EnColl’s technology is a Two-step enzyme Treatment Process (TTP) for the modification and purification of Type-I collagen which results in collagen that is 99% pure, yields the least immunogenicity & renders high bioactivity necessary for treatment, therapy & tissue regeneration for medical applications. Papain, an enzyme extracted from papaya, is known to break the cleavage sites neighboring the disulfide bonds of cysteine. Papain has also been reported to have a lytic (destructive) effect of elastin and bound antibodies, the contaminants that are difficult to remove from purified collagen (Coulson, Biochim. Biophys. Acta 237:378, 1971; and Smith et al., Nature 198:1311-2, 1963). The collagen is further bioactivated by varied degrees of controlled modification of phosphorylation. Purified collagen can be chemically-modified by covalently binding phosphates to hydroxyl groups of hydroxylated amino acids. This reaction (an example for serine is given below) likely involves covalent bonding of phosphate to hydroxyl group of serine, tyrosine and/or threonine, hydroxylysine and hydroxyproline. The reaction is controllable to achieve different degrees of bioactivity for varied applications. EnColl’s phosphorylated collagen renders unique abilities in the growth of soft or hard tissue as needed by the physiological system.