Isolation and characterisation of collagen from elk antler velvet
Do Hun Lee A H , Heeok Hong B H , Gaurav Lodhi A , Sun Hee Cheong A F , Pyo Jam Park A F , Tiejun Hu C , Kim Sangwoo D , Sang Ho Moon E F G and Byong Tae Jeon E F G
+ Author Affiliations
- Author Affiliations
A Department of Biotechnology, Konkuk University, Chungju 380-701, Republic of Korea.
B Department of Medical Science, School of Medicine Konkuk University, Seoul 143-701, Republic of Korea.
C Department of Food Science, Jilin Sino-ROK Institute of Animal Science, Changchun 130600, China.
D National Institute of Animal Science, RDA, Suwon, 441-706, Republic of Korea.
E Division of Food Bioscience, Konkuk University, Chungju 380-701, Republic of Korea.
F Nokyong Research Center, Konkuk University, Chungju 380-701, Republic of Korea.
G Corresponding authors. Email: moon0204@kku.ac.kr; hannokwon@kku.ac.kr
H These authors contributed equally to this work.
Animal Production Science 54(8) 1095-1101 https://doi.org/10.1071/AN13281
Submitted: 3 July 2013 Accepted: 14 October 2013 Published: 17 December 2013
Abstract
Collagen was extracted from the antler velvet of elk (Cervus elaphus). Two types of collagen were prepared namely, acetic acid-soluble collagen and pepsin-soluble collagen. The electrophoretic patterns of both of the collagens showed that they were heterotrimeric, i.e. they consisted of α1α2α3. The total yield of the collagen obtained from the elk antler velvet was 12.1%. Amino acid analysis of the collagen by high-performance liquid chromatography showed that imino acid content such as that of proline and hydroxyproline was high, which might contribute to better visco-elastic properties. The peptide mapping of the collagens showed their similarity with porcine Type I collagen, thereby suggesting that the primary structure of both collagens is identical to that of porcine skin Type I collagen. The thermal denaturation temperature was 37°C, which is comparable to porcine Type I collagen and may also be as a result of high imino acid content.
References
AOAC (1995) ‘Official methods of analysis of AOAC international.’ 16th edn. (Association of Official and Analytical Chemists International: Washington, DC)Asghar A, Henrickson RL (1982) Chemical, biochemical, functional and nutritional characteristics of collagen in food systems. In ‘Advances in food research’. (Eds CO Chichester, EM Marata, BS Schweigert) pp. 237–273. (Academic Press: London)
Balian G, Bowes JH (1977) The structure and properties of collagen. In ‘The science and technology of gelatin’. (Eds AG Ward, A Courts) pp. 1–31. (Academic Press: London)
Choi HK, Kim KH, Kim KH, Kim YS, Lee MW, Whang WK (2006) Metabolomic differentiation of deer antlers of various origins by HNMR spectrometry and principal components analysis. Journal of Pharmaceutical and Biomedical Analysis 41, 1047–1050.
| Metabolomic differentiation of deer antlers of various origins by HNMR spectrometry and principal components analysis.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD28Xks1equ7s%3D&md5=d5c97f092184648d664ae39ead3e69b5CAS | 16495028PubMed |
Eastoe JE, Leach AA (1977) Chemical constitution of gelatin. In ‘The science and technology of gelatin’. (Eds AG Ward, A Courts) pp. 73–107. (Academic Press: New York)
Fernández-Díaz MD, Montero P, Gòmez-Guillèn MC (2001) Gel properties of collagens from skins of cod (Gadus morhua) and hake (Merluccius merluccius) and their modification by coenhancers magnesium sulphate, glycerol and transglutaminase. Food Chemistry 74, 161–167.
| Gel properties of collagens from skins of cod (Gadus morhua) and hake (Merluccius merluccius) and their modification by coenhancers magnesium sulphate, glycerol and transglutaminase.Crossref | GoogleScholarGoogle Scholar |
Foegeding EA, Lanier TC, Hultin HO (1996) Collagen. In ‘Food chemistry’. (Ed. OR Fennema) pp. 902–906. (Marcel Dekker: New York)
Huang TK (1997) ‘Handbook of composition and pharmacological action of commonly used traditional Chinese medicine.’ 2nd edn. (China Medical and Pharmaceutical Science Publishing House Press: Beijing)
Ikoma K, Kobayashi H, Tanaka J, Walsh D, Mann S (2003) Physical properties of Type I collagen extracted from fish scales of Pagrus major and Oreochromis niloticas. Food Chemistry 32, 199–204.
Jeon BT, Moon SH (2006) A review on feeding system for deer production. Journal of Integrated Field Science 3, 39–44.
