Current location - Recipe Complete Network - Healthy recipes - Why can fungi synthesize pectase?
Why can fungi synthesize pectase?

Pectin is the main component of heteropolysaccharides in plant cell walls. It is composed of galacturonic acid with different degrees of esterification polymerized by α-1,4 glycosidic bonds. Pectinase can effectively degrade it Pectin substances mainly include pectinesterase, polygalacturonase and pectin lyase. Pectinase can be used in the extraction and clarification of fruit and vegetable juices and hardening of fruits and vegetables in the food industry, and can also be used in feed The industry uses it as a feed additive to relieve the anti-nutritional effects of pectin, and it is also used in the softening of cloth in the textile industry and papermaking. On the one hand, this study uses microorganisms from different environmental sources as experimental materials to obtain multiple pectinase genes for Candidate enzymes are provided for different industrial needs; on the other hand, polygalacturonase with high specific activity obtained in the laboratory is used as a material to improve it through site-directed mutation to enhance its industrialization potential. From food processing wastewater A pectin methylesterase gene pe8F46 was obtained from Penicillium chrysogenum F46 and was successfully expressed in Pichia pastoris. The optimal pH of the recombinant enzyme PE8F46 is 5.0 and the optimal temperature is 40°C. The enzyme has unique low-temperature characteristics and can operate at 10 °C can also maintain an activity of 52. In the hardening experiment of pineapple blocks, 0.75 PE8F46 and 0.4 calcium lactate*** were treated together for 20 minutes, and the hardness increased by 47.6, which was higher than the same commercial complex enzyme by 13.7. From the source Two endopolygalacturonase genes (AM-pg I and AM-pg II) and one exopolygalacturonase gene (AM- pg III), and was successfully expressed in P. pastoris. The optimal temperature of the recombinant enzyme AM-PG I is 50°C, the optimal pH is 5.0, and the specific activity is higher than that of the currently reported endopolygalacturonase. , is 40,123U/mg