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가축분뇨를 이용한 SCP 생산 균주의 분리 및 균체 단백질 생산
한석균,고유석,안태영,배동훈 한국미생물생명공학회 ( 구 한국산업미생물학회 ) 1996 한국미생물·생명공학회지 Vol.24 No.6
질소원으로서 계분을 이용하는 균주를 선별하고 계분배지에서 균체의 생육속도가 다른 균주에 비하여 우수한 균주를 분리하였다. 형태·생리학적 특성을 기초로 하여 yeast의 분류 기준과 비교하여 본 균주를 Candida sp.로 동정하였으며 본 균주를 Candida sp. D116으로 명명하였다. Poultry feces extract medium에서 4% 농도의 glucose 첨가가 균체 생육에 효과적이었다. D116 균주를 액체 발효하여 균체생산능, 요산 그리고 가용성 단백질의 변화를 조사하였다. 그 결과 약 60시간이 경과하면 액체 발효 배지내의 거의 모든 가용성 단백질 및 요산의 감소를 보였으며 균체생육은 약 36시간 배양하였을 때 최고조에 도달하였고 그 후에는 점차 감소하는 경향을 보였다. SCP의 대량생산의 결과 50%의 계분혼합 배지와 30℃의 배양 온도에서 36시간 배양하여 균주의 생육수준이 3.8×10^9 CFU/ml 농도의 균체를 생산하였고 200 L의 배양액중 약 870 g-dw의 균체를 얻었으며 생산된 군체의 조단백질 함량은 67%이었다. Production of Single Cell Protein from Poultry Feces. Suk-kyun Han, You-Suk Go, Tae-Young Ahn and Dong-Hoon Bal^1*. Deparment of Microbioligy, College of Natural Sciences, Dankook Univerity, Cheonan 330-714 and Research Center for Molecular Microbiology, Seoul Nationa University, Seoul 151-742, Korea, ^1Department of Food Engineering. College of Engineering, Dankook University, Cheonan 330-714 and Bioproducts Research Center of Yonsei University, Seoul 120-749, Korea - From the soil collected form provincial area of South Korea, a microorganisms which have been shown good growth in the minimal poultry feces extract medium was isolated. Supplement of glucose to the poultry feces extract medium helped the complete degraded during the microbial growth. Maximum cell growth (3.8×10^9 CFU/ml) obtained at 36 hours of incubation after inoculation. Uric acid was degraded faster in minimal medium that in the glucose complement medium. VFA (volatile fatty acid), which are known as major compounds of poultry feces odor, were almost removed from the minimal poultry feces extract medium. Glucose supplement to the minimal medium enhanced the growth of microbial cells. Addition of 4% of glucose and 4% of neopeptone to the minimal poultry feces extract medium helped the maximal growth of cells.
南勝義,金聖培,金錫胤 弘益大學校 1982 弘大論叢 Vol.14 No.2
A study has been performed on the mechanical properties and the micro-structure of the welded zone in the high tensile steel produced in Korea. The experimental results indicated that the tensile strength and the hardness were increased in welded zone. The micro-structure of the welded zone was finer than that of the base metal. It may be considered that the increase of the mechanical properties is due to the chemical composition of electrode being different from the base metal and to the structure getting finer through the course of solidification.
Bai, Suk,Chun, Soon Bae,Im, Suhn Young,Choi, Won Ki,Lee, Jin Jong 생화학분자생물학회 1978 BMB Reports Vol.28 No.5
Two forms of glucoamylase (GI and GII) from starch-grown Lipomyces kononenkoae CBS 5608 mutant were purified to apparent homogeneity by means of ultrafiltration, Sephacryl S-200 gel filtration and DEAF Sephadex A-50 chromatography. The apparent molecular weight was calculated as ca. 150 kDa for GI and ca. 128 kDa for GII, respectively. Both enzymes were glycoproteins with isoelecMc points of 5.6 (GI) and 5.4 (GII). They had a pH optimun of 4.5 and were stable from pH 5 to 8. The temperature optimum for both enzymes was 6090, but they were rapidly inactivated above 70�. The Km values toward starch were estimated to be 6.57 ㎎ per ㎖ for GI and 4.52 ㎎ per ㎖ for GII, and the V_(max) values were 16.28 μM per ㎎ for GI and 32.25 μM per ㎎ for GII, respectively. The K_m and Vmax values of GII for a- or p-cyclodextrin were estimated to be 0.15 ㎎ per ㎖ and 2.0 ㎎ per ㎖, respectively (K_m) and 1.02 μM per ㎎ or 1.02 μM per ㎎, respectively (V_(max)). Neither enzyme exhibited pullulanase activity but they released only glucose from starch or cyclodextrin. Amino acid analysis indicated that both glucoamylases were enriched in proline and acid amino acids. Glucoamylase GII strongly cross-reacted with a monoclonal antibody rnised against GI enzymes, and the two enzymes shared very similar amino acid composition. Western blot analysis indicated that L. kononenkoae CBS 5608 mutant produced two forms of glucoamylase on starch, and that synthesis of them was subject to glucose repression.
