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International Journal of Nanoscience and Nanotechnology (IJNN)، جلد ۱۳، شماره ۲، صفحات ۱۸۷-۱۹۴
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عنوان انگلیسی Comparative Studies on the Interaction of ‎Proteinase-K with Fe2O3, Fe3O4 and SiO2 ‎Nanoparticles
چکیده انگلیسی مقاله The interaction of Fe2O3, Fe3O4 and SiO2 nanoparticles with proteinase K activity was investigated using UV–vis spectroscopy. Proteinase K EC (3.4.21.14) is a member of serine protease family, which is produced from fungus Tritirachum album Limber.The effects of nanoparticles on proteinase K activity were studies at 40˚C in pH 7.0 using sodium phosphate as buffer. It was found that in the presence of nano-Fe2O3 and nano-Fe3O4, Vmax was decreased but Km was constant. This results indicated that nano-Fe2O3 and nano-Fe3O4 acted as noncompetitive inhibitors. In the presence of nano-SiO2 the amount of Km increased but Vmax decreased, that showed nano-SiO2 acted as a mixed inhibitor. The dissociation constant (Ki) value for binding nano-Fe2O3, nano-Fe3O4 to proteinase K was equal to 11µM and 8.5µM respectively that indicated the binding of nano-Fe3O4 to the enzyme was stronger than nano-Fe2O3. The KI and Ki value for nano-SiO2 was 22.5µM and 8µM respectively.
کلیدواژه‌های انگلیسی مقاله Proteinase-K, Nanoparticles, Experimental investigation‎
نویسندگان مقاله e یداللهی |
department of biology, university of shahrekord, p.o. box 115, shahrekord, i. r. of ‎iran.‎

b شارقی |
department of biology, university of shahrekord, p.o. box 115, shahrekord, i. r. of ‎iran.‎

m صلواتی نیاسر | salavati niasar
institute of nano science and nano technology, university of kashan, p.o. box 87317-‎‎51167, kashan, i. r. iran.‎
سازمان اصلی تایید شده: دانشگاه کاشان (Kashan university)

نشانی اینترنتی http://www.ijnnonline.net/article_25617_ada075709d1df1471b4761297c505399.pdf
فایل مقاله اشکال در دسترسی به فایل - ./files/site1/rds_journals/423/article-423-401492.pdf
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زبان مقاله منتشر شده en
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