Abstract: Collagen Tripeptide (CTP) has been successfully produced using the advanced biotechnological techniques developed by Miyagi Chemical Industrial, Co. Ltd. CTP, a highly pure collagen tripeptide with glycine at the N-terminus, was produced from collagen prepared from the skin of pigs raised in Japan. CTP exhibited the excellent moisture-retention effect and the characteristic feature of CTP was the extremely low incidence of allergic reaction upon its application to the skin.Moreover, micro-autoradiography confirmed that the tripeptide,which has an average molecular weight of about 280 Da, efficiently permeated  into the stratum corneum, epidermis and the upper part of hair follicles at a high density, and nearly homogenous permeation of this product was observed at the hair and the dermal layer (corium). Also, it was found that the tripeptide components of CTP had the acceleration effects on collagen synthesis of dermal fibroblast cell. The type M-30, M-60, and M-90 of CTP contained collagen tripeptide at levels of approximately 30%, 60%, and 90%, respectively

2) Non-antigenic and Low Allergic Gelatin Produced by Specific Digestion with an Enzyme - Coupled Matrix

Porcine gelatin (heat-denatured collagen) was digested with a bioreactor using an enzyme-coupled matrix (ECM) with purified collagenase. The digested gelatin, FreAlagin type R (M.W. range 200-10000 Da), was further purified by an HPLC system depending upon molecular size. The molecular weight range of the purified fractions, FreAlagin type P and type AD, were 200-500 and 2000-10000 Da, respectively, and glycine was the N-terminal amino acid of both types (>-93%). ECM has the capability of digesting gelatin at a specific point in the sequence before glycine, and it was determined that FreAlagin type P consists of a tri-peptide fraction with the amino acid sequence Gly-X-Y. No types of FreAlagin exhibited any reactivity with gelatin-specific IgG antibody raised in guinea pigs, and they also possessed an extremely low reactivity with gelatin-specific IgE antibody from the sera of patients who had experienced an anaphylactic reaction against gelatin after vaccination or after eating gelatin-containing foods. From these results, it was determined that FreAlagin types R and AD were nonantigenic, low-allergic gelatins. FreAlagin type R, and especially type AD, had strong adsorption-blocking activity comparable to the level of bovine serum albumin, whereas type P and glycine had virtually no adsorptionblocking activity. Therefore, the new types of gelatin, FreAlagin types R and AD, are suitable for pharmaceutical use to avoid gelatin allergy.