USE OF GEL-FILTRATION FOR ISOLATION OF PURE NISIN FROM COMMERCIAL PRODUCTS

  • 1 January 1976
    • journal article
    • research article
    • Vol. 25  (1) , 71-77
Abstract
Commercial nisin was fractionated using a Bio-Gel P-10 column and ion-exchange chromatography on CM-Sephadex C-25. Pure nisin having a titer of 40 .times. 106 units/g was obtained. In polyacrylamide-gel electrophoresis the pure nisin gave 3 bands. Heterogeneity of nisin may be due to the presence of several biological polypeptides. The pure nisin is digested by chymotrypsin but it is not affected by trypsin and pepsin.

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