کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
10129142 1645202 2018 34 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Improve Salinivibrio zinc-metalloprotease function in less polar organic solvents by increasing surface hydrophobicity
ترجمه فارسی عنوان
عملکرد سلینویبریو روی-متالوپروتئازها را در حلال های آلی قطبی کمتری با افزایش هیدروفوبیت سطح
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
چکیده انگلیسی
Organic solvents tend to strip water from protein and thereby disrupt non-covalent forces and decrease enzyme activity and stability. In the present study, we have replaced the surface charge residues in Salinivibrio zinc-metalloprotease (SVP) with hydrophobic ones (E12V, D22I, D24A and D310I) in order to study the effects of surface hydrophobicity with hydrophobic strength of organic solvents. Compared to SVP, D24A exhibited an increase in kcat and catalytic efficiency and a reduction in thermal inactivation rate in aqueous solvent. Structural studies indicated that the replacement of surface charge residues with hydrophobic residues would not induce conformational changes. C50 value (the value of solvent concentration where 50% of enzyme activity remains), ki (irreversible thermoinactivation rate), and kinetic parameters of E12V, D22I, and D24A were higher in isopropanol and n-propanol. D24A is found to be the most efficient mutant for its remarkable decrease in ki value in the presence of isopropanol and n-propanol and a reduction in ki value in the presence of dimethylformamide (DMF) and methanol. C50 value in this variant was increased about 1.2% in DMF, 2% in methanol and isopropanol and 2.5% in n-propanol. Results revealed that, there was a correlation between surface hydrophobicity of SVP and hydrophobic strength of organic solvents.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 120, Part A, December 2018, Pages 440-448
نویسندگان
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