Cardinal acuity on the extraction and characterization of soluble collagen from the underutilized abattoir junks for clinical demands

Improper utilization of solid wastes causes environmental flusters by prying the live organisms in the form of abattoir scraps. One of the most common underutilized biowastes in slaughter houses are bovine Achilles Tendons (AT). It has the rich source of type I collagen, since AT is composed of stiff and rigid materials, the collagen yield in the solubilized form is almost non pragmatic with conservative methods. Herein, this work emphasis the state-of-art on the design of seamless technique for the extraction of collagenous proteins with complete solubilization for clinical and healthcare application. High yield of soluble collagen (72%) was obtained through pepsin digestion coupled ultrasonic wave method. The triple helical structure of the native soluble type I collagen was confirmed through electrophoresis, circular dichroism (CD) and vibrational circular dichroism (VCD) analysis. The scanning electron microscopy (SEM) depicts the highly interconnected microfibrillar porous structure of the collagen as scaffold. The in vitro biocompatibility and fluorescent activity on NIH 3T3 fibroblast cells over the microfibrillar collagen scaffold possess excellent cell viability and proliferation at different time. Thus, it can be concluded that the AT-Collagen could be promising value-added bloom to bioeconomic growth for healthcare industries.