2014
DOI: 10.1016/j.procbio.2014.03.007
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Purification and characterization of solvent stable, alkaline protease from Bacillus firmus CAS 7 by microbial conversion of marine wastes and molecular mechanism underlying solvent stability

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Cited by 66 publications
(40 citation statements)
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“…By contrast, the proteases were noted to be partially deactivated by ethyl acetate, which was previously reported to be a quite harmful polar aprotic solvent to other solvent-stable proteases from P. aeruginosa CTM50182 [7] and B. licheniformis RSP-09-37 [40]. In media containing organic solvents, enzyme deactivation could presumably be due to the disruption of the protein molecule hydrophobic core due to the change of medium hydrophobicity [41,42]. In particular, polar solvents (such as ethyl acetate), which can penetrate into the protein, are more capable of inducing structural changes for the interaction between the active site and substrate than non-polar solvents, as previously reported by Serdakowski and Dordick [43].…”
Section: Effects Of Organic Solvents On Protease Activity and Stabilimentioning
confidence: 84%
“…By contrast, the proteases were noted to be partially deactivated by ethyl acetate, which was previously reported to be a quite harmful polar aprotic solvent to other solvent-stable proteases from P. aeruginosa CTM50182 [7] and B. licheniformis RSP-09-37 [40]. In media containing organic solvents, enzyme deactivation could presumably be due to the disruption of the protein molecule hydrophobic core due to the change of medium hydrophobicity [41,42]. In particular, polar solvents (such as ethyl acetate), which can penetrate into the protein, are more capable of inducing structural changes for the interaction between the active site and substrate than non-polar solvents, as previously reported by Serdakowski and Dordick [43].…”
Section: Effects Of Organic Solvents On Protease Activity and Stabilimentioning
confidence: 84%
“…But, SPTC were found to be notdeactivated by ethyl acetate as STAP which was previously reported to be a quite harmful polar aprotic solvent to other solventstable proteases from Pseudomonas aeruginosa strain CTM50182 [35] and Bacillus licheniformis strain RSP-09-37 [52]. In media containing organic solvents, enzyme deactivation could presumably be due to the disruption of the protein molecule hydrophobic core due to the change of medium hydrophobicity [53,54]. In particular, polar solvents (such as ethyl acetate), which can penetrate into the protein, are more capable of inducing structural changes for the interaction between the active site and substrate than non-polar solvents, as previously reported by Serdakowski and Dordick [55].…”
Section: Effects Of Organic Solvents On Protease Activity and Stabilimentioning
confidence: 87%
“…In addition, a cellulase synthesized by B. flexus exhibited ~70% of its maximum activity at 15% NaCl (Trivedi et al, 2011). Furthermore, both a cellulase synthesized by B. licheniformis AU01 and a protease synthesized by Bacillus firmus CAS7 have been reported to show high activities even on 30% NaCl (Annamalai et al, 2011(Annamalai et al, , 2014. In this study, a newly isolated TK3-Y strain could grow on 17.5% NaCl, and its enzymes had maximum activities at 17.5% NaCl.…”
mentioning
confidence: 69%