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Effect of Sub- and Super-critical Water Treatment on Physicochemical Properties of Porcine Skin

  • Jo, Yeon-Ji ;
  • Kim, Jae-Hyeong ;
  • Jung, Kyung-Hun ;
  • Min, Sang-Gi ;
  • Chun, Ji-Yeon
  • Received : 2014.09.24
  • Accepted : 2014.10.23
  • Published : 2015.02.28

Abstract

Super- and sub-critical water treatments have been of interest as novel methods for protein hydrolysis. In the present study, we studied the effect of sub-critical water (Sub-$H_2O$, $300^{\circ}C$, 80 bar) treatment as well as super-critical water (Super-$H_2O$, $400^{\circ}C$, 280 bar) treatment on the physicochemical properties of porcine skin (PS), which has abundant collagen. Porcine skin was subjected to pre-thermal treatment by immersion in water at $70^{\circ}C$, and then treated with sub- or super-critical water. Physicochemical properties of the hydrolysates, such as molecular weight distribution, free amino acid content, amino acid profile, pH, color, and water content were determined. For the molecular weight distribution analysis, 1 kDa hydrolyzed porcine skin (H-PS) was produced by Super-$H_2O$ or Sub-$H_2O$ treatment. The free amino acid content was 57.18 mM and 30.13 mM after Sub-$H_2O$ and Super-$H_2O$ treatment, respectively. Determination of amino acid profile revealed that the content of Glu (22.5%) and Pro (30%) was higher after Super-$H_2O$ treatment than after Sub-$H_2O$ treatment, whereas the content of Gly (28%) and Ala (13.1%) was higher after Sub-$H_2O$ treatment. Super-$H_2O$ or Sub-$H_2O$ treatment affected the pH of PS, which changed from 7.29 (Raw) to 9.22 (after Sub-$H_2O$ treatment) and 9.49 (after Super-$H_2O$ treatment). Taken together, these results showed that Sub-$H_2O$ treatment was slightly more effective for hydrolysis than Super-$H_2O$ was. However, both Sub-$H_2O$ and Super-$H_2O$ treatments were effective processing methods for hydrolysis of PS collagen in a short time and can be regarded as a green chemistry technology.

