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http://dx.doi.org/10.5851/kosfa.2013.33.4.474

Effects of High Pressure/High Temperature Processing on the Recovery and Characteristics of Porcine Placenta Hydrolysates  

Lee, Mi-Yeon (Department of Food Science and Biotechnology of Animal Resources, Konkuk University)
Choi, Ye-Chul (Department of Food Science and Biotechnology of Animal Resources, Konkuk University)
Chun, Ji-Yeon (Department of Food Science and Biotechnology of Animal Resources, Konkuk University)
Min, Sang-Gi (Department of Bio-Industrial Technologies, Konkuk University)
Hong, Geun-Pyo (Department of Bio-Industrial Technologies, Konkuk University)
Publication Information
Food Science of Animal Resources / v.33, no.4, 2013 , pp. 474-480 More about this Journal
Abstract
This study was performed to investigate the effects of high pressure/high temperature (HPHT) treatment on the recovery efficiency and characteristics of porcine placenta hydrolysates. The placenta hydrolysates were characterized by solubility, free amino acid contents, gel electrophoresis, gel permeation chromatography (GPC) and amino acid composition. Placenta was treated at 37.5 MPa of pressure combined with various temperatures (150, 170, and $200^{\circ}C$) or various holding times (0, 30, and 60 min at $170^{\circ}C$). Insoluble raw placenta collagen was partially solubilized (> 60% solubility) by the HPHT treatment. Free amino group content of placenta collagen was increased from 0.1 mM/g collagen to > 0.3 mM/g collagen after HPHT treatment, reflecting partial hydrolysis of collagen. The molecular weight ($M_w$) distribution showed evidence of collagen hydrolysis by shifting of $M_w$ peaks toward low molecular weight when treated temperature or holding time was increased. Alanine (Ala), glycine (Gly), hydroxyproline (Hyp), and proline (Pro) contents increased after the HPHT treatments compared to a decrease in the others. In particular, the increase in Gly was obvious, followed by Hyp and Pro, reflecting that placenta hydrolysates were mainly composed of these amino acids. However, increasing temperature or holding time hardly affected the amino acid compositions. These results indicate that the HPHT treatment is advantageous to hydrolyze collagen derived from animal by-products.
Keywords
high pressure; high temperature; subcritical water; placenta collagen; hydrolysis;
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1 Ahmad, M., Benjakul, S., and Nalinanon, S. (2010) Compositional and physicochemical characteristics of acid solubilized collagen extracted from the skin of unicorn leatherjacket (Aluterus monoceros). Food Hydrocolloid. 24, 588-594.   DOI   ScienceOn
2 Amashukeli, X., Pelletier, C. C., Kirby, J. P., and Grunthaner, F. J. (2007) Subcritical water extraction of amino acids from Atacama Desert soils. J. Geophys. Res. 112, G04S16.   DOI
3 AOAC. (1990) Official methods of analysis. 15th ed, Association of Official Analytical Chemists, Washington, DC.
4 Benjakul, S. and Morrissey, M. T. (1997) Protein hydrolysates from pacific whiting solid wastes. J. Agric. Food Chem. 45, 3423-3430.   DOI   ScienceOn
5 Brunner, G. (2009) Near critical and supercritical water. Part I. Hydrolytic and hydrothermal processes. J. Supercritical Fluid. 47, 373-381.   DOI   ScienceOn
6 Denis, A., Brambati, N., Dessauvages, B., Guedj, S., Ridoux, C., Meffre, N., and Autier, C. (2008) Molecular weight determination of hydrolyzed collagens. Food Hydrocolloid. 22, 989-994.   DOI   ScienceOn
7 Dunn, M. S. and Brophy, T. W. (1932) Decomposition points of the amino acids. J. Biol. Chem. 99, 221-229.
8 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.   DOI   ScienceOn
9 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 (Salmo salar L.) skin. Food Res. Int. 44, 1536-1540.   DOI   ScienceOn
10 Kim, B. Y., Kim, T., Kang, W. Y., Hyun, B., Cheon, H. Y., and Kim, D. (2010) Functional cosmetic effect of porcine placenta. Korean Chem. Eng. Res. 48, 327-331.
11 Klomklao, S., Benjakul, S., Visessanguan, W., Kishimura, H., and Simpson, B. K. (2006) Proteolytic degradation of sardine (Sardinella gibbosa) proteins by trypsin from skipjack tuna (Katsuwonus pelamis) spleen. Food Chem. 98, 14-22.   DOI   ScienceOn
12 Laemmli, U. K. (1970) Cleavage of structural proteins during assembly of head of bacteriophage T4. Nature 227, 680-685.   DOI   ScienceOn
13 Liu, D., Liang, L., Regenstein, J. M., and Zhou, P. (2012) Extraction and characterization of pepsin-solubilised collagen from fins, scales, skins, bones and swim bladders of bighead carp (Hypophthalmichthys nobilis). Food Chem. 133, 1441-1448.   DOI   ScienceOn
14 Miller, E. J. (1988) Collagen types: Structure, distribution, and functions. In: Collagen. Nimni, M. E. (ed) Boca Raton, CRC Press, Boca Raton, 1, pp. 139-156.
15 Montero, P. and Gomez-Guillen, M. C. (2000) Extracting conditions for megrim (Lepidorhombus boscii) skin collagen affect functional properties of the resulting gelatin. J. Food Sci. 65, 434-438.   DOI   ScienceOn
16 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.   DOI   ScienceOn
17 Nalinanon, S., Benjakul, S., Kishimura, H., and Osako, K. (2011) Type I collagen from the skin of ornate threadfin bream (Nemipterus hexodon): Characteristics and effect of pepsin hydrolysis. Food Chem. 125, 500-507.   DOI   ScienceOn
18 Nimni, M. E. and Harkness, R. D. (1988) Molecular structure and functions of collagen. In: Collagen. Nimni, M. E. Boca Raton, CRC Press, 1, 1-77.
19 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.   DOI   ScienceOn
20 Sunphorka, S., Chavasiri, W., Oshima, Y., and Ngamprasertsith, S. (2012) Kinetic studies on rice bran protein hydrolysis in subcritical water. J. Supercritical Fluid. 65, 54-60.   DOI   ScienceOn
21 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.
22 Zhu, G., Zhu, X., Fan, Q., and Wan, X. (2011) Recovery of biomass wastes by hydrolysis in sub-critical water. Resour. Conserv. Recy. 55, 409-416.   DOI   ScienceOn