JOURNAL BROWSE
Search
Advanced SearchSearch Tips
Effect of High Pressure on the Porcine Placenral Hydrolyzing Activity of Pepsin, Trypsin and Chymotrypsin
facebook(new window)  Pirnt(new window) E-mail(new window) Excel Download
 Title & Authors
Effect of High Pressure on the Porcine Placenral Hydrolyzing Activity of Pepsin, Trypsin and Chymotrypsin
Chun, Ji-Yeon; Jo, Yeon-Ji; Min, Sang-Gi; Hong, Geun-Pyo;
  PDF(new window)
 Abstract
This study investigated the effects of protease treatments (trypsin, chymotrypsin, and pepsin) under various pressure levels (0.1-300 MPa) for the characteristics of porcine placenta hydrolysates. According to gel electrophoretic patterns, the trypsin showed the best placental hydrolyzing activity followed by chymotrypsin, regardless of the pressure levels. In particular, the peptide bands of tryptic-digested hydrolysate were not shown regardless of applied pressure levels. The peptide bands of hydrolysate treated chymotrypsin showed gradual decreases in molecular weights () with increasing pressure levels. However, the pepsin did not show any evidences of placental hydrolysis even though the pressure levels were increased to 300 MPa. The gel permeation chromatography (GPC) profiles showed that the trypsin and pepsin had better placental hydrolyzing activities under high pressure (particularly at 200 MPa), with lower distributions of the hydrolysates. Pepsin also tend to lower the of peptides, while the major bands of hydrolysates being treated at 300 MPa were observed at more than 7,000 Da. There were some differences in amino acid compositions of the hydrolysates, nevertheless, the peptides were mainly composed of glycine (Gly), alanine (Ala), hydroxyproline (Hyp) and proline (Pro). Consequently, the results indicate that high pressure could enhance the placental hydrolyzing activities of the selected proteases and the optimum pressure levels at which the maximum protease activity is around 200 MPa.
 Keywords
porcine placenta;high pressure;hydrolysates;protease;enzyme activity;
 Language
English
 Cited by
1.
Effect of Sub- and Super-critical Water Treatment on Physicochemical Properties of Porcine Skin,;;;;;

한국축산식품학회지, 2015. vol.35. 1, pp.35-40 crossref(new window)
1.
Effect of Sub- and Super-critical Water Treatment on Physicochemical Properties of Porcine Skin, Korean Journal for Food Science of Animal Resources, 2015, 35, 1, 35  crossref(new windwow)
 References
1.
Chicon, R., Lopez-Fandino, R., Alonso, E., and Belloque, J. (2008) Proteolytic pattern, antigenicity, and serum immunoglobin E binding of $\beta$-lactoglobulin hydrolysates obtained by pepsin and high-pressure treatments. J. Dairy Sci. 91, 928-938. crossref(new window)

2.
Clemente, A. (2000) Enzymatic protein hydrolysates in human nutrition. Trend. Food Sci. Technol. 11, 254-262. crossref(new window)

3.
Dunn, B. M. (2001) Overview of pepsin-like aspartic peptidases. Curr. Prot. Protein Sci.unit 21.3, 1-6.

4.
Furthmayr, H. and Timpl, R. (1971) Characterization of collagen peptides by sodium dodecylsulfate-polyacrylamide electrophoresis. Anal. Biochem. 41, 510-516. crossref(new window)

5.
Gimenez, B., Alemán, A., Montero, P., and Gomez-Guillen, M. C. (2009) Antioxidant and functional properties of gelatin hydrolysates obtained from skin of sole and squid. Food Chem. 114, 976-983. crossref(new window)

6.
Gomez-Guillen, M. C., Gimenez, B., Lopez-Caballero, M. E., and Montero, M. P. (2011) Functional and bioactive properties of collagen and gelatin from alternative sources: A review. Food Hydrocolloid 25, 1813-1827. crossref(new window)

7.
Gu, R. Z., Li, C. Y., Liu, W. Y., Yi, W. X., and Cai, M. Y. (2011) Angiotensin I-converting enzyme inhibitory activity of low-molecular-weight peptides from Atlantic salmon (Salmosalar L.) skin. Food Res. Int. 44, 1536-1540. crossref(new window)

8.
Iwai, K., Hasegawa, T., Taguchi, Y., Morimatsu, F., Sato, K., Nakamura, Y., Higashi, A., Kido, Y., Nakabo, Y., and Ohtsuki, K. (2005) Identification of food-derived collagen peptides in human blood after oral ingestion of gelatin hydrolysates. J. Agric. Food Chem. 53, 6531-6536. crossref(new window)

9.
Johnston, N., Dettmar, P. W., Bishwokarma, B., Lively, M. O., and Kouffman, J. A. (2001) Activity/stability of human pepsin: implications for reflux attributed laryngeal disease. Laryngoscope 117, 1036-1039.

10.
Laemmli, U. K. (1970) Cleavage of structural proteins during assembly of head of bacteriophage T4. Nature 227, 680-685. crossref(new window)

11.
Lee, M. Y., Choi, Y. C., Chun, J. Y., Min, S. G., and Hong, G. P. (2013) Effects of high pressure/high temperature processing on the recovery and characteristics of porcine placenta hydrolysayes. Korean J. Food Sci. An. 33, 474-480. crossref(new window)

12.
Nelson,D. R. and Cox, M. M. (2008) Lehninger principles of biochemistry. 5th ed, W. H. Freeman, San Francisco, pp. 183-234.

13.
Northrop, D. B. (2002) Effects of high pressure on enzymatic activity. Biochim.Biophys.Acta. 1595, 71-79. crossref(new window)

14.
Penas, E., Prestamo, G., Baeza, M. L., Martínez-Molero, M. I., and Gomez, R. (2006) Effects of combined high pressure and enzymatic treatments on the hydrolysis and immunoreactivity of dairy whey proteins. Int. Dairy J. 16, 831-839. crossref(new window)

15.
Peñas, E., Prestamo, G., and Gomez, R. (2004) High pressure and the enzymatic hydrolysis of soybean whey proteins. Food Chem. 85, 641-648. crossref(new window)

16.
Rodriguez, J., Gupta, N., Smith, R. D., and Pevzner, P. A. (2008) Does trypsin cut before proline? J. Proteome. 7, 300-305. crossref(new window)

17.
Ruan, K., Lange, R., Bec, N., and Balny, C. (1997) A stable partly denatured state of trypsin induced by high hydrostatic pressure. Biochem. Biophys. Res. Commun. 239, 150-154. crossref(new window)

18.
Skierka, E. and Safdowska, M. (2007) The influence of different acids and pepsin on the extractability of collagen from the skin of Baltic cod (Gadusmorhua). Food Chem. 105, 1302-1306. crossref(new window)

19.
Suzuki, A., Watanabe, M., and Ikeuchi, Y. (1993) Effects of high-pressure treatment on the ultrastructure and thermal behavior of beef intramuscular collagen. Meat Sci. 35, 17-25. crossref(new window)

20.
Szpak, P. (2011) Fish bone chemistry and ultrastructure: implications for taphonomy and stable isotope analysis. J. Archaeol. Sci. 38, 3358-3372. crossref(new window)

21.
Tsugita, A. and Scheffler, J. J. (1982) A rapid method for acid hydrolysis of protein with a mixture of trifluoroacetic acid and hydrochloric acid. Eur. J.Biochem. 124, 585-588.