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소상공인 창업자금 지원의 일자리창출 효과 : 서울신용보증재단의 역할
전덕영,윤병섭 한국상업교육학회 2019 상업교육연구 Vol.33 No.1
The purpose of this study is to analyze the effect of the start-up capital of small businesses in Seoul on the job creation effect centering on the role of the Seoul Credit Guarantee Foundation. 490 firms conducted by the Seoul Credit Guarantee Foundation between 2015 and 2018 were used for the analysis. They are composed of 363 pre-founders who received consulting support to provide start-up funds in founding small businesses and 127 existing founders who did not receive consulting support. The results of the empirical study are as follows. First, it shows that age and total assets which are funding factors of pre-founders have a systematically significant positive effect on the number of jobs. This suggests that job creation effects will be significant if the funding and consulting support is extended to a pre-founder with a high age and a large total assets. This results support the work of Reynolds (1994), van Stel & Storey (2004), and Park Joo-wan and Kang Man-soo (2016). Second, there is a systematic positive effect of rent, industry, and capital ratio on the number of jobs. High rental rates, high capital ratios, and the expansion of funding to existing entrepreneurs who are willing to work in the restaurant industry show a significant job creation effect. This result was supported by Fritsch & Mueller (2008), Ahn Eun-Kyung and Lee Hee-Yeon (2015). Third, as the result of comparing the existing business founder who did not receive the business plan consulting with the preliminary founder who received the business plan consulting, the average ratio of job openings of the existing founders was 1.68 and the average ratio of preliminary job openings was 1.66. The difference of job creation between the two groups was significant. This study suggests that the rich experience of business is more effective than the training experience through consulting. It shows that business experience is important than cousulting training and it is necessary to expand opportunities for re-start of business for small business owners who experienced business failure.
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Rice Bran Lipoxygenase : Purification and Characterization
전덕영,이귀주,이현재,John, Deuk-Young,Lee, Gui-Ju,Lee, Hyun-Jae 생화학분자생물학회 1981 한국생화학회지 Vol.14 No.3
쌀의 도정 과정 중 얻어지는 미강으로부터 lipoxygenase를 분리, 정제하였으며 이 효소가 지닌 과산화 반응의 촉매작용 특성에 관하여 연구 검토하였다. 이 효소의 분자량은 약 100,000 daltons 이었으며 효소의 등전점 (pI) 값은 4.8로 얻어졌다. 이 효소는 상온하에서는 비교적 안정성을 보이고 있으나 $50^{\circ}C$ 이상에서는 상당한 불활성화 현상을 일으키고 있었으며, 이 경우 온도 변화에 따른 불활성화 상수값 $(K_d)$은 40, 50 및 $60^{\circ}C$에서 각각 0.002, 0.014 및 0.136 $min^{-1}$로 얻어졌다. 이 효소가 지닌 기질 특이성은 대두 효소에서와 비슷하였으며 리놀레산 기질에 대한 과산화반응의 촉매 활성도는 중성 pH (6.8~7.0)와 $30^{\circ}C$에서 최대값을 보였다. 한편 효소 기질간의 친화력은 $K_m$ 값을 비교할 때 리놀레산과 산소분자는 비슷한 값인 약 100 ${\mu}M$로서 얻어졌다. 그밖의 효소반응의 초기 속도 측정에 의한 반응 속도론적 실험을 통하여 리놀레산의 과산화반응 양상에 대하여도 고찰해 보았다. A form of lipoxygenase (EC 1. 13. 11. 12) was isolated from rice brans which were obtained from the milling of rice caryopsis, and was purified partially but to give an electrophoretically homogeneous form. The molecular weight of the enzyme was found to be about 100, 000 daltons based on the gel filtration experiment. The optimum activity for the catalytic hydroperoxidation by rice bran lipoxygenase was obtained at neutural pH (pH 6. 8 to 7. 0) and at $30{^{\circ}C$. The enzyme show ed a relative stability under the neutral pH and at room temperature, but a marked deactivation of the enzyme protein was observed at the preincubation temperature above a $50^{\circ}C$. The first order deactivation constants for the enzyme were calculated to be 0.002, 4.014, 0.136 and 0.281 per minute at 40, 50, 60 and $70^{\circ}C$, respectively. The isoelectric point of the enzyme was about 4. 8 based on the isoelectrofocusing experiment, The enzyme was found to be very specific toward linoleate for the hydroperoxidation as in the case of the soybean enzyme, but the estimated $K_m$ values for linoleate and molecular oxygen were found to be about the same. Based on the steady state kinetic experiment measuring the initial velocity of the enzyme reaction, it was also suggested that the hydroperoxidation of linoleate is proceeded through the formation of a ternary complex between the enzyme and two substrate ligands.
