مقالههای Gholamreza Farnoosh
توجه: محتویات این صفحه به صورت خودکار پردازش شده و مقالههای نویسندگانی با تشابه اسمی، همگی در بخش یکسان نمایش داده میشوند.
اطلاعات انتشار: Journal of Applied Biotechnology Reports، اول،شماره۱، Winter ۲۰۱۴، سال ۰
تعداد صفحات: ۱۰
Organophosphorus chemicals are compounds which have been used as pesticides and insecticides in agriculture. They’re also used as nervous agents and have raised many problems for human and environment. Among the most important methods of decontamination from these compounds are biodegradation methods. Using OPH enzyme in degradation the mentioned compounds is seen as one of the desirable ways, but low activity and specification and low thermostability are among factors significantly decreasing the optimal application of this enzyme. Using methods of protein engineering based on the alteration of specific protein positions in order to improve the activity, specification and thermostability are some common ways used currently. Numerous studies have been done to increase activity and thermostability of OPH enzyme with alteration of some special amino acids the result of which was an increase against different substrates. OPH enzyme active site connected to substrates that consisted of three large, small and releasing packets were one of the goal areas of changing amino acids used by researchers to improve engineered activities. Among other ways of making enzymes more rigid and stable were bending loops by replacing Proline, creating disulfide bonds, ionic bonds by replacing charged amino acids.
۲Enzymatic Degradation of Organophosphate Compounds: Evaluation of High–level Production, Solubility and Stability
نویسنده(ها): Gholamreza Farnoosh، Ali Mohammad Latifi، Khosro Khajeh، Hossein Aghamollaei، Ali Najafi
اطلاعات انتشار: Journal of Applied Biotechnology Reports، دوم،شماره۴، Autumn ۲۰۱۵، سال ۰
تعداد صفحات: ۶
The use of organophosphorus hydrolase (OPH) enzyme to degrade Chemical Warfare Agents is one of the most frequently used decontamination methods. OPH is a ~36 kDa homodimeric metalloprotein that is found in the membrane of Flavobacterium sp. strain ATCC 27551 and Brevundimonas diminuta MG and is capable of hydrolyzing a wide range of oxon and thion , such as paraoxon and parathion. OPH gene (opd) has been expressed in many hosts, such as bacteria, insect cells, fungi, and Streptomyces spp. High level and soluble expression and correct folding of each protein are of important factors. Fusion proteins, including TRX, Gb1 and MBP, are commonly used to increase solubility, folding and in some cases, stability. The present study evaluated thioredoxin (TRX) role in OPH expression level, solubility and stability by cloning the opd gene into pET32a and pET21a and expressing the resulting vectors in E. coli shuffle T7. The pET32a vector encodes a fusion protein containing TRX that is not present in the pET21a. The results revealed an increased expression level, solubility and stability in OPH produced by the pET32a–opd construct compared to the pET21a vector due to the presence of the TRX fusion in pET32a vector.
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