• Journal of the Korean Crystal Growth and Crystal Technology
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• v.10 no.3
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• pp.189-198
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• 2000

The stochiometric mixture of evaporating materials for the $CuGaSe_2$single crystal thin films were prepared from horizontal furnace. Using extrapolation method of X-ray diffraction patterns for the polycrystal $CuGaSe_2$, it was found tetragonal structure whose lattice constant $a_0}$ and $c_0$ were 5.615 $\AA$ and 11.025 $\AA$, respectively. To obtains the single crystal thin films, $CuGaSe_2$mixed crystal was deposited on throughly etched GaAs(100) by the Hot Wall Epitaxy (HWE) system. The source and substrate temperature were $610^{\circ}C$ and $450^{\circ}C$ respectively, and the growth rate of the single crystal thin films was about 0.5$\mu\textrm{m}$/h. The crystalline structure of single crystal thin films was investigated by the double crystal X-ray diffraction (DCXD). Hall effect on this sample was measured by the method of van der Pauw and studied on carrier density and mobility depending on temperature. From Hall data, the mobility was likely to be decreased by pizoelectric scattering in the temperature range 30 K to 150 K and by polar optical scattering in the temperature range 150 K to 293 K. The optical energy gaps were found to be 1.68 eV for CuGaSe$_2$sing1e crystal thin films at room temperature. The temperature dependence of the photocurrent peak energy is well explained by the Varshni equation then the constants in the Varshni equation are given by $\alpha$ = $9.615{\times}10^{-4}$eV/K, and $\beta$ = 335 K. From the photocurrent spectra by illumination of polarized light of the $CuGaSe_2$single crystal thin films. We have found that values of spin orbit coupling $\Delta$So and crystal field splitting $\Delta$Cr was 0.0900 eV and 0.2498 eV, respectively. From the PL spectra at 20 K, the peaks corresponding to free bound excitons and D-A pair and a broad emission band due to SA is identified. The binding energy of the free excitons are determined to be 0.0626 eV and the dissipation energy of the acceptor-bound exciton and donor-bound exciton to be 0.0352 eV, 0.0932 eV, respectively.

• Korean Journal of Microbiology
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• v.52 no.2
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• pp.192-201
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• 2016

Recently, Psychrobacter sp. ArcL13 strain showing the extracellular lipase activity was isolated from the Chuckchi Sea of the Arctic Ocean. However, due to the low expression levels of the enzyme in the natural strain, the production of recombinant lipase is crucial for various applications. Identification of the gene for the enzyme is prerequisite for the production of the recombinant protein. Therefore, in the present study, a novel lipase gene (ArcL13-Lip) was isolated from Psychrobacter sp. ArcL13 strain by gene prospecting using PCR, and its complete nucleotide sequence was determined. Sequence analysis showed that ArcL13-Lip has high amino acid sequence similarity to lipases from bacteria of some Psychrobacter genus (84-90%) despite low nucleotide sequence similarity. The lipase gene was cloned into the bacterial expression plasmid and expressed in E. coli. SDS-PAGE analysis of the cells showed that ArcL13-Lip was expressed as inclusion bodies with a molecular mass of about 35 kDa. Refolding was achieved by diluting the unfolded protein into refolding buffers containing various additives, and the highest refolding efficiency was seen in the glucose-containing buffer. Refolded ArcL13-Lip showed high hydrolytic activity toward p-nitrophenyl caprylate and p-nitrophenyl decanoate among different p-nitrophenyl esters. Recombinant ArcL13-Lip displayed maximal activity at $40^{\circ}C$ and pH 8.0 with p-nitrophenyl caprylate as a substrate. Activity assays performed at various temperatures showed that ArcL13-Lip is a cold-active lipase with about 40% and 73% of enzymatic activity at $10^{\circ}C$ and $20^{\circ}C$, respectively, compared to its maximal activity at $40^{\circ}C$.