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Fig. 6 | Microbial Cell Factories

Fig. 6

From: Structural and functional characterization of a novel cold-active S-formylglutathione hydrolase (SfSFGH) homolog from Shewanella frigidimarina, a psychrophilic bacterium

Fig. 6

Stability of SfSFGH. a Thermal unfolding of SfSFGH was monitored at 222 nm from 20 to 90 °C using far-UV CD measurements. b Intrinsic fluorescence spectra were recorded with increasing concentrations of urea from 0 to 5 M. c Chemical stability of SfSFGH. Residual activities were measured after incubation of the enzyme for 1 h in various conditions. Effects of SDS (d) and urea (e) on the enzymatic activity of SfSFGH. All experiments were performed in triplicate

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Microbial Cell Factories

ISSN: 1475-2859

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