Atrophic Rhinitis Vaccine의 액체배지에서 항원 생성에 관한 연구 : 제1보. 최적 항원 생성 배지 결정 part 1. Optimum composition of media ingredients for antigenicity

권태종,박세철 건국대학교 산업기술연구원 1996 건국기술연구논문지 Vol.21 No.-

In order to develope an effective production method of Atrophic Rhinitis (A. R.) vaccine, the physiological characteristics of Bordetella bronchiseptica, causative pathogen of A. R. in swine, were investigated by using the immunological techniques. The optimum culture conditions for the cell growth and epitome production of Bordetella bronchiseptica were monosodium glutamate 2.0%, yeast extract 1.0%, magnesium chloride 0.1%, and riboflavin 0.003%, initial pH 7.4 for 48hrs.

Photoshop을 이용한 하악 후퇴 수술후의 연조직 안모 예측

권대근,김종배 대한악안면성형재건외과학회 2002 Maxillofacial Plastic Reconstructive Surgery Vol.24 No.4

Various computer software has been applied to predict soft tissue profile after orthognathic surgery. In this study, the Photoshop program was introduced to simulate the surgical result. The purpose of the study was to evaluate reliability of the program in prediction of profile changes as a result of mandibular set-back surgery. Based on predicted hard tissue changes, soft tissue changes were recorded with pre- and post-operative lateral cephalogram of 26 patients with skeletal Class Ⅲ deformity. All patients underwent bilateral sagittal split osteotomy. The mean mandibular set-back was 6.2㎜ (Pog) and soft tissue moved 6.3㎜, 100% in Pog' point post-operatively. Difference between the between real horizontal soft tissue changes and predicted changes has not been detected statistically. However, the result revealed vertical soft tissue profile prediction was unsatisfactory. This prediction method can be used as additional informative tool for the patient explanation.

Methanol 자화성 효모에 의한 균체 단백질 생산

권태종,이동희,정호권,최태부 건국대학교 1992 學術誌 Vol.36 No.2

SCP producing yeast JAM -3032 that has high productivity potential with methanol as carbon and energy source was isolated from soil, and conditions for SCP production, nutritional values, and alcohol oxidase of the microorganism were investigated. Isolated strain JAM-3032 was identified as Pichina on the morphological, cultural, physiological and biochemical characteristics. The production of cell mass reached at maximal level after 54 hrs cultivation at 28℃, pH 6.0 in the medium containing methanol 3.0%, yeast extract 0.8%, K2HPO4 0.1%, KH2PO4 0.1%. MgSO4ㆍ7H2O 0.05%, alanine 0.01%, nicotinic acid 0.04%, and biotin 0.04%. Dry cells of Pichia sp. JAM -3032 was composed of proteins 53.3%, carbohydrates 31. 5%, nucleic acids 5.6%, lipids 2.9%, ash 6.4% and amino acid composition of the proteins was satisfied in FAO reference. Biosynthesis of the alcohol oxidase of the strain JAM -3032 was induced by methanol. The enzyme was purified by treatment of ammonium sulfate fractionation, DEAE-Sephadex A-50 ion exchange chromatography and Sepharose 6B gel nitration. The purified enzyme was homogeneous on SDS-PAGE, and molecular weight was estimated to be about 520,000 D that was consisted of 8 subunits containing FAD as coenzyme. The optimal pH and temperature for the enzyme reaction was 7.5 and 37℃, respectively. Activation energy was 17.1Kcal/mol and half inactivating temperature was 40℃. The enzyme activity was inhibited by Ag+, Cu2+ and Hg2+ ions remarkably. The enzyme acted on methanol specifically, and its Km value was 0.89 mM.

