Food Science of Animal Resources (한국축산식품학회지)

Korean Society for Food Science of Animal Resources (한국축산식품학회)
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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)
  • Received : 2013.05.08
  • Accepted : 2013.07.22
  • Published : 2013.08.31
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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.

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References

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