Studies on characteristics of enzymes extracted from chicken proventriculus duodenum pancreas and their effect on porcine fibers.

• Main Authors: Sheu, Suh Rong, 許素容
• Other Authors: Chen Ming-Tsao, Liu Deng-Cheng
• Format: Others
• Language: zh-TW
• Published: 1998
• Online Access: http://ndltd.ncl.edu.tw/handle/47309515598643751160

碩士 === 國立中興大學 === 畜牧學系 === 86 === The purpose of this study was to extract crude enzymes from chicken proventriculus, pancreas and duodenum to determine the activities of pepsin, trypsin and chymotrypsin. On the other hand, to investigate the effect of pH value, salt concentration and temperature on the activity of these enzymes. Finally, these crude enzymes were added into pork loin to study the changes of protein and histology of muscle and used as a reference for an tenderizer from animal in the further. In aspect of the characteristics of enzymes, the activity of pepsin from chicken proventriculus was significantly higher than from duodenum (P<0.05). The activity of trypsin and chymotrypsin from chicken pancreas had the highest value but lowest value was found in chicken duodenum. The relative activity of pepsin from chicken proventriculus and duodenum was the highest at pH 3. The relative activity of crude trypsin from chicken duodenum had higher value at pH 6 but that for chicken pancreas was at pH 9. Otherwise, the relative activity of chymotrypsin from chicken pancreas and duodenum was higher at pH 6. The relative activity of pepsin, trypsin and chymotrypsin decreased with the salt concentration. The optimum temperature of pepsin from chicken proventriculus and duodenum was 60℃. The optimum temperature of trypsin from chicken duodenum and pancreas was 60℃ but that of chymotrypsin from chicken duodenum and pancreas was 50℃. In enzymatic purification, A higher activity of trypsin from pancreas was extracted by a series of steps such as homogenate, centrifuge, 0-75% ammonium sulfate and P-benzamidine-sepharose 6B affinity column and its specific activity and yield was 456.94 units/mg and was 21 %. Also, a higher activity of Chymotrypsin was obtained by S-Sepharose FF column and its specific activity and yield was 25.06 units/mg and 30.14 %. Salmonella in chicken pancreas was inhibited by soaking with 4% lactic acid for 10min . In application of crude pancreas enzyme, pork lion with 10% crude pancreas enzyme powder had better protein degradation than 5% crude enzyme powder by electrophoresis. In the shearing test, the shearing value of pork loin with 5% crude pancreas enzyme powder decreased at 20℃ with the time. However, Myofibrillar of pork loin with 5% crude pancreas enzyme powder broken down with the time by scanning electron micrographs.