α-Amylase Inhibitor 생산균 Streptomyces sp. AI-118의 분리 및 동정

권태종,서동진 建國大學校 附設 産業技術硏究所 1992 논문집 Vol.17 No.-

a-amylase의 효소작용을 저해하는 물질을 생산하는 균주를 토양에서 분리, 동정하였으며 저해물질 생산의 최적 조건을 검토하였다. 본균을 방선균 종정법에 따라 결과 새로운 균주로 판명되어 Streptomyces sp. AI-118이라고 명명하였다. 본 균주는 탄소원으로 corn starch 3.0%, 질소원으로 soy bean meal 1.0%, 무기염으로 NaCI 0.05%, MnSO₄·4H₂O 0.0001%, CuSO₄·5H₂O 0.0001%를 사용한 배지에서 initial pH 6.0, 30℃ 그리고 배양 72시간일 때 최대의 저해물질을 생산하였다. A microorganism, strain AI-118, capable of producing a new a-amylase inhibitor in culture broth was isolated from soil and identified as Streptomyces sp. on the morphological, cultural and physiological characteristics. The preferable medium composition has been determined to be as follows:3.0% corn starch, 1.0% soy bean meal, 0.05% NaCl, 0.05% K₂HPO₄, 0.0001%MnSO₄· 4H₂O and 0.0001% CuSO₄·5H₂O(pH6.0). The inhibitor was maximally produced after 60-80hr cultivation in a jar fermentor at 30℃.

스테인리스강 용접부의 잔류응력이 피로특성에 미치는 영향

권종완,양현태 한국공작기계학회 2001 한국생산제조학회지 Vol.10 No.5

In the weldments, the crack propagation rate is changed due to the residual stress. The crack propagation rate is high in the region with the residual stress. However it shows the same behavior with the base metal in the region that does not include the residual stress. The fatigue crack growth rate for the material with residual stresses can be predicted more precisely by using the effective stress ratio. The difference between experimental results and prediction results seems to be due to the redistribution of the residual stresses and microstructural change.

알칼리수의 3 차원 초분자 구조에 관한 컴퓨터 분자 모델링

권태종,정호권,강상모,이동희,정선호 건국대학교 산업기술연구원 1997 건국기술연구논문지 Vol.22 No.-

The supramolecular structures of an alkaline or mineral water molecule were simulated and their various structural and dynamical properties were studied in comparison with those of the pure water molecules. Molecular modeling was performed with Quanta molecular interface program under the CHARm forcefields. Molecular mechanic calculation and molecular dynamic calculation were performed for pure and alkaline supramolecular water structures. The change of the number of hydrogen bondings, radius of Gyration and total dipole moment of the supramolecular structures for pure and alkaline water molecules were investigated as a function of temperature. Alkaline or mineral water were shown to be more energetically stable, more compact and more capable in formation of hydrogen bonds in their supramolecular structures.

효모(pichia sp. JAM-3032)가 생산하는 Methanol oxidase의 정제 및 성질

權泰鍾 건국대학교 1993 學術誌 Vol.37 No.2

Alcohol oxidase produced by methanol utilizable Pichia sp. JAM-3032 was purified and its characteristics were investigated. The enzyme was purified 2.5-fold by precipitation with ammonium sulfate, DEAE-Sephadex A-50 and Sephadex G-200 column chromatography with yield of 25.3% from cell free extract. The alcohol oxidase was composed with eight subunits, and each subunit contained one FAD as prosthetic group and Mg2+ as cofactor. Pichia JAM-3032 alcohol oxidase contained higher percentage of glycine and alanine, but lower tyrosine and glutamic acid compared with Kloeckera alcohol oxidase.

Bacillus속의 균주가 생산하는 Alkali성 단백질 분해효소의 성질 : 제 2 보.Bacillus alcalophilus가 생산하는 Alkaline protease의 생산 part 2. Production of alkaline protease from Bacillus alcalophilus

權泰鐘,康福哲 建國大學校 附設 産業技術硏究所 1993 논문집 Vol.18 No.-

전보에서 분리 동정한 Bacillus alcalophilus를 공시균으로 하여 alkaline protease를 생산하기 위한 최적조건을 검토한 결과는 다음과 같다. 1) 효소생산에 있어서 탄소원으로는 glucose가 효과적이었으며 그 최적농도는 0.8%였다. 2) 유기 질소원으로는 soybean meal 1.5% 첨가에 의하여 효소 생산량이 가장 높았다. 3) 탄산염으로 Na₂CO₃를 1.5% 첨가하였을 경우 효소의 생산량이 높았다. 4) 금속염으로는 MgSO₄·7H₂O를 최종농도가 2mM로 첨가하였을때 약 5.2배 증가되었다. 5) isoleucine 0.3% 첨가시 효소 생산량이 약 2.5배 증가되었다. 6) alkaline protease 생산시 초발 pH는 12였으며 최적온도는 40℃, 배양시간은 72시간에 최고치를 보였다. Cultural conditions for production of the alkaline protease by Bacillus alcalophilus was investigated. For the enzyme production, 0.8% glucose and 1.5% soybean meal was favorable as carbon and nitrogen source, respectively. The enzyme production was increased by the addition of Na₂CO₃ at the concentration of 1.5%. Addition of 2mM of MgSO₄7H₂O and 0.3% isoleucine increased the enzyme formation with 5.2 and 2.5-fold, respectively. Optimal initial pH for the enzyme production was pH 12 and temperature was 40℃. The enzyme production reached at maximum level after 72 hrs cultivation.