Kimura S, Ohno Y (1987) Fish Type I collagen: tissue-specific existence of two molecular forms, (α1)2α2 and α1α2α3, in Alaska Pollack. Comparative Biochemistry and Physiology. Part B: Comparative Biochemistry 88, 409–413.
| Fish Type I collagen: tissue-specific existence of two molecular forms, (α1)2α2 and α1α2α3, in Alaska Pollack.Crossref | GoogleScholarGoogle Scholar |
Kimura S, Ohno Y, Miyauchi Y, Uchida N (1987) Fish skin type I collagen: wide distribution of an α3 subunit in teleosts. Comparative Biochemistry and Physiology. Part B: Comparative Biochemistry 88, 27–34.
| Fish skin type I collagen: wide distribution of an α3 subunit in teleosts.Crossref | GoogleScholarGoogle Scholar | 1:STN:280:DyaL1c%2FltlyjsA%3D%3D&md5=4a20d55d7f7c862e5f3e2fd113f24940CAS |
Kimura S, Zhu XP, Matsui R, Shijoh M, Takamizawa S (1988) Characterization of fish muscle Type I collagen. Journal of Food Science 53, 1315–1318.
| Characterization of fish muscle Type I collagen.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaL1cXmtV2rs7c%3D&md5=a9e50188faec3bc2b4c9560b35533e0fCAS |
Kittiphattanabawon P, Benjakul S, Visessanguan W, Nagai T, Tanaka M (2005) Characterisation of acid-soluble collagen from skin and bone of bigeye snapper (Priacanthus tayenus). Food Chemistry 89, 363–372.
| Characterisation of acid-soluble collagen from skin and bone of bigeye snapper (Priacanthus tayenus).Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2cXnsVGit7Y%3D&md5=20820f387534f1a05238011b3af174c2CAS |
Kolodziejska I, Sikorski ZE, Niecikowska C (1999) Parameters affecting the isolation of collagen from squid (Illex argentinus) skins. Food Chemistry 66, 153–157.
| Parameters affecting the isolation of collagen from squid (Illex argentinus) skins.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK1MXjs12hsbg%3D&md5=48c08d5480e56ace54a7c323aa99fa60CAS |
Laemmli UK (1970) Cleavage of structural proteins during assembly of head of bacteriophage T4. Nature 227, 680–685.
| Cleavage of structural proteins during assembly of head of bacteriophage T4.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD3MXlsFags7s%3D&md5=abdcf0bd12d8773f5e79c34e09e19ab8CAS | 5432063PubMed |
Matsui R, Ishida M, Kimura S (1991) Characterization of an α3 chain from the skin Type I collagen of chum salmon (Oncorhynchus keta). Comparative Biochemistry and Physiology. Part B: Comparative Biochemistry 99, 171–174.
| Characterization of an α3 chain from the skin Type I collagen of chum salmon (Oncorhynchus keta).Crossref | GoogleScholarGoogle Scholar |
Nagai T, Ogawa T, Nakamura T, Ito T, Nakagawa H, Fujiki K, Nakao M, Yano T (1999) Collagen of edible jellyfish exumbrella. Journal of the Science of Food and Agriculture 79, 855–858.
| Collagen of edible jellyfish exumbrella.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK1MXivVOktrk%3D&md5=85f0c185a396a28ca2d5877ca8923a86CAS |
Nagai T, Worawattanamateekul W, Suzuki N, Nakamura T, Ito T, Fujiki K, Nakao M, Yano T (2000) Isolation and characterization of collagen from rhizostomous jellyfish (Rhopilema asamushi). Food Chemistry 70, 205–208.
| Isolation and characterization of collagen from rhizostomous jellyfish (Rhopilema asamushi).Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD3cXktF2qu7c%3D&md5=d8ab1d310676751c404f203e7f25febeCAS |
Nakamura YN, Iwamoto H, Ono Y, Nishimura S, Tabata S (2003) Relationship among collagen amount, distribution and architecture in the M. Longissimus thoracis and M. pectoralis profundus from pigs. Meat Science 64, 43–50.
| Relationship among collagen amount, distribution and architecture in the M. Longissimus thoracis and M. pectoralis profundus from pigs.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD38Xps12qsLY%3D&md5=07128206871e57024cf06988daf55c00CAS | 22062661PubMed |
Nimni ME, Harkness RD (1988) Molecular structures and functions of collagen. In ‘Collagen. Vol. 1: Biochemistry’. (Ed. ME Nimni) pp. 1–78. (CRC Press: Boca Raton, FL)
Ogawa M, Moody MM, Portier RJ, Bell J, Schexnayder MA, Losso JN (2003) Biochemical properties of blackdrum and sheephead seabream skin collagen. Journal of Agricultural and Food Chemistry 51, 8088–8092.
