Study On Activity Of Pectinase And Hemicellulase And Purification Of Pectinase Secreted From CXJZ95-198 Strain

The thesis studied the total exocellular proteins, reductant sugar and the pectinase enzyme activity of CXJZ95-198 strain in glucose, mannose, xylan, mannosan and pectin culture media.Compared enzyme activity of pectinase, xylanose and β-mannanose. The secreted proteins in ferment fluid from different culture media were analysed by SDS-PAGE electrophoresis. A pectinase from CXJZ95-198 was purified. Results have made know: (1) The changes of protein content secreted by CXJZ95-198 in the five media glucose mannose xylan mannosan and pectin were 1.28mg/ml, 1.17mg/ml, 0.94mg/ml, 0.75mg/ml and 0.73mg/ml.The pectinase activity was maximum in the mannose (79.39U/ml) with the order of glucose(73.33 U/ml) mannosan(24.25 U/ml) xylan(17.45 U/ml) and pectin(15.98 U/ml). (2) In mannose medium the β-mannanose activity is the most supreme (85.55 U/ml), the prectinase activity(73.39 U/ml) is take second place,the xylanose activity(17.91 U/ml) is third. (3) By the analysis of SDS-PAGE electrophoresis, CXJZ95-198 secrets exocellular proteins bands (include protein subunit) in media of glucose, mannose ,xylan, mannosan and pectin respective were 32 bands, 33 bands,35 bands, 36 bands and 21 bands respectively . The colour of most detected bands became light in the five media with the order of mannosan, mannose, xylan, glucose and pectin. (4)The pectinase in the supernatant was purified by centrifuge , acetone precipitation and sephadex G-75 cloumngel filtration. The specific activity was increased 9.8-fold with an activity recovery of 32.98% .The molecular weight of pectinase was 42.2KD estimated by SDS-PAGE.