? The characterization of acid and pepsin soluble collagen from ovine bones (Ujumuqin sheep)
Quick Search in JIA      Advanced Search  
    2018, Vol. 17 Issue (03): 704-711     DOI: 10.1016/S2095-3119(17)61751-9
Food Science Current Issue | Next Issue | Archive | Adv Search Previous Articles  |  Next Articles  
The characterization of acid and pepsin soluble collagen from ovine bones (Ujumuqin sheep)
GAO Ling-ling, WANG Zhen-yu, LI Zheng, ZHANG Cai-xia, ZHANG De-quan  
Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-products Processing, Ministry of Agriculture, Beijing 100193, P.R.China
 Download: PDF in ScienceDirect (0 KB)   HTML (1 KB)   Export: BibTeX | EndNote (RIS)      Supporting Info
Abstract Ovine bones are the major by-products after slaughtered.  The present study was conducted to extract and characterize acid soluble collagens (ASC) and pepsin soluble collagens (PSC) from ovine bones (Ujumuqin sheep).  Ovine bones collagen were identified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and liquid chromatography-tandem mass spectrometry (LC-MS/MS) as type I collagen.  The results of Fourier transform infrared (FTIR) spectra analysis testified the existence of triple superhelical structure in both ASC and PSC, showing pepsin did not disrupt the triple helical structure of ovine bones collagen.  Glycine, accounting for one-third of total amino acids, was the major amino acid for ovine bones collagen.  Higher imino acid content was responsible for higher thermal denaturation temperature of ovine bones collagen compared to fish collagens.  The isoelectric point of ASC was lower than PSC due to the higher content of acidic amino acids.  Therefore, this study provides the potential reference for collagen extraction and application of ovine bones by-procduct.
E-mail this article
Add to my bookshelf
Add to citation manager
E-mail Alert
Articles by authors
Key wordsovine bones     collagen     characterization     amino acid composition     denaturation temperature     
Received: 2017-05-11; Published: 2017-06-07

This work has been funded by the emarked fund for China Agriculture Research System (CARS-39), the National Agricultural Science and Technology Innovation Program.

Corresponding Authors: Correspondence ZHANG De-quan, Tel/Fax: +86-10-62818740, E-mail: dequan_zhang0118@126.com   
About author: GAO Ling-ling, E-mail: gaolinglingwork@163.com;
Cite this article:   
GAO Ling-ling, WANG Zhen-yu, LI Zheng, ZHANG Cai-xia, ZHANG De-quan. The characterization of acid and pepsin soluble collagen from ovine bones (Ujumuqin sheep)[J]. Journal of Integrative Agriculture, 2018, 17(03): 704-711.
http://www.chinaagrisci.com/Jwk_zgnykxen/EN/ 10.1016/S2095-3119(17)61751-9      or     http://www.chinaagrisci.com/Jwk_zgnykxen/EN/Y2018/V17/I03/704
[1] Abe Y, Krimm S. 1972. Normal vibrations of crystalline polyglycine I. Biopolymers, 11, 1817-1839.
[2] Barth A, Zscherp C. 2002. What vibrations tell about proteins. Quarterly Reviews of Biophysics, 35, 369-430.
[3] Barzideh Z, Latiff A A, Gan C Y, Benjakul S, Karim A A. 2014. Isolation and characterisation of collagen from the ribbon jellyfish (Chrysaora sp.). International Journal of Food Science & Technology, 49, 1490-1499.
[4] 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 Science and Technology, 66, 453-459.
[5] Chen L, Li X, Ni N, Liu Y, Chen L, Wang Z, Shen Q W, Zhang D. 2016. Phosphorylation of myofibrillar proteins in post-mortem ovine muscle with different tenderness. Journal of the Science of Food and Agriculture, 96, 1474-1483.
[6] Chen Y, Ye R, Wang Y. 2015. Acid-soluble and pepsin-soluble collagens from grass carp (Ctenopharyngodon idella) skin: A comparative study on physicochemical properties. International Journal of Food Science & Technology, 50, 186-193.
[7] Dai N, Etzkorn F A. 2009. cis-Trans proline isomerization effects on collagen triple-helix stability are limited. Journal of the American Chemical Society, 131, 13728-13732.
[8] Doyle B B, Bendit E G, Blout E R. 1975. Infrared spectroscopy of collagen and collagen-like polypeptides. Biopolymers, 14, 937-957.
[9] Duan R, Zhang J, Du X, Yao X, Konno K. 2009. Properties of collagen from skin, scale and bone of carp (Cyprinus carpio). Food Chemistry, 112, 702-706.
[10] Edwards H G M, Farwell D W, Holder J M, Lawson E E. 1997. Fourier-transform Raman spectroscopy of ivory: II. Spectroscopic analysis and assignments. Journal of Molecular Structure, 435, 49-58.
[11] Engel J, Bächinger H P. 2005. Structure, stability and folding of the collagen triple helix. Topics in Current Chemistry, 247, 7-33.
[12] Farrell Jr H M, Wickham E D, Unruh J J, Qi P X, Hoagland P D. 2001. Secondary structural studies of bovine caseins: Temperature dependence of β-casein structure as analyzed by circular dichroism and FTIR spectroscopy and correlation with micellization. Food Hydrocolloids, 15, 341-354.
