Easy and Rapid Purification of Highly Active Nisin
Figure 3
Bactericidal activity of the various nisin purification fractions. Equal amounts of protein of the different elution fractions (Step I–V) from the purification of commercial nisin (a) and from nisin secreted by the L. lactis NZ9700 strain (b) were run on a tricine-SDS-PA gel and overlaid with nisin-sensitive L. lactis NZ9000 cells (see Section 2). The position of marker proteins with known molecular weight (kDa) are indicated on the left. The growth inhibition zones are visible as dark areas. Lanes I–V represent the five different elution fractions of the cation exchange chromatography. For both purifications, maximum growth inhibition is observed for the Step II elution fraction (400 mM NaCl). Notably, the growth inhibition zone is only visible at a position of ~3.5 kDa.
