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Fig. 4 | Microbial Cell Factories

Fig. 4

From: Enhanced recombinant protein capture, purity and yield from crude bacterial cell extracts by N-Lauroylsarcosine-assisted affinity chromatography

Fig. 4

Purification of a recombinant E. coli β-galactosidase. A Comparative chromatographic profile of mAU signal at 280 nm for affinity chromatography of purification of β-gal-H6 with and without N-L. The corresponding SDS-PAGE coupled to TGX stain free gel Technology (Bio-Rad) of selected elution fractions is also shown. B Circular Dichroism (CD) spectra of β-gal-H6 protein samples purified with the N-L method C Tryptophan fluorescence spectrum of β-gal-H6 protein samples purified with N-L. D Center of Spectral Mass (CSM) of tryptophan fluorescence spectrum of β-gal-H6 samples purified with N-L, versus temperature. Inset: Tm values calculated from a sigmoidal model of CSM vs temperature. E DLS measurements of particle size distribution (by volume) of β-gal-H6 samples. F Thermal profile of β-gal-H6 protein size. G Comparative enzymatic activity of β-gal-H6 samples. Differences were not statistically different (p > 0.05)

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Microbial Cell Factories

ISSN: 1475-2859

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