These experiments were conducted to investigate the purification and some characteristics of potato pullulanse.
1. The crude enzyme was purified by acetic acid fractionation, 20% ethanol fractionation, ammonium sulfate fractionation and DEAE-cellulos...
These experiments were conducted to investigate the purification and some characteristics of potato pullulanse.
1. The crude enzyme was purified by acetic acid fractionation, 20% ethanol fractionation, ammonium sulfate fractionation and DEAE-cellulose column chromatography. The specific activity of the purified enzyme was 0.0726U/mg. protein and yield of enzyme activity was 26.1%.
2. The relative mobility of the purified enzyme on polyacrylamide gel electrophoresis was 0.62.
3. In the early stage of reaction, maltotriose and small amounts of oligosaccharides(hexa-, norna-, and dodecasaccharide) were detected. However, in the later stage of reaction, only maltotriose was detected.
4. The optimum temperature, the optimum pH, the stable pH range and the stable temperature of the purified enzyme were 50℃, pH 6.5, pH 4.5-8.5 and below 40℃, respectively.
5. The purified enzyme was greatly inhibited by Ag+ and Hg2+
6. The purified enzyme hydrolyzed pullulan almost completely, whereas it hydrolyzed amylopectin and soluble starch weakly.