The recombinant protein produced in the present investigation is human type II collagen which is the major collagenous component in the cartilage [16] . Purified recombinant human type II collagen is regarded very useful in applications for cartilage repair [17] . The formation of stable triple helical collagen at physiological temperature requires C-P4H activity [16, 18] . Consequently, the coexpression of C-P4H, an α 2 β 2 tetramer located within the lumen of the endoplasmic reticulum, has been proven essential for the production of temperature-stable recombinant collagens [7, 8] . Recombinant type II collagen has been produced successfully in the baculovirus expression system [19, 20] and in P. pastoris [8, 20] .