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전덕영 全南大學校家政科學硏究所 1994 生活科學硏究 Vol.4 No.-
Expressions of food additives imprinted on food package were investigated to get an idea what food additives are prevalently used in commercial processed foods. Total 378 foods were surveyed at supermarkets. The 76% of foods surveyed contained food additives and 100 food additives were used among 400 food additives that were permitted legally. Among them following additives were most frequently used with decreasing order; citric acid, monosodium glutamate, food yellow No.5, baking powder, food yellow No.4, potassium sorbate. Major additives of confectioneries or ice creams were synthetic colouring agents. All Danmujis(pickle) included saccharin and sorbic acid salt as a sweetener and a preservative, respectively. All margarines contained sodium dehydroacetic acid. Sodium nitrite, erythorbic acid, and sodium sorbate were comprised in all kinds of hams and sausages. p-Oxybenzoic acid butyl esters were found in all commercial Kanjangs(soy sauce).
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미강에 함유된 리폭시게나제외 분리 , 정제 및 효소의 특성에 관한 연구
전덕영,이귀주,이현재 ( Deuk Young John,Gui Ju Lee,Hyun Jae Lee ) 생화학분자생물학회 1981 BMB Reports Vol.14 No.3
A form of lipoxygenase (EC 1. 13. 11. 12) was isolated from rice brans which were obtained from the milling of rice caryopsis, and was purified partially but to give an electrophoretically homogeneous form. The molecular weight of the enzyme was found to be about 100, 000 daltons based on the gel filtration experiment. The optimum activity for the catalytic hydroperoxidation by rice bran lipoxygenase was obtained at neutural pH (pH 6. 8 to 7. 0) and at 30℃. The enzyme show ed a relative stability under the neutral pH and at room temperature, but a marked deactivation of the enzyme protein was observed at the preincubation temperature abov a 50℃. The first order deactivation constants for the enzyme were calculated to be 0.002, 4.014, 0.136 and 0.281 per minute at 40, 50, 60 and 70℃, respectively. The isoelectric point of the enzyme was about 4. 8 based on the isoelectrofocusing experiment, The enzyme was found to be very specific toward linoleate for the hydroperoxidation as in the case of the soybean enzyme, but the estimated K_m values for linoleate and molecular oxygen were found to be about the same. Based on the steady state kinetic experiment measuring the initial velocity of the enzyme reaction, it was also suggested that the hydroperoxidation of linoleate is proceeded through the formation of a ternary complex between the enzyme and two substrate ligands.
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디티오트레이톨과 철 ( 3 ) 이온에 의한 대장균 글루타민 합성효소의 비효소적 절단에 대한 연구
전덕영,김강화,변시명 ( Deok Young Jhon,Kanghwa Kim,Si Myung Byun ) 생화학분자생물학회 1989 BMB Reports Vol.22 No.4
Optimum reaction condition for the cleavage of Escherichia coli glutamine synthetase in the presence of oxygen, iron(III), and dithiothreitol has been established. The condition is 5 mM dithiothreitol, 0.1 mM iron(III), pH 7.0, 37℃, and 4hours of reaction time, when the enzyme concentration is 0.06 mM as subunit basis. The cleavage pattern strongly depends on the addition of ligands of the enzyme, glutamic acid, glutamine, L-methionine-S-sulfoximine, to the reaction mixture while the ligands do not change the cleavage pattern of rabbit muscle pyruvate kinase which is also attacked by the cleavage system. The results indicate that the cleavage reaction occurrs at the polypeptide segments which consist the active site of the glutamine synthetase.
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