Keywords

sub-critical water;super-critical water;porcine skin;collagen;hydrolysates

References

  1. Mosquera, M., Giménez, B., da Silva, I. M., Boelter, J. F., Montero, P., Gómez-Guillén, M. C., and Brandelli, A. (2014) Nanoencapsulation of an active peptidic fraction from sea bream scales collagen. Food Chem. 156, 144-150. https://doi.org/10.1016/j.foodchem.2014.02.011
  2. Shigemura, Y., Akaba, S., Kawashima, E., Park, E. Y., Nakamura, Y., and Sato, K. (2011) Identification of a novel foodderived collagen peptide, hydroxyprolyl-glycine, in human peripheral blood by pre-column derivatisation with phenyl isothiocyanate. Food Chem. 129, 1019-1024. https://doi.org/10.1016/j.foodchem.2011.05.066
  3. Watchararuji, K., Goto, M., Sasaki, M., and Shotiprunk, A. (2008) Value-added subcritical water hydrolysate from rice bran and soybean meal. Bioresour. Technol. 99, 6207-6213. https://doi.org/10.1016/j.biortech.2007.12.021
  4. Zhang, Z., Li, G., and Shi, B. (2006) Physicochemical properties of collagen, gelatin and collagen hydrolysate derived from bovine limed split wastes. J. Society Leather Technol. Chem. 90, 23-28.
  5. Jung K. H., Choi, Y. C., Chun, J. Y., Min, S. G., and Hong, G. P. H. (2014) Effects of concentration and reaction time of trypsin, pepsin, and chymotrypsin on the hydrolysis efficiency of porcine placenta. Korean J. Food Sci. An. 34, 151-157. https://doi.org/10.5851/kosfa.2014.34.2.151
  6. 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. https://doi.org/10.5851/kosfa.2013.33.4.474
  7. Ravber, M., Knez, Ž., and Škerget, M. (2015) Simultaneous extraction of oil- and water-soluble phase from sunflower seeds with subcritical water. Food Chem. 166, 316-323. https://doi.org/10.1016/j.foodchem.2014.06.025
  8. Nagarajan, M., Benjakul, S., Prodpran, T., Songtipya, P., and Kishimura, H. (2012) Characteristics and functional properties of gelatin from splendid squid (loligo formosana) skin as affected by extraction temperatures. Food Hydrocolloid. 29, 389-397. https://doi.org/10.1016/j.foodhyd.2012.04.001
  9. Penninger, J. M. L., Kersten, R. J. A., and Baur, H. C. L. (2000) Hydrolysis of diphenylether in supercritical water: Effects of dissolved nacl. J. Supercrit Fluids. 17, 215-226. https://doi.org/10.1016/S0896-8446(00)00046-2
  10. Rauscher S., Baud S., Miao M., Keeley F. W., and Pomès R. (2006) Proline and glycine control protein self-organization into elastomeric or amyloid fibrils. Structure 14, 1667-1676. https://doi.org/10.1016/j.str.2006.09.008
  11. Sato, N., Daimon, H., and Fujie, K. (2002) Decomposition of glycine in high temperature and high pressure water. Kag. Kog. Ronbunshu. 28, 113-117. https://doi.org/10.1252/kakoronbunshu.28.113
  12. Alargov, D., Deguchi, S., Tsujii, K., and Horikoshi, K. (2002) Reaction behaviors of glycine under super- and subcritical water conditions. Orig Life Evol Biosph. 32, 1-12. https://doi.org/10.1023/A:1013906319253
  13. Benjakul, S. and Morrissey, M. T. (1997) Protein hydrolysates from pacific whiting solid wastes. J. Agric. Food Chem. 45, 3423-3430. https://doi.org/10.1021/jf970294g
  14. Brunner, G. (2014) Supercritical fluid science and technology. Chapter 2. Properties of pure water. Brunner, G. (ed), Elsevier, 5, pp. 9-93.
  15. Brunner, G. (2009) Near critical and supercritical water. Part I. Hydrolytic and hydrothermal processes. J. Supercritical Fluid. 47, 373-381. https://doi.org/10.1016/j.supflu.2008.09.002
  16. Cho, Y. J., Seo, J. E., Kim, Y. J., Lee, N. H., Hong, S. P., and Kim, Y. H. (2006) Study on the degradation of pig skin collagen using irradiation technique. J. Korean. Soc. Food. Sci. Nutr. 35, 588-593. https://doi.org/10.3746/jkfn.2006.35.5.588
  17. Chun, J. Y., Jo, Y. J., Min, S. G., and Hong, G. P. (2014) Effect of high pressure on the porcine placenral hydrolyzing activity of pepsin, trypsin and chymotrypsin. Korean J. Food Sci. An. 34, 14-19. https://doi.org/10.5851/kosfa.2014.34.1.14
  18. Dong, X. B., Li, X., Zhang, C. H., Wang, J. Z., Tang, C. H., Sun, H. M., Jia, W., Li, Y., and Chen, L. L. (2014) Development of a novel method for hot-pressure extraction of protein from chicken bone and the effect of enzymatic hydrolysis on the extracts. Food Chem. 157, 339-346. https://doi.org/10.1016/j.foodchem.2014.02.043
  19. 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. https://doi.org/10.1016/j.foodres.2011.04.006

Cited by

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  2. Fish collagen peptide inhibits the adipogenic differentiation of preadipocytes and ameliorates obesity in high fat diet-fed mice vol.104, 2017, https://doi.org/10.1016/j.ijbiomac.2017.05.151
  3. Characterization of soy protein hydrolysates produced by varying subcritical water processing temperature vol.43, 2017, https://doi.org/10.1016/j.ifset.2017.08.011

Acknowledgement

Supported by : Korea Institute of Planning and Evaluation for Technology