FOOD SCIENCE ›› 2010, Vol. 31 ›› Issue (2): 87-91.doi: 10.7506/spkx1002-6630-201002021

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Extraction and Characterization of TypeⅠCollagen from Bovine Bone

LIU Li-li1,2,MA Mei-hu1,*,YANG Xie-li2   

  1. 1. College of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, China;
    2. Department of Food and Bioengineering, Henan University of Science and Technology, Luoyang 471003, China
  • Received:2009-03-05 Revised:2009-08-24 Online:2010-01-15 Published:2010-12-29
  • Contact: MA Mei-hu1,*,


In the present study, critical process steps for extracting type Ⅰ collagen from bovine bone, such as defatting, decalcification and extraction medium selection were optimized. Along with this, purified collagen was analyzed through SDSPAGE, UV, FT-IR and DSC, and compared with the standard of calf-tendon type I collagen. Results indicated that the optimal extraction process was based on low-temperature ethyl ether reflux defatting and decalcification of bovine bone powder with a particle size of 5 × 10 mm using 0.48% hydrochloric acid, followed by extraction using a mixed solution simultaneously containing 1% citric acid and 1% pepsin. The extracted collagen was identified as type I collagen and the purity reached electrophoretic grade. Furthermore, the unique triple helical structure of type I collagen remained very well.

Key words: bovine bone, type Ⅰ collagen, extraction, SDS-PAGE, differential scanning calormetry (DSC), Fourier transform infrared spectroscopy (FT-IR)

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