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

被引:12
作者
Lee, Mi-Yeon [2 ]
Choi, Ye-Chul [2 ]
Chun, Ji-Yeon [2 ]
Min, Sang-Gi [1 ]
Hong, Geun-Pyo [1 ]
机构
[1] Konkuk Univ, Dept Bioind Technol, Seoul 143701, South Korea
[2] Konkuk Univ, Dept Food Sci & Biotechnol Anim Resources, Seoul 143701, South Korea
关键词
high pressure; high temperature; subcritical water; placenta collagen; hydrolysis; FUNCTIONAL-PROPERTIES; RICE BRAN; COLLAGEN; SKIN; EXTRACTION; PROTEINS; GELATIN;
D O I
10.5851/kosfa.2013.33.4.474
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
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 degrees C) or various holding times (0, 30, and 60 min at 170 degrees 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.
引用
收藏
页码:474 / 480
页数:7
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