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Figure 4 | Microbial Cell Factories

Figure 4

From: Production and purification of staphylococcal nuclease in Lactococcus lactis using a new expression-secretion system and a pH-regulated mini-reactor

Figure 4

Purification of secreted rNuc protein by cationic exchange chromatography. (A) Ion exchange chromatogram for rNuc purified from the supernatant of strain 918 grown in GM17v. NaCl concentration (brown line) and absorption at 280 nm (blue line) are shown. Fractions analysed by SDS-PAGE are indicated by grey bars underneath. (B) SDS-PAGE analysis of different fractions (E2-11) of the cationic exchange chromatography stained by Coomassie brilliant Blue. MW: Molecular Weight Marker, D: Diluted culture supernatant, FT: Flow Through, W: Washing, E1-12: Elution fractions number 1-12. Secreted rNuc protein (after signal peptide cleavage by signal peptidase) and the mature NucA form (resulting from pro-peptide processing by HtrA surface protease, as previously observed [3]), are indicated by arrows.

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Microbial Cell Factories

ISSN: 1475-2859

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