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관광 관련학과 대학졸업 청년 취업자의 직무일치에 영향을 미치는 요인분석 - 사회계열 주요학과와의 비교 -
안소연 ( Ahn So-youn ),임은순 ( Yim Eun-soon ),김하니 ( Kim Ha-ny ) 한국호텔리조트학회(구 한국호텔리조트카지노산학학회) 2020 호텔리조트연구 Vol.19 No.1
This study analyzed ‘Graduates Occupational Mobility Survey 2017 (2016GOMS)’ data with SPSS 2.0 to determine the factors affecting job match, to look into the level of match between major, education and skills of tourism graduates, and to compare and analyze them with graduates from social science majors, which are relatively similar to tourism major. College graduates in tourism showed the lowest level in all three variables; job match, major satisfaction and importance of knowledge of college major in employment, of the difference analysis between majors. Whereas, tourism majors showed no significant differences in the education level match and the skill level match by gender unlike other majors. College major, major satisfaction, reasons for choosing major, whether to set a specific employment goal, and the importance of knowledge of major in employment are the variables affecting the education match. Establishment type, reasons for choosing major, GPA, and the importance of knowledge of college major in employment are the variables affecting the skill match. Those affecting the major match are major satisfaction, GPA and the importance of knowledge of college major in employment. The ‘importance of knowledge of college major in employment’ is the one variable that influences all of the education match, skill match, and major match.
Aspergillus niger 글루코오스 산화효소의 유도 발현
안소연,조현영,공광훈 中央大學校 基礎科學硏究所 2002 基礎科學硏究所 論文集 Vol.16 No.-
Glucose oxidase catalyzes the oxidation of β-D-glucose to gluconic acid. It is necessary to be obtained maximum glucose oxidase activity because the enzyme is used commercially for various applications, in particular extracelluar glucose oxidase. For high activity of extracellular glucose oxidase, we used the enzyme from Aspergillus niger and YEP medium. Extracellular glucose oxidase activity as high as 7.5Uml^-1 was obtained with sucrose as carbon source and peptone as nitrogen source. The result of testing a various of medium condition was obtainable the highest enzyme activity in condition of culture medium of 1% sucrose(w/v), 2% peptone(w/v) and 1% yeast extract(w/v) at 25℃. Our work indicate an economically attractive process for enzyme production. In addition Aspergillus niger glucose oxidase was purified by DEAE-Sephacel chromatography. The activity of the enzyme proceeded at pH 5.5 and the effective substrate of the enzyme was only glucose.
인체 글루타티온 전달효소에 있는 알지닌 13 변이체의 기질 특이성에 관한 연구
안소연,공광훈 中央大學校 基礎科學硏究所 2001 基礎科學硏究所 論文集 Vol.15 No.-
In order to study the roole of residue in the active site of glutathione S-transferase(GST), Arg13 residue in human GST P 1-1 was replaced with alanine, leucine or lysine by site-directed mutagenesis to obtain mutants R13A, R13L and R13K. These mutants were expressed in Escherichia coli and purified to electrophoretic homogeneity by affinity chromatography on immobilized GSH. The specific activities were determined by measuring the initial rates of the enzymes-catalyzed conjugation of GSH towards electrophilic substrates. Our results suggest that Arg13 in human GST P1-1 contributes to the binding of electroophilic substrate, but it is not needed for the glutathione peroxidase activity and the steroid isomerase activity of human glutathione S-transferase p1-1.