Extracellular enzymes of Phytophthora infestans: endo-cellulase, -glucosidases, and 1,3-...

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Extracellular enzymes of Phytophthora infestans: endocellulase, -glucosidases, and 1,3--glucanases

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Page 1 ABSTRACT An endo-cellulase, two -glucosidases, and two 1,3--glucanases from Phytophthora infestans were partially purified from the culture filtrate and their biochemical properties determined. The molecular weights were estimated by chromatography on Sephacryl S-200 and were 21 000 (endo-cellulase), 160 000 230 000 and 32 000 (-glucosidases I and II), 160 000 230 000 and 21 000 (-glucanases I and II). The optimal pH of the endocellulase was 6.0. The other enzymes showed the following optimal pH and temperature values: -glucosidase 1,5.5 and 48 C; -glucosidase II, 5.25 and 30 C; 1,3--glucanase 1, 7.0and40 C; and 1,3--glucanase II, 4.5 and 45 C. The -glucosidase II was unstable above 30 C, while the other enzymes remained stable to 43 C. The -glucosidase I did not show MichaelisMenten kinetics for p-nitrophenylglucopyranoside (pNPG) and gentiobiose as substrates. The extrapolated Km value for pNPG was 1.1 mmol/L and the Km value for cellobiose was 280 mmol/L. The Km values of the -glucosidase II were 34 mmol/L for pNPG, 340 mmol/L for cellobiose, and 42 mmol/L for gentiobiose. Finally, the Km value of the 1,3--glucanase II for laminarin was 0.29 g/L. The isoelectric point of the enzymes were 3.2 (endo-cellulase), 3.3 (-glucosidase I), 4.7 (-glucosidase II), and 3.4 (the two 1,3--glucanases). At 10 mmol/L, Cu2+ inhibited the -glucosidase I by 90%, and the -glucosidase II by about 50%. The 1,3-(3-glucanase II was inhibited 75% by Mn2+ and 35% by Cu2+. [less] FULL-TEXT View 0 DOWNLOADS

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http://www.researchgate.net/publication/237193072_Extracellular_enzymes_of_Phytopht... 11-Mar-14