• Journal of Electrical Engineering and Technology
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• 제7권4호
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• pp.501-512
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• 2012

Social welfare maximization in a double-sided auction market is performed by implementing an aggregation-based particle swarm optimization (CAPSO) algorithm for optimal placement and sizing of one Static Synchronous Series Compensator (SSSC) device. Dallied simulation results (without/with line flow constraints and without/with SSSC) are generated to demonstrate the impact of SSSC on the congestion levels of the modified IEEE 14-bus test system. The proposed CAPSO algorithm employs conventional quadratic smooth and augmented quadratic nonsmooth generator cost curves with sine components to improve the accurate of the model by incorporating the valve loading effects. CAPSO also employs quadratic smooth consumer benefit functions. The proposed approach relies on particle swarm optimization to capture the near-optimal GenCos and DisCos, as well as the location and rating of SSSC while the Newton based load flow solution minimizes the mismatch equations. Simulation results of the proposed CAPSO algorithm are compared to solutions obtained by sequential quadratic programming (SQP) and a recently implemented Fuzzy based genetic algorithm (Fuzzy-GA). The main contributions are inclusion of customer benefit in the congestion management objective function, consideration of nonsmooth generator characteristics and the utilization of a coordinated aggregation-based PSO for locating/sizing of SSSC.

• Journal of Microbiology and Biotechnology
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• 제24권5호
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• pp.597-604
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• 2014

$\small{D}$-Phenylglycine aminotransferase ($\small{D}$-PhgAT) from Pseudomonas stutzeri ST-201 is useful for enzymatic synthesis of enantiomerically pure $\small{D}$-phenylglycine. However, its low protein solubility prevents its application at high substrate concentration. With an aim to increase the protein solubility, the N-terminus of $\small{D}$-PhgAT was genetically fused with short peptides ($A_1$ ${\alpha}$-helix, $A_2$ ${\alpha}$-helix, and ALAL, which is a hybrid of $A_1$ and $A_2$) from a ferredoxin enzyme of a halophilic archaeon, Halobacterium salinarum. The fused enzymes $A_1$-$\small{D}$-PhgAT, $A_2$-$\small{D}$-PhgAT, and ALAL-$\small{D}$-PhgAT displayed a reduced pI and increased in solubility by 6.1-, 5.3-, and 8.1- fold in TEMP (pH 7.6) storage, respectively, and 5-, 4.5-, and 5.9-fold in CAPSO (pH 9.5) reaction buffers, respectively, compared with the wild-type enzyme (WT-$\small{D}$-PhgAT). In addition, all the fused $\small{D}$-PhgAT displayed higher enzymatic reaction rates than the WT-DPhgAT at all concentrations of L-glutamate monosodium salt used. The highest rate, $23.82{\pm}1.47$ mM/h, was that obtained from having ALAL-$\small{D}$-PhgAT reacted with 1,500 mM of the substrate. Moreover, the halophilic fusion significantly increased the tolerance of $\small{D}$-PhgAT in the presence of NaCl and KCl, being slightly in favor of KCl, where under the same condition at 3.5 M NaCl or KCl all halophilic-fused variants showed higher activity than WT-$\small{D}$-PhgAT.