AI Article Synopsis
- The study focused on the subtilase SR5-3 from Halobacillus sp., a bacterium from salt-rich environments like Thai fish sauce, examining its role as a halophilic serine protease.
- Researchers analyzed how the size and structure of different substrates affect the enzyme's activation in salt conditions, using specific peptide substrates for their experiments.
- Findings indicated that the salting out effect contributes to SR5-3's halophilic properties, with its hydrolytic activity linked to the substrate's characteristics, particularly in relation to their fit in the enzyme's active sites.
Article Abstract
The secreted extracellular subtilase SR5-3 from Halobacillus sp. bacterium, isolated from the high-salt environment of Thai fish sauce, was utilized as a model halophilic serine protease. The dependence of salt activation on the size and structure of substrates was evaluated assaying the enzyme with Suc-AAPF-MCA and with the Fluorescence Resonance Energy Transfer (FRET) peptide Abz-AAPFSSKQ-EDDnp. Solvent isotope effects (SIE) and the thermodynamic parameters for activation of the hydrolysis of Suc-AAPF-MCA and Abz-AAPFSSKQ-EDDnp by SR5-3 protease in the presence of salts were also performed. All the obtained results support the notion that the salting out effect is responsible for the halophilic character of SR5-3, and the magnitude of its hydrolytic activity is mainly derived from the improvement of catalytic and/or interaction steps depending on the nature and size of the substrates, principally if they occupy the substrate prime subsites.
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| http://dx.doi.org/10.1016/j.bbapap.2008.10.017 | DOI Listing |
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