Aspergillus sp.(C-58) 菌株가 生産하는 Inulin 分解酵素에 關한 硏究 : Part2. The effect of culture conditions on the soild cultivation 第二報 固體培養에 따른 培養條件

權泰鍾 건국대학교 1981 學術誌 Vol.25 No.1

A strain of Aspergillus species C-58 was produced much inulin hydrolyzing enzyme(EC 3.2.1.7) in wheat bran solid medium than glucose liquid medium Optimal conditions for the inulase production by Asp. sp. C-58 strain on wheat bran solid medium were established. The results were as follows. 1.Optimal content of moisture on the inulase production at the wheat bran solid medium was about 50% 2.Inulase production on the wheat bran medium from Asp. sp. C-58 strain was increased by addition of 3%-glucose solution. 3.Organic nitrogen sources, inorganic nitrogen sources and inorganic salts which there were no or very little increase in wheat bran medium. 4.Effectual initial pH on the inulase production were pH 4.0 to 5.0. 5.Optimum culture period on the inulase production was to be 5 days.

Bacillus 속의 균주가 생산하는 Alkali성 단백질 분해효소의 성질 : Park 3. Properties and purification of alkaline protease produced by Bacillus alkalophilus 제3보. Bacillus alkalophilus가 생산하는 Alkaline protease 의 정제 및 성질

權泰鐘,康福哲 건국대학교 산업기술연구원 1994 건국기술연구논문지 Vol.19 No.-

Bacillus alkalophilus가 생산하는 alkaline protease의 성질을 조사하기 위하여 acetone 침전법, DEAE-Sephadex A-50 column chromatography법, CM-cellulose column chromatography법과 Sephacryl S-200을 이용한 gel filtration법으로 약 9.6배 정제하였으며, 정제효소는 acrylamide gel electrophoresis에 의하여 단일 band를 보였다. 정제효소의 최적 pH는 pH 11∼12였으며 안정 pH 범위는 pH 8∼12였다. 정제효소의 최적온도는 50℃였으며 열에 대한 안정성은 ??? ion 존재하에서는 55℃까지였다. Li₂SO₄, MgSO₄, CaCl₂에 의하여 효소작용이 촉진되었으며 HgCl₂, AgNO₃및 FeSO₄에 의하여 저해되었다. 본 효소는 PMSF, EDTA, SDS 및 iodoacetic acid에 크게 저해되었다. 본 정제 효소는 Tween계 계면활성제에 의하여 촉진되었으며 음이온계 계면활성제에 의하여 약 33% 저해되었다. 본효소의 Km치는 casein을 기질로 하였을 때 효소 ml당 0.44%였으며 ???는 9,000unit/ml이었다. An alkaline protease produced by Bacillus alkalophilus was purified and characterized. The enzyme was purified about 9.6 folds by acetone precipitation, DEAE-Sephadex A-50 and CM-cellulose column chromatography and gel filtration with Sephacryl S-200, and showed a single band on acrylamide gel electrophoresis. The optimal pH and temperature were around 11~12 and 50℃, respectively. The enzyme was stable in the pH range of 8∼12 and up to 55℃ in the presence of ???. The enzyme activity was stimulated by Li₂SO₄, MgSO₄, CaCl₂and surface active agent as Tweens but inhibited by AgNO₃and HgCl₂, PMSF, EDTA, SDS, iodoacetic acid and anionic detergent. The Km and Vmax of the enzyme for casein were 0.44% and 9,000 U/ml, respectively.