Fusarium oxysporum, pectinesterase

In further work on this series, the same methods were used for the examination of the action pattern of highly purified pectinesterase produced by Fusarium oxysporum f. sp. vasinfectum.49 This pectinesterase was found to affect highly esterifled pectin by a mechanism similar to that of tomato pectinesterase, that is, more than half of the enzymic activity occurred at the reducing ends of the molecules, and the rest attacked a different locus or loci of the pectin chains. These conclusions were supported by a comparison of the effect of clostridial lyase on pectin partly de-esterified in an alkaline solution with its effect on pectin partly de-esterified by Fusarium oxysporum pectinesterase. The lyase did not act on the randomly... 

Miller and Macmillan [4] carried out purification of pectinesterase from Fusarium oxysporum f. sp. vasinfectum culture fluid (fivefold degree of purification). According to the obtained data the purified enzyme possessed very low polygalacturonatlyase one. Disk electrophoresis at pH 4.3 revealed two protein components. The authors did not study distribution of pectinesterase activity in these components. Molecular weight of fungal pectinesterase determined using gel — filtration on Sefadex G — 75 was found to be 35,000. 

Miller and Macmillan49 purified pectinesterase produced by Fusarium oxysporum f. sp. vasinfectum by chromatography on DEAE-Sephadex A-25, Sephadex G-75, CM-Sephadex C-50, and CM-cellulose. The homogeneity of the pectinesterase obtained was confirmed by disc electrophoresis an apparent molecular weight of 35,000 was estimated by its behavior on a column of Sephadex G-75 (Superfine). 

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