ArticleExtremophiles : life under extreme conditions2014
Effect of organic solvents on the structure and activity of moderately halophilic Bacillus sp. EMB9 protease.
Article in Extremophiles : life under extreme conditions, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 27 citations in OpenAlex.
- Article
- Biophysical characterization of the inactivation of E. coli transketolase by aqueous co-solvents.Scientific reports · 2021Article
- Cloning, Expression, and Structural Elucidation of a Biotechnologically Potential Alkaline Serine Protease From a Newly Isolated HaloalkaliphilicFrontiers in microbiology · 2020Article
- Enhancement of laccase activity by pre-incubation with organic solvents.Scientific reports · 2019Article
- Highly efficient synthesis of arbutin esters catalyzed by whole cells ofRSC advances · 2018Article
- Enhanced Production and Characterization of a Highly Stable Extracellular Protease from an Extreme Halophilic IsolateIranian journal of pharmaceutical research : IJPR · 2018Article
- Medium-based optimization of an organic solvent-tolerant extracellular lipase from the isolated halophilic Alkalibacillus salilacus.Extremophiles : life under extreme conditions · 2015Article
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2 authors at 1 institution in 1 country.
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Abstract
Halophilic enzymes have been manifested for their stability and catalytic abilities under harsh operational conditions. These have been documented to withstand denaturation in presence of high temperature, pH, presence of organic solvents and chaotropic agents. The present study aims at understanding the stability and activity of a halophilic Bacillus sp. EMB9 protease in organic solvents. The protease was uniquely stable in polar solvents. A clear correlation was evident between the protease function and conformational transitions, validated by CD and fluorescence spectral studies. The study affirms that preservation of protein structure, possibly due to charge screening of the protein surface by Ca(2+) and Na(+) ions provides stability against organic solvents and averts denaturation. Salt was also found to exert a protective effect on dialyzed protease against chaotropism of solvents. Presence of 1 % (w/v) NaCl restored the activity in the dialyzed protease and prevented denaturation in methanol, toluene and n-decane. The work will have further implication on discerning protein folding in saline as well as non-aqueous environments.
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