Effect of High Pressure on the Porcine Placenral Hydrolyzing Activity of Pepsin, Trypsin and Chymotrypsin

다국어 초록 (Multilingual Abstract)

This study investigated the effects of protease treatments (trypsin, chymotrypsin, and pepsin) under various pressure lev-els (0.1-300 MPa) for the characteristics of porcine placenta hydrolysates. According to gel electrophoretic patterns, thetrypsin showed the best placental hydrolyzing activity followed by chymotrypsin, regardless of the pressure levels. In par-ticular, the peptide bands of tryptic-digested hydrolysate were not shown regardless of applied pressure levels. The peptidebands of hydrolysate treated chymotrypsin showed gradual decreases in molecular weights (Mw) with increasing pressurelevels. However, the pepsin did not show any evidences of placental hydrolysis even though the pressure levels were increa-sed to 300 MPa. The gel permeation chromatography (GPC) profiles showed that the trypsin and pepsin had better placentalhydrolyzing activities under high pressure (particularly at 200 MPa), with lower Mw distributions of the hydrolysates. Pepsinalso tend to lower the Mw of peptides, while the major bands of hydrolysates being treated at 300 MPa were observed atmore than 7,000 Da. There were some differences in amino acid compositions of the hydrolysates, nevertheless, the peptideswere mainly composed of glycine (Gly), alanine (Ala), hydroxyproline (Hyp) and proline (Pro). Consequently, the resultsindicate that high pressure could enhance the placental hydrolyzing activities of the selected proteases and the optimumpressure levels at which the maximum protease activity is around 200 MPa.

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