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Reproducing kernel based evaluation of incompatibility tensor in field theory of plasticity
Aoyagi, Y.,Hasebe, T.,Guan, P.C.,Chen, J.S. Techno-Press 2008 Interaction and multiscale mechanics Vol.1 No.4
This paper employs the reproducing kernel (RK) approximation for evaluation of field theory-based incompatibility tensor in a polycrystalline plasticity simulation. The modulation patterns, which is interpreted as mimicking geometrical-type dislocation substructures, are obtained based on the proposed method. Comparisons are made using FEM and RK based approximation methods among different support sizes and other evaluation conditions of the strain gradients. It is demonstrated that the evolution of the modulation patterns needs to be accurately calculated at each time step to yield a correct physical interpretation. The effect of the higher order strain derivative processing zone on the predicted modulation patterns is also discussed.
S. P. Singh,M. K. Purohit,C. Aoyagi,M. Kitaoka,K. Hayashi 한국생물공학회 2010 Biotechnology and Bioprocess Engineering Vol.15 No.2
In vivo folding of many proteins can be facilitated by growth temperature, extent of induction, and molecular chaperones, which prevent over-expressed protein from being trapped into insoluble inclusion bodies. In the present report, we describe the role of molecular chaperones and growth temperature on the solubilization of overexpressed Cellobiose Phosphorylase (CBP) in Escherichia coli. The growth of host at low temperature enhanced enzyme in soluble fraction. Similarly, induction of target gene at low level of IPTG also yielded higher enzyme in soluble fraction. The synergistic effect of low temperature and induction on the prevention of inclusion bodies was also evident from our results. In addition, co-expression of the target gene with two types of molecular chaperones (GroESL and KODHsp) was also attempted. However,none of these chaperones enhanced the solubilization under in vivo conditions. Nevertheless, effective role of low growth temperature coupled with low level of induction appeared to be an attractive feature for producing recombinant protein.