Abstract:

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)