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| EnColl Corporation, established in 1994, is a California corporation that develops, manufactures and markets Type-I collagen-based products. EnColl uses its patented technology for the preparation of high purity and charge modified collagen (U.S. Patents 5,814,328 (1998); 6,127,143 (2000) & 6,548,077(2003). The company's technologies and manufacturing system yields a series of high quality products required for various medical fields such as general and plastic surgery (healing of wounds, burns and dermal ulcers/sores), orthopedic surgery (bone regeneration, spinal fusion), oral surgery (periodontal and dental products), and neurological injuries (brain/nerve regeneration), drug delivery, biopharmaceutical research, and cosmetic & dietary applications. |
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| EnColl was founded in 1994 by Dr. S. Gunasekaran. He is recognized as one of the world's foremost collagen experts. EnColl's proprietary collagen production technology makes the company a leader in this field. The Twice Treatment Process (TTP) and other unique purification steps of the patented technology results in a pure (99%), less immunogenic and better biocompatible collagen than those that are currently in the commercial market (proven pre-clinical studies). Further patented surface modified or energized collagen, "CollagenPRO", can be used for different biomedical applications. The company currently uses this patented technology to develop additional, advanced biotech products. |
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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.
Collagen has become an important tool for hastening the healing process of injured tissues. Current collagen products (derived through the extraction or recombinant methods) have potential problems in terms of the purity, immunogenicity and other related-problems rendering the collagen unsuitable for bio-medical and research applications. The traditional manufacturers of medical grade collagen and others have agreed that they have considerable amounts of type-III collagen contamination in their products. This results in a 3% rejection of their collagen when implanted in human. EnColl's high purity collagen has proven to be a better opportunity for all medical applications. |
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