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کاربرد نوع شرط:
- جایگاه : پژوهشی
- مجله: Progress in Biological Sciences
- نوع مقاله: Journal Article
- کلمات کلیدی: Canola,Synthetic Gene,Glyphosate tolerance,Gene optimization,Glyphosate oxidoreductase
- چکیده:
- چکیده انگلیسی: The engineering of transgenic canola (Brassica napus L. ) to make tolerance to the broad-spectrum herbicide, glyphosate, is one of the most effective approaches for weed management. Glyphosate inhibits the enzyme EPSPS (5-enolpyruvylshikimate-3-phosphate synthase) enzyme which functions in the shikimate pathway and has a key role in biosynthesis of aromatic amino acids required for survival of the plant. Induction of glyphosate tolerance in transgenic canola via introducing mutated epsps to the plant genome has been previously reported. By this strategy, enzyme’s affinity for glyphosate is reduced. Applying glyphosate degrading enzyme of bacterial origin such as glyphosate oxidoreductase (GOX) in combination with a glyphosate-tolerant epsps is the ultimate approach to provide commercial rates of glyphosate tolerance. In this project, a synthetic geneencoding GOX enzyme with plant codon preferences was designed. The structure of the synthetic construct and its mRNA were analyzed by bioinformatic tools. This synthetic gene was subcloned and transformed into canola plant via Agrobacterium mediated transformation in order to investigate the potential roles in increasing glyphosate tolerance. The presence, copy numbers and expression of the transgene were confirmed by PCR, Southern blotting and RT-PCR analyses, respectively. The bioassay with glyphosate challenging showed that the transgenic plant tolerated glyphosate at a concentration of 1.5 mM whereas the non-transformed canola was unable to survive in the presence 0.5 mM glyphosate.
- انتشار مقاله: 11-10-1348
- نویسندگان: Faranak Hadi,Amir Mousavi,Ali Hatef Salmanian,Kambiz Akbari Noghabi
- مشاهده
- جایگاه : پژوهشی
- مجله: Progress in Biological Sciences
- نوع مقاله: Journal Article
- کلمات کلیدی: Canola,Synthetic Gene,Glyphosate tolerance,Gene optimization,Glyphosate oxidoreductase
- چکیده:
- چکیده انگلیسی: The engineering of transgenic canola (Brassica napus L. ) to make tolerance to the broad-spectrum herbicide, glyphosate, is one of the most effective approaches for weed management. Glyphosate inhibits the enzyme EPSPS (5-enolpyruvylshikimate-3-phosphate synthase) enzyme which functions in the shikimate pathway and has a key role in biosynthesis of aromatic amino acids required for survival of the plant. Induction of glyphosate tolerance in transgenic canola via introducing mutated epsps to the plant genome has been previously reported. By this strategy, enzyme’s affinity for glyphosate is reduced. Applying glyphosate degrading enzyme of bacterial origin such as glyphosate oxidoreductase (GOX) in combination with a glyphosate-tolerant epsps is the ultimate approach to provide commercial rates of glyphosate tolerance. In this project, a synthetic geneencoding GOX enzyme with plant codon preferences was designed. The structure of the synthetic construct and its mRNA were analyzed by bioinformatic tools. This synthetic gene was subcloned and transformed into canola plant via Agrobacterium mediated transformation in order to investigate the potential roles in increasing glyphosate tolerance. The presence, copy numbers and expression of the transgene were confirmed by PCR, Southern blotting and RT-PCR analyses, respectively. The bioassay with glyphosate challenging showed that the transgenic plant tolerated glyphosate at a concentration of 1.5 mM whereas the non-transformed canola was unable to survive in the presence 0.5 mM glyphosate.
