| 초록 |
Protease inhibitors have been usually isolated through a number of steps using various chromatographical methods, which are time consuming and tedious. In this study, an efficient and low-cost polyacrylamide affinity gel electrophoresis (PAAGE) method for the detection and isolation of chymotrypsin inhibitor from a crude extract was studied. The affinity gel was obtained by immobilization of chymotrypsin on 5% (w/v) poly acrylamide-oleic acid gel, and the affinity gel was applied to PAAGE and reverse electrode electro-elution using a modified commercial electrophoresis kit. PAAGE method showed higher isolation efficiency for chymotrypsin inhibitor from Ganoderma lucidum crude extract than a chromatographical method. Specific activity and yield of chymotrypsin inhibitor increased compared with a chromatographical method. Also, two isomers of the inhibitor could be isolated by this method. |
