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    Production of glucoamylase by aspergillus niger under solid state fermentation

    , Article International Journal of Engineering, Transactions B: Applications ; Volume 25, Issue 1 , 2012 , Pages 1-7 ; 1728-144X (ISSN) Nahid, P ; Vossoughi, M ; Roostaazad, R ; Ahmadi, M ; Zarrabi, A ; Hosseini, S. M ; Sharif University of Technology
    Abstract
    In this study, Glucoamylase production by Aspergillus niger was investigated under solid state fermentation using low cost by-products of agricultural processes as substrate. Highest enzyme production was observed when a combination of wheat bran (WB) and corn flour (CF) was used as compared to WB+ rice bran, WB+ rice flour and WB alone. Several compositions of corn flours were experimented. The best combination of WB in addition of 10% corn flour resulted maximum enzyme activities. Study of the fermentations in flasks revealed 373.3 IU/gds and 41.4 g/l for the enzyme activity and protein concentration respectively under conditions of 30± 1°C, pH 4.7 and time 96 h. Optimum conditions... 

    Vesicle deformations by clusters of transmembrane proteins

    , Article Journal of Chemical Physics ; Volume 134, Issue 8 , 2011 ; 00219606 (ISSN) Bahrami, A. H ; Jalali, M. A ; Sharif University of Technology
    2011
    Abstract
    We carry out a coarse-grained molecular dynamics simulation of phospholipid vesicles with transmembrane proteins. We measure the mean and Gaussian curvatures of our protein-embedded vesicles and quantitatively show how protein clusters change the shapes of their host vesicles. The effects of depletion force and vesiculation on protein clustering are also investigated. By increasing the protein concentration, clusters are fragmented to smaller bundles, which are then redistributed to form more symmetric structures corresponding to lower bending energies. Big clusters and highly aspherical vesicles cannot be formed when the fraction of protein to lipid molecules is large  

    Rigidity of transmembrane proteins determines their cluster shape

    , Article Physical Review E - Statistical, Nonlinear, and Soft Matter Physics ; Volume 93, Issue 1 , 2016 ; 15393755 (ISSN) Jafarinia, H ; Khoshnood, A ; Jalali, M. A ; Sharif University of Technology
    American Physical Society 
    Abstract
    Protein aggregation in cell membrane is vital for the majority of biological functions. Recent experimental results suggest that transmembrane domains of proteins such as α-helices and β-sheets have different structural rigidities. We use molecular dynamics simulation of a coarse-grained model of protein-embedded lipid membranes to investigate the mechanisms of protein clustering. For a variety of protein concentrations, our simulations under thermal equilibrium conditions reveal that the structural rigidity of transmembrane domains dramatically affects interactions and changes the shape of the cluster. We have observed stable large aggregates even in the absence of hydrophobic mismatch,...