[13] Foegeding E, Lanier T, Hultin H. 1996. Characteristics of edible muscle tissues. Food Chemistry, 3, 879-942.
[14] Guzzi Plepis A M D, Goissis G, Das-Gupta D K. 1996. Dielectric and pyroelectric characterization of anionic and native collagen. Polymer Engineering and Science, 36, 2932-2938.
[15] Jackson M, Choo L P I, Watson P H, Halliday W C, Mantsch H H. 1995. Beware of connective tissue proteins: Assignment and implications of collagen absorptions in infrared spectra of human tissues. Biochimica et Biophysica Acta-Molecular Basis of Disease, 1270, 1-6.
[16] Jeevithan E, Wu W H, Wang N P, Lan H, Bao B. 2014. Isolation, purification and characterization of pepsin soluble collagen isolated from silvertip shark (Carcharhinus albimarginatus) skeletal and head bone. Process Biochemistry, 49, 1767-1777.
[17] Karayannakidis P D, Chatziantoniou S E, Zotos A. 2014. Effects of selected process parameters on physical and sensorial properties of yellowfin tuna (Thunnus albacares) skin gelatin. Journal of Food Process Engineering, 37, 461-473.
[18] Kittiphattanabawon P, Benjakul S, Sinthusamran S, Kishimura H. 2015. Characteristics of collagen from the skin of clown featherback (Chitala ornata). International Journal of Food Science & Technology, 50, 1972-1978.
[19] Kittiphattanabawon P, Benjakul S, Visessanguan W, Kishimura H, Shahidi F. 2010. Isolation and characterisation of collagen from the skin of brownbanded bamboo shark (Chiloscyllium punctatum). Food Chemistry, 119, 1519-1526.
[20] Laemmli U K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
[21] Lee J K, Kang S I, Kim Y. J, Kim M J, Heu M S, Choi B D, Kim J S. 2016. Comparison of collagen characteristics of sea- and freshwater-rainbow trout skin. Food Science and Biotechnology, 25, 131-136.
[22] Liu D, Liang L, Regenstein J M, Zhou P. 2012. Extraction and characterisation of pepsin-solubilised collagen from fins, scales, skins, bones and swim bladders of bighead carp (Hypophthalmichthys nobilis). Food Chemistry, 133, 1441-1448.
[23] Liu D, Nikoo M, Boran G, Zhou P, Regenstein J M. 2015. Collagen and gelatin. Annual Review of Food Science and Technology, 6, 527-557.
[24] Liu D, Zhou P, Li T, Regenstein J M. 2014. Comparison of acid-soluble collagens from the skins and scales of four carp species. Food Hydrocolloids, 41, 290-297.
[25] Li Z, Wang B, Chi C, Zhang Q, Gong Y, Tang J, Luo H, Ding G. 2013. Isolation and characterization of acid soluble collagens and pepsin soluble collagens from the skin and bone of Spanish mackerel (Scomberomorous niphonius). Food Hydrocolloids, 31, 103-113.
[26] Matmaroh K, Benjakul S, Prodpran T, Encarnacion A B, Kishimura H. 2011. Characteristics of acid soluble collagen and pepsin soluble collagen from scale of spotted golden goatfish (Parupeneus heptacanthus). Food Chemistry, 129, 1179-1186.
[27] Nagai T, Suzuki N. 2000. Isolation of collagen from fish waste material-skin, bone and fins. Food Chemistry, 68, 277-281.
[28] Nagai T, Suzuki N, Nagashima T. 2008. Collagen from common minke whale (Balaenoptera acutorostrata) unesu. Food Chemistry, 111, 296-301.
[29] Nam K A, You S G, Kim S M. 2008. Molecular and physical characteristics of squid (Todarodes pacificus) skin collagens and biological properties of their enzymatic hydrolysates. Journal of Food Science, 73, C249-C255.
[30] Payne K J, Veis A. 1988. Fourier transform IR spectroscopy of collagen and gelatin solutions: Deconvolution of the amide I band for conformational studies. Biopolymers, 27, 1749-1760.
[31] Shoulders M D, Raines R T. 2009. Collagen structure and stability. Annual Review of Biochemistry, 78, 929-958.
[32] Singh P, Benjakul S, Maqsood S, Kishimura H. 2011. Isolation and characterisation of collagen extracted from the skin of striped catfish (Pangasianodon hypophthalmus). Food Chemistry, 124, 97-105.
[33] Toldrá F, Mora L, Reig M. 2016. New insights into meat by-product utilization. Meat Science, 120, 54-59.
[34] Veeruraj A, Arumugam M, Ajithkumar T, Balasubramanian T. 2015. Isolation and characterization of collagen from the outer skin of squid (Doryteuthis singhalensis). Food Hydrocolloids, 43, 708-716.
[35] Zhou G, Zhang W, Xu X. 2012. China’s meat industry revolution: Challenges and opportunities for the future. Meat Science, 92, 188-196.
No Similar of article
Copyright © 2015 ChinaAgriSci.com, All Rights Reserved
Chinese Academy of Agricultural Sciences (CAAS) No. 12 South Street, Zhongguancun, Beijing 100081, P. R. China
http://www.ChinaAgriSci.com   JIA E-mail: jia_journal@caas.cn