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- 저자 : Yasser R Abdel-Fattah (검색결과 4 건)
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Abdel-Fattah, Yasser R.,Kashyout, Abdel-Hady B.,Sheta, Walaa M. World Technopolis Association 2013 World Technopolis Review Vol.2 No.2
Egypt has been known as the light house of science and innovation not only in the Middle East but to the world across ages. Recently, there have been many ups and downs that positioned Egypt in a lower rank that it actually deserves according to its long history. This review entitles the current condition of science, technology and innovation in Egypt and the consequent setting up of best practices of science and technology parks (STPs) experiences. Egypt's science, technology and innovation (STI) system is highly centralized and dominated by the public sector, with R&D happening mostly in state-run universities and research centers supervised by the Ministry of Higher Education and Ministry of Scientific Research. R&D indicators state that Egypt ranking is 40th worldwide for the published articles (around 10,000 papers in 2011), while the numbers of issued patents (350 local and 50 international in 2011) is still far beyond expected. STPs in Egypt are addressed in this review by three examples; smart village in Cairo, Investment zone in Borg El-Arab City and Technology Valley in Ismailia. The three models are discussed in details and a suggested road map for developing more STPs is estimated.
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Yasser R. Abdel-Fattah,Abdel-Hady B. Kashyout,Walaa M. Sheta 세계과학도시연합 2013 World Technopolis Review Vol.2 No.2
Egypt has been known as the light house of science and innovation not only in the Middle East but to the world across ages. Recently, there have been many ups and downs that positioned Egypt in a lower rank that it actually deserves according to its long history. This review entitles the current condition of science, technology and innovation in Egypt and the consequent setting up of best practices of science and technology parks (STPs) experiences. Egypt’s science, technology and innovation (STI) system is highly centralized and dominated by the public sector, with R&D happening mostly in state-run universities and research centers supervised by the Ministry of Higher Education and Ministry of Scientific Research. R&D indicators state that Egypt ranking is 40th worldwide for the published articles (around 10,000 papers in 2011), while the numbers of issued patents (350 local and 50 international in 2011) is still far beyond expected. STPs in Egypt are addressed in this review by three examples; smart village in Cairo, Investment zone in Borg El-Arab City and Technology Valley in Ismailia. The three models are discussed in details and a suggested road map for developing more STPs is estimated.
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M. R. El-Aassar,Mahmoud H. M. A. Shibraen,Yasser R Abdel-Fattah,Ahmed A. Elzain 한국섬유공학회 2019 Fibers and polymers Vol.20 No.11
Enzyme immobilization onto nanomaterials is a strategy to overcome the difficulties of the free enzymesapplications where the immobilization process affords excellent reusability and operational stability against temperature andpH, and high surface area for the catalytic reaction. In this work, poly(Acrylonitrile-co-Styrene/Pyrrole), (poly(AN-co-ST/Py)), copolymer nanofibers were successfully fabricated using the electrospinning technique. Laccase enzyme from Trametesversicolor was immobilized onto functionalized poly(AN-co-ST/Py) nanofibers by covalent attachment usingpolyethylenediamine (PEI) via physical adsorption and multipoint covalent attachment to the functional groups onto thepolymeric surface. Since the relative activity of the immobilized Laccase depends on the amount of the coupled PEI onto thepolymeric nanofibers, a colorimetric assay via copper ions complex formation was applied for the estimation of the processyield. Accordingly, the various factors affecting the PEI coupling process such as concentration, time, pH and temperaturewere investigated; Besides their influence on the morphology of the resultant nanofibers. Furthermore, thermal and pHstability, storage stability, and reusability were evaluated and compared. The optimum reaction temperature and pH for theimmobilized enzyme were 70 oC and 6.0, respectively. The scanning electron microscopy (SEM) images showed that themodified nanofibers with PEI have kept its nanofibers structure and uniform morphology with an average diameter ofapproximately 559.2 nm. Within 35 days, the immobilization process reduces the activity loss from 59 % to 29 %, whilethermal incubation at 50 oC for 2 hrs causes activity loss for the free and immobilized enzymes by 65 % and 30 %respectively. Therefore, the prepared copolymer nanofibers proposed in this work showed promising potential forapplications to enzyme immobilization.
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( Rania S Ahmed ),( Amira M Embaby ),( Mostafa Hassan ),( Nadia A Soliman ),( Yasser R Abdel-fattah ) 한국미생물생명공학회(구 한국산업미생물학회) 2021 한국미생물·생명공학회지 Vol.49 No.2
The present study addresses isolation, optimization, partial purification, and characterization of a haloalkaline serine protease from a newly isolated haloarchaeal strain isolated from Wadi El Natrun in Egypt. We expected that a two-step sequential statistical approach (one variable at a time, followed by response surface methodology) might maximize the production of the haloalkaline serine protease. The enzyme was partially purified using Hiprep 16/60 sephacryl S-100 HR gel filtration column. Molecular identification revealed the newly isolated haloarchaeon to be Natrialba hulunbeirensis strain WNHS14. Among several tested physicochemical determinants, casamino acids, KCl, and NaCl showed the most significant effects on enzyme production as determined from results of the One-Variable-At-A-time (OVAT) study. The Box- Behnken design localized the optimal levels of the three key determinants; casamino acids, KCl, and NaCl to be 0.5% (w/v), 0.02% (w/v), and 15% (w/v), respectively, obtaining 62.9 U/ml as the maximal amount of protease produced after treatment at 40℃, and pH 9 for 9 days with 6-fold enhancement in yield. The enzyme was partially purified after size exclusion chromatography with specific activity, purification fold, and yield of 1282.63 U/mg, 8.9, and 23%, respectively. The enzyme showed its maximal activity at pH, temperature, and NaCl concentration optima of 10, 75℃, and 2 M, respectively. Phenylmethylsulfonyl fluoride (PMSF, 5 mM) completely inhibited enzyme activity.
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