- انتشار مقاله: 11-10-1348
- نویسندگان: Faranak Hadi,Amir Mousavi,Ali Hatef Salmanian,Kambiz Akbari Noghabi
- مشاهده
- جایگاه : پژوهشی
- مجله: Iranian Journal of Veterinary Medicine
- نوع مقاله: Journal Article
- کلمات کلیدی: Aspergillus parasiticus,Listeria monocytogenes,Escherichia coli O157:H7,Candida parapsilosis,data organization method
- چکیده: زمینـه مطالعه: لاکتوباسیلها بعنوان منبعی ارزشمند برای ترکیبات ضد میکربی شناخته می شوند و از پتانسیل بالایی جهت محافظت بیـولـوژیـک غـذا در بـرابـر میکـروارگـانیسمهای مرتبط با آن برخوردارند. هدف: توان ضد میکربی 63 جدایه لاکتوباسیل لبنی علیه چهار میکروارگانیسم مهم مرتبط با غذا سنجیده شد. همچنین روش جدیدی به منظور سازماندهی دادههای حاصل از آزمون میکربی معرفی گردید که نتیجه آن مقایسهای مستدل تر و بر پایه اطلا عات بیشتر از حساسیت میکروارگانیسمهای شاخص به یک گروه از ترکیبات بود. ارتباط pH و خصوصیات ضد میکربی نیز سنجیده شد. روش کار: روش microbroth dilution assay جهت ارزیابی حساسیت میکروارگانیسمهای شاخص به سوپ رویی عاری از سلول کشت مایع (cell free culture supernatant; CFCS) لا کتوباسیلها مورد استفاده قرار گرفت. سازماندهی و پردازش نتایج حاصل از آزمونهای میکربی به هر دو روش سنتی ( بیان مقادیر حداقل غلظت ممانعت کننده رشد و حداقل غلظت کشنده) و روش پیشنهادی جدید که قدرت اثر مقایسهای هر نمونه CFCS علیه میکروارگانیسمهای شاخص مقایسه شونده را نشان می دهد، صـورت گـرفـت. نتـایـج: حسـاسیـت سـویـه های تست شده از ترتیب زیر تبعیت کرد: > L. monocytogenes > A. parasiticus > C. parapsilosis 7:H157.E. coli O لیستریا مونوسایتوژنز بر خلاف حساسیت بالا، بیشترین مقاومت را نسبت به مرگ در میـان میکـروارگـانیسـمهای آزمایش شده از خود نشان داد. میزان کارامدی CFCS لاکتوباسیلها در کشتن سویه های تست شده، ترتیب حساسیت زیر را نشان داد: > A. parasiticus > C. parapsilosis > L. monocytogenes 7:H157E. coli O. بین میزان pH وخصوصیت ضد میکربی ارتباط وجود داشت. PHهای CFCS غلیظ شده با مقادیر کمتر از 4 و 5/4 اثر مشخصی را به ترتیب بر روی حساسیت C. parapsilosis وE. coli داشتند. نتیجه گیری نهایی: توانایی لاکتوباسیلها در ممانعت از رشد میکروارگانیسمهای شـاخـص امیـدوار کننـده بـود و روش پیشنهـادی بـرای سـازمـانـدهـی دادههـا، بـا فـراهـم نمـودن اطلاعـات بیشتر موجب مقایسه دقیقتر میکروارگانیسمهای شاخص گردید.
- چکیده انگلیسی: BACKGROUND: Lactobacilli are known as a valuable source
of antimicrobial compounds and have a high potential of use in
food biopreservation against food related microorganisms.
OBJECTIVES: Antimicrobial potency of 63 dairy lactobacilli
isolates against four highly important food-related microorganisms
were evaluated. In addition, a new way in data organization was
introduced, which led to a more informative and rational
comparison of indicator microorganisms' susceptibilities to a set
of compounds. Correlation of pH and antimicrobial properties
was investigated. METHODS: Microbroth dilution assay was
used to evaluate indicator microorganisms' susceptibility to
lactobacilli CFCS (cell free culture supernatant). Results were
organized by both the conventional way - demonstrating the
minimum inhibitory and lethal concentrations of CFCS - and a
new suggested method, representing comparative effectiveness
of each CFCS specimen against indicator microorganisms of
comparison interest. RESULTS: Susceptibilities of tested strains
were in the following order: Escherichia coliO157:H7 > Listeria
monocytogenes > Aspergillus parasiticus> Candida parapsilosis.
Despite the high susceptibility of L. monocytogenes, it showed
the highest resistance to death among the tested microorganisms.
Eefficiency of Lactobacilli CFCS in killing the tested strains
showed the following susceptibility order: E. coli O157:H7 > A.
parasiticus> C. parapsilosis> L. monocytogenes. Antimicrobial
property was in correlation with the pH value of CFCS. PH had
a pronounced impact on susceptibilities of C. parapsilosisand E.