배진숙(Jin Suk Bai),이명하(Myung Ha Lee) 한국간호행정학회 2005 간호행정학회지 Vol.11 No.4
This study is to identify the effect of organizational characteristics on knowledge sharing in a general hospital nurses. Method: The objects of this study were 358 nurses who had worked in a general Hospital. Data were collected from May, 3rd to May, 10th in 2004 through questionnaire. Five structured Instruments were used to collect the data. Result: The knowledge sharing of nurses was the positive correlation with openness of communication, learning orientation, the support of director of nursing department, and application of information technology(r=431∼611, p=000). The degree of nurse`s knowledge sharing showed a significant difference according to nurses` education level, duration of working, duty shift, working field, position in Hospital(p=.05). Openness of communication appeared into a most important predictor in knowledge sharing of Nurses, and then was learning orientation, the support of director of nursing department, application of information technology in order(p=.000). All of these variables explained 55.1% of knowledge sharing of nurses. Conclusion: To increase knowledge sharing of nurses, nursing organization will have to make up organization culture of opening communication and learning orientation of nurse, promote up the support of director of nursing department and application of information technology.
Chun, Soon-Bai,Bai, Suk,Im, Suhn-Young,Choi, Won-Ki,Lee, Jin-Jong Korean Society for Biochemistry and Molecular Biol 1995 Journal of biochemistry and molecular biology Vol.28 No.5
Two forms of glucoamylase (GI and GII) from starch-grown Lipomyces kononenkoae CBS 5608 mutant were purified to apparent homogeneity by means of ultrafiltration, Sephacryl S-200 gel filtration and DEAE Sephadex A-50 chromatography. The apparent molecular weight was calculated as ca. 150 kDa for GI and ca. 128 kDa for GII, respectively. Both enzymes were glycoproteins with isoelectric points of 5.6 (GI) and 5.4 (GII). They had a pH optimun of 4.5 and were stable from pH 5 to 8. The temperature optimum for both enzymes was $60^{\circ}C$, but they were rapidly inactivated above $70^{\circ}C$. The $K_m$ values toward starch were estimated to be 6.57 mg per ml for GI and 4.52 mg per ml for GII, and the $V_{max}$ values were 16.28 ${\mu}M$ per mg for GI and 32.25 ${\mu}M$ per mg for GII, respectively. The $K_m$ and $V_{max}$ values of GII for ${\alpha}-$ or ${\beta}-cyclodextrin$ were estimated to be 0.15 mg per ml and 2.0 mg per ml, respectively ($K_m$) and 1.02 ${\mu}M$ per mg or 1.02 ${\mu}M$ per mg, respectively ($V_{max}$). Neither enzyme exhibited pullulanase activity but they released only glucose from starch or cyclodextrin. Amino acid analysis indicated that both glucoamylases were enriched in proline and acid amino acids. Glucoamylase GII strongly cross-reacted with a monoclonal antibody raised against GI enzymes, and the two enzymes shared very similar amino acid composition. Western blot analysis indicated that L. kononenkoae CBS 5608 mutant produced two forms of glucoamylase on starch, and that synthesis of them was subject to glucose repression.
Jo, Young Suk,Hwang, Eun Suk,Lee, Ju Hee,Lee, Yunhyeong,Kim, Seul Young,Choi, Yun-Sun,Bai, Youn-Sun,Hong, Jun Hwa,Kim, Yun-Jeung,Lee, Ihn-Suk,Rha, So Young,Ro, Heung-kyu,Shong, Minho The Korean Academy of Medical Sciences 2008 JOURNAL OF KOREAN MEDICAL SCIENCE Vol.23 No.2
<P>Members of the inhibitors of differentiation (Id) family of helix-loop-helix (HLH) proteins are known to play important roles in the proliferation and differentiation of many cell types. Thyroid-stimulating hormone (TSH) regulates proliferation and differentiation by activating TSH receptor (TSHR) in thyrocytes. In this study, we found that Id2, one of the Id family proteins, is a major target for regulation by TSH in FRTL-5 thyroid cells. TSH rapidly increases the Id2 mRNA level in FRTL-5 thyroid cells but the Id2 protein showed biphasic regulatory patterns, being transiently reduced and subsequently induced by TSH treatment. Transient reduction of Id2 protein was noted within 2 hr of TSH treatment and was mediated by proteasomal degradation. Moreover, reduced Id2 expression correlated with the activity of the phosphatidylinositol 3 kinase pathway, which is activated by TSH. Although TSH increases the activity of the Id2 promoter, TSH-induced activation of this promoter was independent of c-Myc. Id2 did not alter TTF-1- and Pax-8-mediated effects on the regulation of the Tg promoter. Thus, in summary, we found that TSH regulates Id2 expression, but that Id2 does not alter the expression of thyroid-specific genes, such as Tg, in FRTL-5 thyroid cells.</P>