| Biochemical properties of blackdrum and sheephead seabream skin collagen.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD3sXpsVamur4%3D&md5=4bde939cc1f557c19b959e25a1db7937CAS | 14690401PubMed |
Papon P, Leblon J, Meijer PHE (2007) Gelation and transitions in biopolymers. In ‘The physics of phase transitions’. (Eds P Papon, J Leblon, PHE Meijer) pp. 189–213. (Springer: Heidelberg, Germany)
Parenteau-Bareil R, Gauvin R, Cliché S, Gariépy C, Germain L, Berthod F (2011) Comparative study of bovine, porcine and avian collagens for the production of a tissue engineered dermis. Acta Biomaterialia 7, 3757–3765.
| Comparative study of bovine, porcine and avian collagens for the production of a tissue engineered dermis.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC3MXhtFSqs7rI&md5=16578d8eaf520306e2c8cbd89fe9f031CAS | 21723967PubMed |
Piez KA, Gross J (1960) The amino acid composition of some fish collagens: the relation between composition and structure. The Journal of Biological Chemistry 235, 995–999.
Ramachandran GN, Sasisekharan V (1965) Refinement of the structure of collagen. Biochimica et Biophysica Acta 109, 314–316.
| Refinement of the structure of collagen.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaF28Xht1Gjtg%3D%3D&md5=7ec8ceeafde51ab3e45171149b3c0227CAS | 5864027PubMed |
Rigby BJ (1968) Amino-acid composition and thermal stability of the skin collagen of the Antarctic ice-fish. Nature 219, 166–167.
| Amino-acid composition and thermal stability of the skin collagen of the Antarctic ice-fish.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaF1cXksFSjurw%3D&md5=dc93bfbb6904c086ecdb75e69acb585eCAS | 5659642PubMed |
Saito M, Kunisaki N, Urano N, Kimura S (2002) Collagen as the major edible component of sea cucumber (Stichopus japonicus). Journal of Food Science 67, 1319–1322.
| Collagen as the major edible component of sea cucumber (Stichopus japonicus).Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD38XkvVyqsLc%3D&md5=756e5dca0e5110fb2457acbba298018fCAS |
Sarbon NMhd, Badii F, Howell NK (2013) Preparation and characterisation of chicken skin gelatin as an alternative to mammalian gelatine. Food Hydrocolloids 30, 143–151.
| Preparation and characterisation of chicken skin gelatin as an alternative to mammalian gelatine.Crossref | GoogleScholarGoogle Scholar |
Schrieber R, Gareis H (2007) ‘Gelatine handbook.’ (Wiley-VCH GmbH & Co: Weinhem, Germany)
Senaratne LS, Park PJ, Kim SK (2006) Isolation and characterization of collagen from brown backed toadfish (Lagocephalus gloveri) skin. Bioresource Technology 97, 191–197.
| Isolation and characterization of collagen from brown backed toadfish (Lagocephalus gloveri) skin.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2MXhtVanurnJ&md5=db4203efa2f4aa2cd1e4f739b3873abcCAS | 15964191PubMed |
Sunwoo HH (1998) Isolation, characterization and localization of glycosamines in growing antlers of wapiti (Cervus elaphus). Comparative Biochemistry and Physiology. Part B. Biochemistry & Molecular Biology 120, 273–283.
| Isolation, characterization and localization of glycosamines in growing antlers of wapiti (Cervus elaphus).Crossref | GoogleScholarGoogle Scholar | 1:STN:280:DyaK1M%2FgsVSltg%3D%3D&md5=aedc6889a708fad8bd7e950afd078fc3CAS |
Sunwoo HH, Nakano T, Hudson RJ, Sim JS (1995) Chemical composition of antlers from wapiti (Cervus elaphus). Journal of Agricultural and Food Chemistry 43, 2846–2849.
| Chemical composition of antlers from wapiti (Cervus elaphus).Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK2MXovFSktbo%3D&md5=7d04272c5ce9f1fce17cc356def23512CAS |
Te Nijenhuis K (1997) Thermoreversible networks: viscoelastic properties and structure of gels. Advances in Polymer Science 130, 1–267.
Wardale RJ, Duance VC (1993) Characterization of porcine articular and growth plate collagens. Journal of Cell Science 105, 975–984.
Wong DWS (1989) ‘Mechanism and theory in food chemistry.’ (Van Nostrand Reinhold: New York)
Yoshimura K, Terashima M, Hozan D, Shirai K (2000) Preparation and dynamic viscoelasticity characterization of alkali – solubilized collagen from shark skin. Journal of Agricultural and Food Chemistry 48, 685–690.
| Preparation and dynamic viscoelasticity characterization of alkali – solubilized collagen from shark skin.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD3cXhtlKjtrw%3D&md5=966addbf75f8e8d4d907a8b829460b2eCAS | 10725134PubMed |
