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Kim, Deok-Kyu;Jin, Hu-Jie;Song, Min-Jong;Park, Choon-Bae
- Proceedings of the Korean Institute of Electrical and Electronic Material Engineers Conference
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- 2005.07a
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- pp.187-188
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- 2005
The characteristics of GaN epitaxial layers grown on silicon (111) substrates by metalorganic vapor phase epitaxy have been investigated. The only control of AlN thickness was found to decrease the stress sufficiently for avoiding crack formation in an overgrown thick ($2.6{\mu}m$) GaN layer. X-ray diffraction and photoluminescence measurements are used to determine the effect of AlN thickness on the strain in the subsequent GaN layers. Strong band edge photoluminescence of GaN on Si(111) was observed with a full width at half maximum of the bound exciton line as low as 17meV at 13K.
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이동석;김지연;김한복
- Korean Journal of Microbiology
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- v.36 no.3
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- pp.203-208
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- 2000
A Baczllus circdans KCTC3004 $\alpha$-amylase gene contained in a recombinant plasmid pAL850 was transferred into a new shuttle vector plasmid pALSIlI by ligating linearlzed DNAs of pUC19 and pUB110. B. subtilis RM125 and B. megatenurn ATCC14945 transfonned with pALS111 produced the $\alpha$-amylase substantially Most of the enzyme was produced during the exponential growth period. The maxiinurn activities of the $\alpha$-amylase produced by the Bucillus transformants were compared with that of the B. circulans gene donor strain. The B. subtilis RM125(pALS111) enzyme showed the actlvicy 95 times higher than that of the gene donor cells, followed by the B, nzegaterium ATCC14945(pALSlll) enzyme with activity 34 limes higher than that of the gene donor cells. While E coli secreted about 10% of the produced enzyme, B. subtilis excreted the enzyme inlo the medium wholly and B. megaterirun about 98% ofthe total product. The plasmid pALSI11 was quite stable inB. nzegaterium (92%), inoderately stable in B. subtilis (76%), but was unstable in E. coli (38%). The SDS-PAGE and zymogram of this enzyme produced in E. coli(pALS111), B. subtilis( pALS111) or B. megateril~m (pALS111) indicated a molecular weight of 55,000. The enzymes overproduced in three different host cells hydrolyzed starch to produce mainly maltoaiose and mallooligosaccharides.
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