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논문 기본 정보

자료유형
학술저널
저자정보
Jung, Kyung-Hun (Department of Bio-Industrial Technologies, Konkuk University) Choi, Ye-Chul (Department of Bio-Industrial Technologies, Konkuk University) Chun, Ji-Yeon (Department of Bio-Industrial Technologies, Konkuk University) Min, Sang-Gi (Department of Bio-Industrial Technologies, Konkuk University) Hong, Geun-Pyo (Department of Food Bioengineering, Jeju National University)
저널정보
한국축산식품학회 한국축산식품학회지 한국축산식품학회지 제34권 제2호
발행연도
2014.1
수록면
151 - 157 (7page)

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This study investigated the effects of three proteases (trypsin, pepsin and chymotrypsin) on the hydrolysis efficiency of porcine placenta and the molecular weight (Mw) distributions of the placental hydrolysates. Because placenta was made up of insoluble collagen, the placenta was gelatinized by applying thermal treatment at $90^{\circ}C$ for 1 h and used as the sample. The placental hydrolyzing activities of the enzymes at varying concentrations and incubation times were determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and gel permeation chromatography (GPC). Based on the SDS-PAGE, the best placental hydrolysis efficiency was observed in trypsin treatments where all peptide bands disappeared after 1 h of incubation as compared to 6 h of chymotrypsin. Pepsin hardly hydrolyzed the placenta as compared to the other two enzymes. The Mw distribution revealed that the trypsin produced placental peptides with Mw of 106 and 500 Da. Peptides produced by chymotrypsin exhibited broad ranges of Mw distribution (1-20 kDa), while the pepsin treatment showed Mw greater than 7 kDa. For comparisons of pre-treatments, the subcritical water processing (37.5 MPa and $200^{\circ}C$) of raw placenta improved the efficiency of tryptic digestions to a greater level than that of a preheating treatment ($90^{\circ}C$ for 1 h). Consequently, subcritical water processing followed by enzymatic digestions has the potential of an advanced collagen hydrolysis technique.

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