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측면 연마된 광섬유와 완전도체면 아래의 유전체 사이에서의 결합과 전파특성의 해석
권광희,윤기홍,김정훈,송재원,박의돈,손석우,Kwon, Kwang-Hee,Yoon, Ki-Hong,Kim, Jeong-Hoon,Song, Jae-Won,Park, Euy-Dong,Son, Seok-Woo 한국통신학회 2003 韓國通信學會論文誌 Vol.28 No.2A
완전도체면 아래의 유전체와 측면 연마된 광섬유의 소산장 결합 및 전파특성에 대한 해석 연구 결과를 나타내었다. 두 구조에서의 전파특성과 소산장 결합 관계를 해석하기 위해 결합모드 방정식과 혼합 모드(compound-mode) 방정식을 이용하여 코아와 유전체의 굴절률 및 구조의 각 변수에 대한 특성을 나타내었다. 그리고 측면 연마된 광섬유와 완전도체면 아래의 유전체가 결합할 때 일어나는 광섬유에서의 감쇠현상을 비교하기 위하여 감쇠상수를 구하여 함께 비교하였다. A theoretical presentation of evanescent coupling is offered with respect to the refractive indexes between a side polished optical fiber and an infinitely planar waveguide with a conductor cladding(PWGCC). The PWG is suspended at a constant distance from an unclad fiber core and attached with the perfect conductor(PEC) on one side. The behavior of the distributed coupler is examined using a coupled mode model, which takes account of the two dimensions of the waveguide configuration. The coupling and propagation of light were found to depend on both the relationship between the refractive index values of each structure and the configuration of the side polished fiber used in the PWGCC. The spreading of light in the unconfined direction of the PWGCC is described in terms of a simple geometrical interpretation of the synchromization condition that is in agreement with a previous investigation of the problem based on the coupled-mode theory(CMT). The power of the light propagation in the fiber decreased exponentially along the fiber axis as it was transferred to the PWGCC.
α-Amylase 고생산성 Bacillus licheniformis 변이주의 개발과 특성 분석
정허진,정경화,장종수,윤기홍,박승환,김훈 ( Heo Jin Jeong,Kyung Hwa Jung,Jong Soo Chang,Ki Hong Yoon,Seung Hwan Park,Hoon Kim ) 한국응용생명화학회 1998 Applied Biological Chemistry (Appl Biol Chem) Vol.41 No.1
A mutant strain which hyperproduced thermostable α-amylase was obtained by chemical mutagenesis of Bacillus licheniformis. The mutant strain, SK-5, produced the enzyme about 50 times higher than the original strain. The mutant was longer and slimmer in shape, slower in growth compared to the original strain. Nucleotide sequence analysis of the SK-5 α-amylase gene revealed no changes in the the structural gene. The changes found in the promoter region might be responsible for the hyperproduction of the enzyme by the mutant. No structural changes in the enzyme structure could be observed when the, secreted enzymes at various culture times were analyzed by Western blot.