Effects of Concentration and Reaction Time of Trypsin, Pepsin, and Chymotrypsin on the Hydrolysis Efficiency of Porcine Placenta

• 발행기관: 한국축산식품학회
• 저자명: Kyung Hun Jung Ye Chul Choi Ji Yeon Chun Sang Gi Min Geun Pyo Hong
• 간행물 정보: 『Food Science of Animal Resources』Korean Journal for Food Science of Animal Resources 제34권 제2호, 151~157쪽, 전체 7쪽
• 주제분류: 농수해양 > 식품과학
• 파일형태: PDF
• 발행일자: 2014.04.30

영문 초록

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°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°C) of raw placenta improved the efficiency of tryptic digestions to a greater level than that of a preheating treatment (90°C for 1 h). Consequently, subcritical water processing followed by enzymatic digestions has the potential of an advanced collagen hydrolysis technique.

키워드

porcine placenta collagen peptide hydrolysis protease efficiency