• Journal of Microbiology and Biotechnology
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• v.1 no.1
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• pp.22-30
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• 1991

In order to secrete the Bacillus subtilis cytidine deaminase (CDase, cytidine/2'-deoxycytidine deaminase) encoded by the B. subtilis cdd gene in E. coli by the aid of signal sequences, the cdd gene was fused in-frame to either amyE or penP signal sequences and the gene expression and CDase localization were examined. For the penP signal sequence::cdd fusion, the cdd gene with 9 amino acids truncated from the 5'-terminus was fused in-frame to the signal sequence, then the $cdd^{+}$ colonies were not occurred from the minimal plate by cdd complementation. The result suggests that 9 amino acids on the $NH_2-terminal$ of CDase have an essential function in the enzyme activity. The hybrid protein obtained by fused gene amyE signal sequence::cdd structural gene gave $cdd^{+}$ phenotype and about half of the total CDase activity was found to be secreted in the periplasm of E. coli transformant JF611/pSO202. The periplasmic CDase activity of JF611 harboring pSO52 containing the intact cdd gene was considerablely lower than that of the cells harboring pSO202 carrying the hybrid cdd gene. This suggests that the CDase was secreted to the periplasm through the cytoplasmic membrane by the aid of the amyE signal sequence in the E. coli transformant.

• Korean Journal of Microbiology
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• v.52 no.2
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• pp.220-225
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• 2016

To improve antioxidant glutathione (GSH) content and saccharification ability in sake yeasts of Saccharomyces cerevisiae, the ${\gamma}$-glutamylcysteine synthetase gene (GSH1) from S. cerevisiae, glucoamylase gene (GAM1) and ${\alpha}$-amylase gene (AMY) from Debaryomyces occidentalis were co-expressed in sake yeasts for manufacturing a refreshing alcoholic beverage abundant in GSH from rice starch. The extracellular GSH content of the recombinant sake yeasts increased 1.5-fold relative to the parental wide-type strain. The saccharification ability by glucoamylase of the new yeast strain expressing both GAM1 and AMY genes was 2-fold higher than that of the yeast strain expressing only GAM1 gene when grown in the culture medium containing 2% (w/v) rice starch. It generated 11% (v/v) ethanol from 20% (w/v) rice starch and consumed up to 90% of the starch content after 7 days of fermentation.

• Journal of Microbiology and Biotechnology
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• v.9 no.5
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• pp.668-671
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• 1999

The gene encoding Schwanniomyces occidentalis $\alpha-amylase$(AMY) was introduced into Saccharomyces cerevisiae var. diastaticus which secreted only glucoamylase, by using a linearized yeast integrating vector to develop stable strains with a capability of secreting $\alpha-amylase$and glucoamylase simultaneously. A dominant selectable marker, the geneticin(G418) resistance gene (Gt^r$), was cloned into a vector to screen wild-type diploid transformants harboring the AMY gene. The amylolytic activities of transformants were about 3-7 times higher than those of the recipient strains. When grown in nonselective media, the transformants with the linearized integrating vector containing the AMY gene exhibited almost all of the mitotic stability after 100 generations.

• Journal of Microbiology and Biotechnology
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• v.24 no.4
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• pp.447-452
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• 2014

To isolate novel and useful microbial enzymes from uncultured gastrointestinal microorganisms, a fecal microbial metagenomic library of the pygmy loris was constructed. The library was screened for amylolytic activity, and 8 of 50,000 recombinant clones showed amylolytic activity. Subcloning and sequence analysis of a positive clone led to the identification a novel gene (amyPL) coding for ${\alpha}$-amylase. AmyPL was expressed in Escherichia coli BL21 (DE3) and the purified AmyPL was enzymatically characterized. This study is the first to report the molecular and biochemical characterization of a novel ${\alpha}$-amylase from a gastrointestinal metagenomic library.

• 대한치과보철학회:학술대회논문집
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• 1999.04a
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• pp.91.1-91.1
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• 1999

• Korean Architects
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• s.508
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• pp.74-82
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• 2011

• Asian-Australasian Journal of Animal Sciences
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• v.12 no.7
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• pp.1011-1014
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• 1999

Blood protein polymorphism of fowls in Laos was analyzed by electrophoresis. Blood samples were collected in the area of Viangchan, Louangphrabang and Pakxe. Out of 17 loci, polymorphism was detected at the following seven loci; ES-1, Amy-1, Akp-akp, Akp-2, Alb, Tf and Pas. The other ten loci; Amy-3, LDH, 6-PGD, PGM, PHI, To, MDH, Es-D, Hb-l, Hb-2 were noted to be monomorphic. The proportion of polymorphic loci $(P_{poly})$, the expected average heterozygosity per individual ($\bar{H}$), and the subdivision index $(G_{ST})$ of the native fowl in Laos was $0.412{\pm}0.123$, 0.106 and 0.026, respectively. Genetic distance between native fowls in Laos, Bangladesh, and Nepal was clustered in one group.

• Proceedings of the Membrane Society of Korea Conference
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• 2000.07a
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• pp.1-38
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• 2000

• Korean Architects
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• s.488
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• pp.60-61
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• 2009

본 기행문은 2009한국건축문화대상 계획건축물부문 심사위원인 필자가 수상자들을 인솔하여 해외건축탐방을 다녀온 뒤 건축 기행문을 게재한 것이다.

• 수도
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• v.24 no.4 s.85
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• pp.14-20
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• 1997