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호텔주방의 물리적 작업환경이 조리사의 조직몰입에 미치는 영향 분석: 직무만족 매개효과 중심으로
박효남,황현주 한국외식산업학회 2020 한국외식산업학회지 Vol.16 No.2
The purpose of this study is to assume that the job satisfaction of the cook will have a mediating effect in the relationship between the physical environment of the hotel kitchen and the organizational commitment of the cook, and to grasp the correlation and degree of influence. Furthermore, the purpose of this study was to grasp the path and the direct and indirect effects of the relationships among the variables in this study. To this end, the differences and relationships between the main variables according to the general characteristics of the subjects were examined, and the paths and direct and indirect effects between them were investigated. First, it was confirmed that the physical working environment of the hotel kitchen had a statistically significant positive (+) effect on the job satisfaction of the cook. This means that the physical working environment of the kitchen, that is, the comfort, space, and convenience of the kitchen environment, needs to be recognized as a component that can affect the job satisfaction of the cook in the kitchen. Second, as a result of this study, it seems that the physical working environment of the hotel kitchen shows a statistically significant positive (+) direct effect on the organizational commitment of the cook. Organizational commitment is defined as the psychological state of organizational members. Looking at this aspect, it can be judged that the physical working environment of the hotel kitchen has a positive effect on the psychological state of the cook, and thus has a positive effect on work. Third, whether the job satisfaction variable of the cook, the central research problem of this study, plays a mediating role between the physical working environment of the hotel kitchen and the organizational commitment of the cook. As a result of this study, it was found that the job satisfaction of the cook had a statistically significant positive effect on the physical working environment of the hotel kitchen and the organizational commitment of the cook. In other words, it is judged that the job satisfaction of the cook plays a positive mediating role between the physical working environment of the hotel kitchen and the organizational commitment of the cook.
제조합균주 E. coli Ck1092가 생산하는 2,3-Dihydroxybiphenyl Dioxygenase의 정제 및 특성
박효남,김영수,김영창,김치경,임재윤 한국미생물생명공학회 ( 구 한국산업미생물학회 ) 1996 한국미생물·생명공학회지 Vol.24 No.3
4-CB 분해균주인 Pseudomonas sp. P20으로부터 pcbC 유전자를 클로닝하여 얻은 E. coli CK1092로부터 2,3-DHBP dioxygenase을 분리, 정제하여 효소적 특성을 조사하였다. 효소의 정제는 acetone 침전, DEAE-Se-phadex A-25 ion exchange chromatography, preparative electrophoresis 방법으로 정제하였다. 2,3-DHBP dioxygenase의 분자량은 약 270 kDa으로 추정되며, SDS-PAGE에 의한 분자량은 34 kDa이였다. 따라서, 동일한 subunit 8개 존재하는 octamer로 추정된다. 이 효소는 2,3-DHBP에 대해 높은 기질특이성을 보였으며, 3-methylcatechol, 4-methylcatechol, 4-chlorocatechol에 대해서는 활성을 보이지 않았다. 2,3-DHBP에 대한 Km 값은 18 μM이였으며 30μM 이상의 기질농도에서 활성이 감소하였다. 효소활성의 최적 pH는 8.0이였으며, pH 7.0~10.0 범위에서는 안정하였고, 최적 활성 온도는 40~60℃이며, 60℃까지는 비교적 안정하였다. 또한, 이 효소는 Cu^2+, Fe^2+, Fe^3+ 이온들에 의하여 효소활성이 저해되었고, H_2O_2와 EDTA에 의해서도 활성이 저해되었으며, 10%의 유기용매에 의해서 안정화되지 않았다. 효소활성부위를 알아보기 위해 화학변형제를 처리해 본 결과 tryosine, tryptophan과 histidine이 효소활성에 관여할 것으로 추정된다. 2,3-DHBP dioxygenase was purified from E. coli CK1092 carrying the pcbC gene, which was cloned from 4-chlorobiphenyl-degrading Pseudomonas sp. P20. Purification of this enzyme was done by acetone precipitation, DEAE-Sephadex A-25 ion exchange chromatography, and preparative gel electrophoresis. The molecular weight of subunit was 34 kDa determined by SDS-PAGE, and that of native enzyme was about 270 kDa. It suggests that this enzyme consist of eight identical subunits. This enzyme was specifically active against only 2,3-DHBP as a substrate with 18 μM of Km value, but not catechol, 3-methylcatechol, 4-methylcatechol and 4-chlorocatechol. The optimal pH and temperature of 2,3-DHBP dioxygenase were pH 8.0 and 40~60℃. The enzyme was inhibited by Cu^2+, Fe^2+ and Fe^3+ ions, and was inactivated by H_2O_2 and EDTA. The lower concentrations of some organic solvents such as acetone and ethanol don't stabilize the activity of 2,3-DHBP dioxygenase. The enzyme was completely inactivated by adding the reagents such as N-bromosuccinimide, iodine and p-diazobenzene sulfonic acid.
재조합균주 E. coli CK1092가 생산하는 2,3-Dihydroxybiphenyl Dioxygenase의 정제 및 특성
박효남,김영수,김영창,김치경,임재윤,Park, Hyo-Nam,Kim, Young-Soo,Kim, Young-Chang,Kim, Chi-Kyung,Lim, Jai-Yun 한국미생물 · 생명공학회 1996 한국미생물·생명공학회지 Vol.24 No.3
2,3-DHBP dioxygenase was purified from E. coli CK1092 carrying the pcbC gene, which was cloned from 4-chlorobiphenyl-degrading Pseudomonas sp. P20. Purification of this enzyme was done by acetone precipitation, DEAE- Sephadex A-25 ion exchange chromatography, and preparative gel electrophoresis. The molecular weight of subunit was 34 kDa determined by SDS-PAGE, and that of native enzyme was about 270 kDa. It suggests that this enzyme consist of eight identical subunits. This enzyme was specifically active against only 2,3-DHBP as a substrate with 18 $\mu$M of Km value, but not catechol, 3-methylcatechol, 4-methylcatechol and 4-chlorocatechol. The optimal pH and temperature of 2,3-DHBP dioxygenase were pH 8.0 and 40-60$\circ$C. The enzyme was inhibited by Cu$^{2+}$, Fe$^{2+}$ and Fe$^{3+}$ ions, and was inactivated by H$_{2}$0$_{2}$2 and EDTA. The lower concentrations of some organic solvents such as acetone and ethanol don't stabilize the activity of 2,3-DHBP dioxygenase. The enzyme was completely inactivated by adding the reagents such as N-bromosuccinimide, iodine and p- diazobenzene sulfonic acid.