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RISS 인기검색어
- 검색키워드
- 저자 : Ali-Asghar Naderi (검색결과 3 건)
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Influence of fiber paths on buckling load of tailored conical shells
Ali-Asghar Naderi,Gholam-Hossein Rahimi,Mohammad Arefi 국제구조공학회 2014 Steel and Composite Structures, An International J Vol.16 No.4
The purpose of this paper is to propose a method for evaluation of varying stiffness coefficients of tailored conical shells (TCS). Furthermore, a comparison between buckling loads of these shells under axial load with the different fiber path is performed. A circular truncated conical shell subjected to axial compression is taken into account. Three different theoretical path containing geodesic path, constant curvature path and constant angle path has been considered to describe the angle variation along the cone length, along cone generator of a conical shell are offered. In the TCS with the arbitrary fiber path, the thickness and the ply orientation are assumed to be functions of the shell coordinates and influencing stiffness coefficients of the structure. The stiffness coefficients and the buckling loads of shells are calculated basing on classical shells theory (CST) and using finite-element analysis (FEA) software. The obtained results for TCS with arbitrary fiber path, thickness and ply orientation are derived as functions of shell longitudinal coordinate and influencing stiffness coefficients of structures. Furthermore, the buckling loads based on fiber path and ply orientation at the start of tailored fiber get to be different. The extent of difference for tailored fiber with start angle lower than 20 degrees is not significant. The results in this paper show that using tailored fiber placement could be applied for producing conical shells in order to have greater buckling strengths and lower weight. This work demonstrates the use of fiber path definitions for calculated stiffness coefficients and buckling loads of conical shells.
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Ali Asghar Javidparvar,Reza Naderi,Bahram Ramezanzadeh,Ghasem Bahlakeh 한국공업화학회 2019 Journal of Industrial and Engineering Chemistry Vol.72 No.-
Graphene oxide (GO) was used as a smart pH-sensitive carrier for delivery of green corrosion inhibitors tothe active corrosion sites of metal. Results demonstrated the physisorption and chemisorption of ceriumonto the GO surface. The open circuit potential, polarization test and electrochemical impedancespectroscopy measurements as well asfield-emission scanning electron microscopy and energydispersive spectroscopy were used to study the corrosion inhibition power of GO–Ce system. Resultsrevealed that as a result of cerium oxide/hydroxidefilm generation on the cathodic regions, the corrosionof mild steel was remarkably inhibited in the chloride solution.
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Reyhane Zamani,Sayyed Shahryar Rahpeyma,Moein Aliakbari,Mousa Naderi,Mohsen Yazdanei,Saeed Aminzadeh,Jafar Khezri,Kamahldin Haghbeen,Ali Asghar Karkhane 한국생물공학회 2023 Biotechnology and Bioprocess Engineering Vol.28 No.4
Improving the thermal stability of enzymes is an essential factor in the industrial applications of enzymes. Many methods related to increased thermal stability were explained, and increasing salt bridges is one of the strategies for improving the thermal stability of enzymes. In this study, mutations T59E, I145R, N149R, V219D, and A262R are introduced into the native cellulase gene to produce the mutant 5M-cel5E cellulase. In silico results showed that the mutation increased the salt bridges from 15 to 28. Root mean square fluctuation (RMSF) calculations confirmed that the mutation increased protein stability. Furthermore, the docking results showed that the affinity of cellobiose for the 5M-cel5E active site (-122.759) was slightly decreased compared to native cellulase (-130.93). No enzymatic activity was found in 5M-cel5E cellulase after cloning, expression and purification. Activated the enzyme with a back mutation of R149N, the result of which was named 4M-cel5E. The last mutation increases the salt bridges from 15 to 22, creating 4 salt bridge networks. The 4M-cel5E enzyme exhibited a maximum activity of 463 U/mg at pH 6.0 and 45°C. The mutations also increased the enzyme thermal stability up to 1.5 and 3.4-fold at temperatures of 65 and 67oC, respectively. These mutations made the Clostridium thermocellum cellulase suitable for various industries such the biofuel and paper.
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