توجه: محتویات این صفحه به صورت خودکار پردازش شده و مقاله‌های نویسندگانی با تشابه اسمی، همگی در بخش یکسان نمایش داده می‌شوند.
۱The role of enzymes and quantum dots in the making biosensor
نویسنده(ها): ، ،
اطلاعات انتشار: دومین کنفرانس بین المللی و سومین همایش ملی کاربرد فناوری های نوین در علوم مهندسی، سال
تعداد صفحات: ۵
Rapid and sensitive method ologies for the detection of protein are in urgent requirement for clinicdi– agnostics. Localized surface plasmon resonance (LSPR) of metal nano structures has the potential to circumvent this problem due to its sensitive optical properties and strong electro magnetic near–field enhancements. In this work, an enzyme medi at edplasmonic biosensor on the basis of adual–functional nano hybrid was developed for the detection of thrombin. Enzymes, like glucose oxidase and catalase, were modified with pyrene function–alities and then loaded into the graphene nanodots encaged porous gold electrode via non–covalent stacking interaction between pyrene and graphene..<\div>

۲Application of different enzyme in detergents
اطلاعات انتشار: دومین کنفرانس بین المللی و سومین همایش ملی کاربرد فناوری های نوین در علوم مهندسی، سال
تعداد صفحات: ۵
Alkaline crude enzymes from the viscera of the Tunisian barbel (Barbus callensis) were extracted and characterized. Proteolytic crude extract from barbel viscera was active and stable in alkaline solution. The crude alkaline proteases showed stability towards various surfactants, bleach agents and compatibility with some commercial detergents. Alkaline proteases from the viscera of the barbel were tested in chicken feather–degradation and showed important feather degrading activity. The lipase showed optima activity at pH 8.5 and 20 ◦C. The lipase activity was activated by metal ions, such as Ca2+ and Mn2+, and surfactants, such as Tween 80, Tween 20, sodium dodecyl benzene sulfonate and urea. Oxidising agents, such as H2O2 and NaClO, were found to have little effect on the activity of the lipase, and most organic solvents can enhance the activity of the lipase. The optimum temperature for enzyme activity was 60 ◦C, and the activity and stability of trypsin was highly dependent on the presence of calcium ion. At 60 ◦C, Ca2+ (5 mM) stimulated the protease activity by 220%. The trypsin kinetic constants, Km and kcat, were 0.312 mM and 2.03 s−1. The enzyme showed high stability towards non–ionic surfactants and oxidizing agent. In addition, the enzyme showed excellent stability and compatibility with some commercial solid and liquid detergents.<\div>

۳Effect of enzymes and PH on thecancer drug delivery
اطلاعات انتشار: دومین کنفرانس بین المللی و سومین همایش ملی کاربرد فناوری های نوین در علوم مهندسی، سال
تعداد صفحات: ۴
The enoyl acyl–carrier protein reductase (ENR) enzyme of the apicomplexan parasite family has been intensely studied for antiparasitic drug design for over a decade, with the most potent inhibitors targeting the NAD+ bound form of the enzyme.Proteins, peptides and nucleic acids are commonly isolated and purified in almost all bioscience laboratories. Methods based on molecular recognition are currently the most powerful tool in separation processes due to their selectivity and recovery. The aim of this study was to prove the versatility and the ability of an affinity carrier containing the immobilised ligand oracin (previously developed by our workgroup) to selectively bind carbonyl–reducing enzymes. These enzymes play an important role in metabolic pathways of various endogenic compounds and xenobiotics. Many important drugs, such as doxorubicin, daunorubicin, haloperidol and the model anticancer drug oracin, are metabolised by carbonyl– reducing enzymes.<\div>
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