Production method for cyclic dipeptide derived from native collagen

Abstract

In this study, a new method for producing cyclo(-Gly-Pro) using collagen as a raw material was examined. First, collagen was enzymatically hydrolysed and purified to obtain collagen tripeptide (CTP), rich in "Gly-X-Y" tripeptides. After heating this product under atmospheric pressure in an aqueous solution at 95? for 24 h, purification was achieved by reverse-phase column chromatography. The isolated component was confirmed to be cyclo(-Gly-Pro) through structural analysis by MS and NMR spectroscopies. Purity was determined to be 93.6%, and the recovery rate from CTP was 22%, indicating that much Gly-Pro-Y in CTP contributed to cyclization. The cyclization rate from Gly-Pro-Hyp or Gly-Pro-Ala was much higher than that of Gly-Pro, suggesting that cyclo(-Gly-Pro) was efficiently generated from the Gly-Pro-Y sequence. In summary, this is a simple, practical manufacturing method for producing cyclo(-Gly-Pro) from collagen at low cost with high efficiency.