.L., Matsudaira, P., Baltimore, D., Darnell, J. (2000). Molecular Cell Biology. Section 22.3 : Collagen: The Fibrous Proteins of the Matrix, Edited by W. H. Freeman, New York.
• Mahboob, S. (2015). Isolation and characterization of collagen from fish waste material- skin, scales and fins of Catla catla and Cirrhinus mrigala. J Food Sci Technol, 52(7): 4296-4305.
• Manjula, U. D. P., Jayamanne, S. C., Thushari, G. G. N. (2015). Effect of pretreatment on physical properties of yellow fin tuna (Thunnus albacares) fish glue. Int J Fish Aquat Stud, 2(4S): 14-21.
• Nalinanon, S., Benjakul, S., Visessanguan, W., Kishimura, H. (2008). Tuna pepsin: characteristics and its use for collagen extraction from the skin of threadfin bream (Nemipterus spp.). J Food Sci, 73(5): C413-C419.
• Ninan, G., Joseph,J., Aliyamveettil, Z. A. (2014). A comparative study on the physical,chemical and functional properties of carp skin and mammalian gelatins. J Food Sci Technol, 51(9): 2085–2091.
• Peck Loo, K., Mashitah, M. D. (2013). Extraction of Acid and Pepsin Soluble Collagen from Selected Malaysian Freshwater Fish Muscles: Modified Lowry’s Measurement Method. J. Agrobiotech, 4: 17-32.
• Prayitno, P. (2007). Extraction of Collagen from Chicken Feet with Various Acidic Solutions and Soaking Time. Animal Production, 9(2): 99-104.
• Ran, X. G., Wang, L. Y. (2014). Use of ultrasonic and pepsin treatment in tandem for collagen extraction from meat industry by‐products. J Sci Food Agric, 94(3): 585-590.
• Ricard-Blum, S. (2011). The collagen family. Cold Spring Harb Perspect Biol, 3: 1-19.
• Santos, M. H., Silva, R. M., Dumont, V. C., Neves, J. S., Mansur, H. S., Heneine, L. G. D. (2013). Extraction and characterization of highly purified collagen from bovine pericardium for potential bioengineering applications. Mater Sci Eng: C, 33(2): 790-800.
• Schmidt, M. M., Dornelles, R. C. P., Mello, R. O., Kubota, E. H., Mazutti, M. A., Kempka, A. P., Demiate, I. M. (2016). Collagen extraction process. Int Food Res J, 23(3): 913-922.
• See, S. F., Ghassem, M., Mamot, S., Babji, A. S. (2015). Effect of different pretreatments on functional properties of African catfish (Clarias gariepinus) skin gelatin. J Food Sci Technol, 52(2): 753-762.
• Sibilla, S., Godfrey, M., Brewer, S., Budh-Raja, A., Genovese, L. (2015). An Overview of the Beneficial Effects of Hydrolysed Collagen as a Nutraceutical on Skin Properties: Scientific Background and Clinical Studies. Open Nutraceuticals J, 8: 29-42.
• Simões, G. S., Silveira, E. T. F., de Oliveira, S. R., Poleze, E., Allison, J. R., Ida, E. I., Shimokomaki, M. (2014). Optimum conditions for extracting collagen from the tunica albuginea of immunologically castrated pig testes and the functional properties of the isolated collagen. Meat Sci, 96(4): 1460-1468.
• Sinthusamran, S., Benjakul, S., Kishimura, H. (2013). Comparative study on molecular characteristics of acid soluble collagens from skin and swim bladder of seabass (Lates calcarifer). Food Chem, 138(4): 2435-2441.
• Sionkowska, A., Kozłowska, J., Skorupska, M., Michalska, M. (2015). Isolation and characterization of collagen from the skin of Brama australis. Int J Biol Macromol, 80: 605-609.
• Song, H., Li, B. (2017). Beneficial Effects of Collagen Hydrolysate: A Review on Recent Developments. Biomed J Sci & Tech Res, 1(2): 1-4.
• Song, K. M., Jung, S. K., Kim, Y. H., Kim, Y. E., Lee, N. H. (2018). Development of industrial ultrasound system for mass production of collagen and biochemical characteristics of extracted collagen. Food Bioprod Process, 110: 96-103.
• Tan, Y., Chang, S. K. (2018). Isolation and characterization of collagen extracted from channel catfish (Ictalurus punctatus) skin. Food Chem, 242: 147-155.
• Wang, L., Yang, B., Du, X., Yang, Y., Liu, J. (2008). Optimization of conditions for extraction of acid-soluble collagen from grass carp (Ctenopharyngodon idella) by response surface methodology. Innovative Food Sci Emerg Technol, 9(4): 604-607.
• Włodarczyk, M. G., Kubisz, L., Włodarczyk, D. (2017). Amino acid composition in determination of collagen origin and assessment of physical factors effects. Int J Biol Macromol, 104: 987-991.
• Xu, S., Yang, H., Shen, L., Li, G. (2017). Purity and yield of collagen extracted from southern catfish (Silurus meridionalis Chen) skin through improved pretreatment methods. Int J Food Prop, 20(sup1): S141-S153.
• Yang, H., Shu, Z. (2014). The extraction of collagen protein from pigskin. J Chem Pharm Res, 6(2): 683-687.
• Yasothai, R., Giriprasad, R. (2015). Extraction of protein by enzymatic hydrolysis. Int J Environ Sci Technol, 4(1): 190-192.
• Yu, F., Zong, C., Jin, S., Zheng, J., Chen, N., Huang, J., Chen, Y., Huang, F., Yang, Z., Tang, Y., Ding, G. (2018). Optimization of Extraction Conditions and Characterization of Pepsin-Solubilised Collagen from Skin of Giant Croaker (Nibea japonica). Mar Drugs, 16(1): 29.
• Zhou, C., Li, Y., Yu, X., Yang, H., Ma, H., Yagoub, A. E. A., Cheng, Y., Hu, J., Otu, P. N. Y. (2016). Extraction and characterization of chicken feet soluble collagen. LWT-Food Sci Technol, 74: 145-153.
• Zhou, P., Regenstein, J. M. (2005). Effects of alkaline and acid pretreatments on Alaska pollock skin gelatin extraction. J Food Sci, 70(6): c392-c396.
• Zou, Y., Xu, P., Li, P., Cai, P., Zhang, M., Sun, Z., Sun, C., Xu, W., Wang, D. (2017). Effect of ultrasound pre-treatment on the characterization and properties of collagen extracted from soft-shelled turtle (Pelodiscus sinensis). LWT-Food Sci Technol, 82: 72-81.