coli in pH values of concentrated CFCS lower than 4 and 4.5,
respectively. CONCLUSIONS: Potency of lactobacilli isolates in
growth inhibition of the indicator microorganisms was found
promising, and the suggested data organization method provided
additional information, leading to more precise comparison of
indicator microorganisms.- انتشار مقاله: 23-05-1392
- نویسندگان: Hadi Maleki,Ali Misaghi,Mohsen Amini,Abbas Saidi,Kambiz Akbari Noghabi
- مشاهده
- جایگاه : پژوهشی
- مجله: Iranian Journal of Pharmaceutical Sciences
- نوع مقاله: Journal Article
- کلمات کلیدی: Pseudomonas aeruginosa,Biosynthesis,Polyhydroxyalkanoate,Carboxylic acid
- چکیده:
- چکیده انگلیسی: In the present study, four carbon sources were tested for the polyester synthesis of Pseudomonas aeruginosa PA01 which is a ubiquitous environmental bacterium and is one of the top three causes of opportunistic human infections. These included linear C8 to C11 carboxylic acids. Octanoic acid, nonanoic acid, decanoic acid and undecanoic acid were added to M1 minimal medium to final concentrations of 60, 40, 30 and 20 mM, respectively. When P. aeruginosa was cultivated in M1 minimal medium with decanoate and nonanoate as the sole carbon sources, polyhydroxyalka-noate (PHA) was achieved up to 55.75% (w/w) and 24.53% (w/w), respectively. The maximum PHA yield at 30 ºC was obtained when decanoic acid was used as sole carbon source. Use of nonanoic acid as carbon source was resulted in a minimum PHA yield at 30 ºC. An increase in the cultivation temperature from 30 ºC to 37 ºC resulted in decrease of PHA content and cell dried weight as well. Based on the type of carbon source different monomers at the level higher than 1 mol% to 62 mol% were detected which included 3-hydroxyoheptanoic acid (C7), 3-hydroxyoctanoic acid (C8), 3-hydroxynonanoic acid (C9), 3-hydroxydecanoic acid (C10), and 3-hydroxyundecanoic acid (C11).
- انتشار مقاله: 13-09-1386
- نویسندگان: Kambiz Akbari Noghabi,Hossein Shahbani Zahiri,Abbas Sahebghadam Lotfi,Mitra Shourian,Gholamreza Karbalaei,Iman Rad,Solmaz Ahadi,Mahmood Arabnezhad
- مشاهده
- جایگاه : پژوهشی
- مجله: Iranian Journal of Biotechnology
- نوع مقاله: Journal Article
- کلمات کلیدی: Metalloprotease,Serratia sp,Enzyme characterization,Therapeutic applications
- چکیده:
- چکیده انگلیسی: Background: Proteolytic enzymes have an important role in variety of physiological and pathological functions. They have been used in therapeutic and pharmaceutical applications. Characterizations of extracellular proteases from various strains of S. marcescens indicate that most strains produce a very similar major metalloprotease. This metalloprotease (serrapeptidase, serrapeptase) is an important pharmaceutical agent. Serrapeptase has been used in Asian and European countries for the treatment of inflammatory diseases, cardiovascular disorders, and bacterial infections. Objectives: In the present study, purification and characterization of extracellular metalloprotease from Serratia sp. ZF03 for therapeutic purposes were reported. Materials and Methods: In this study the protease gene encoding a zinc-metalloprotease was isolated from the previously isolated red-pigmented Serratia sp. ZF03. The gene was sequenced and submitted to the GenBank. Proteolytic activity was detected by skim milk agar plate method and zymography. This fragment was found to encode an extracellular zinc-metalloendopeptidase with a molecular weight of approximately 50 kDa. The metalloprotease was purified by ammonium sulfate precipitation and dialysis, and then characterized. The effects of various inhibitors and reagents on protease activity and its kinetic parameters were also determined. Results: The nucleotide sequence demonstrated that deduced amino acid sequence has a higher identity with those of metalloprotease from serralysin family. Production of metalloprotease was highest at 48th h of cultivation. Optimum protease activity occurred at a temperature range of 50-55ºC and a pH range of 8.0-10. EDTA as a metal chelator, significantly inhibited protease activity. Zymography and inhibition assays showed that metalloprotease is the major secreted protease of Serratia sp. ZF03. The kinetic parameters, Km and Vm, were 0.00105 mg/ml and 0.0531 mM/min, respectively. Conclusions: Since the metalloprotease of this strain has strong proteolytic properties and good stability, it would be a suitable candidate to be used as an effective drug in the medicine and pharmaceutical industries.
- انتشار مقاله: 25-08-1392
- نویسندگان: Navvabeh Salarizadeh,Sadegh Hasannia,Kambiz Akbari Noghabi,Reza Hassan Sajedi
- مشاهده