새조개 가공부산물을 이용한 속성 액젓의 제조 및 저장안정성

김명희,조영철,배태진,손정호,김귀식 여수대학교 1997 論文集 Vol.11 No.2

A rapid processing for fermented fish sauce from cockle shell by-product and their quality and storage stability was investigated. The weight ratio of cockle shell by-product about the whole cockle shell was 32.7%, and contents of moisture, portein, lipid, carbohydrate and ash were 83.1%, 10.7%, 2.4%, 1.0% and 2.9%, respetively. The cockle shell by-product was homogenized with addition of water and hydrolyzed at 50℃ for 8 hours added 4% Protease N.P.(3.14ㆍ10⁴U/g). The hydrolysate was thermally treated at 100℃ for 60 minutes with 4% invert sugar and 20% table salt was finally added to the product. The chemical compositon of moisture, carbohydrate, ash, salinity, total nitrogen and amino type nitrogen of fermented sauce from cockle shell by-product were 65.4%, 3.9%, 20.8%, 18.9%, 1,683 mg% and 1,426 mg%, respectively. The major nucleotides and their relative compounds in the product were AMP and hypoxanthine and their contents were 3.36μ mole/g and 1.95μ mole/g. And major free amino acid were glutamic acid, lysine, leucine, valine and aspatic acid.

정상 성인에서 총콜레스테롤의 분별치와 관련 요인 : 전북지역 한 종합병원의 정기검진자를 중심으로

김지식,여영규,홍인선 THE KOREAN SOCIETY FOR BIOMEDICAL LABORATORY SCIEN 1996 Journal of biomedical laboratory sciences Vol.2 No.2

정상 성인에서 혈청 총 콜레스테롤의 분별치 및 관련된 제요인을 파악하기 위하여 1995년 3월부터 10월까지 8개월 동안 전주 예수병원에서 의료보험 피보험자와 피부양자를 대상으로한 정기 건강 검진을 받은 대상자 중 성별, 연령별, 혈압, 체중, 기타 생화학적 검사 결과를 분석하였으며, 이들 중 고혈압 등 질병이 없는 건강한 집단으로 1,818명을 분석하였다. 혈청 총 콜레스테롤의 분별치를 산정 하기 위한 75th percentile값을 보면, 21∼30세군에 191 mg/dl, 31∼40군에서 195 mg/dl, 41∼50세군에서 214 mg/dl, 51∼60세군에서 227 mg/dl, 그리고 61세 이상 군에서 222 mg/dl이었다. 90th percentile값을 보면, 21∼30세군에서 214 mg/dl, 31∼40군에서 214 mg/dl, 41∼50세군에서 239 mg/dl, 51∼60세군에서 253mg/dl, 그리고 61세 이상군에서 248 mg/dl 이었다. 혈청 총 콜레스테롤과 각 변수간의 상관관계는 연령과는 남.여 모두 유의한 관계를 보였고(p<0.001), 특히 여자에서 높은 상관성을 보였다. 비만지수인 PIBW, BMI와도 유의한 상관성을 보였고, 수축기혈압과 이완기혈압과도 관련성을 보였다. 대상자들의 흡연 여부와 혈청 총 콜레스테롤과의 관계는 흡연군이 191.6±35.0 mg/dl 이었고, 비흡연군이 194.9±35.9 mg/dl였으며 두 집단간에는 유의한 차이를 보이지 않았다. 음주에 따른 혈청 총 콜레스테롤의 측정치는 비음주군에서는 196.0±36.0 mg/dl 이었고, 음주군에서는 188.9±34.5 mg/dl로 두 군간에는 유의한 차이를 보였다. 운동 습관과 혈청 총 콜레스테롤의 관계는 규칙적으로 운동을 하는 군은 192.1±33.3 mg/dl이었고, 운동을 하지 않는 군은 195.8±37.0 mg/dl였으며 두 군간에는 유의한 차이를 보였다. The cut-off values and related factors for total cholesterol of serum in normal Korean adults were studied from March to October, 1995, based on the data of 1,818 healthy adults of human involved the male and female. The comparisons of the serum total cholesterol levels were analyzed by sex, age, systolic blood pressure, diastolic blood pressure, body weight, height, PIBW, BMI and other biochemical tests. 1. The serum total cholesterol level were 194.4 mg/dl in total group, 186.9 mg/dl for male, and 197.6 mg/dl for female. 2. There was no significant differences by sex among the 21 to 50 ages group, but significantly higher in women than in men over 51 years old. 3. In general, the levels of serum total cholesterol were increased with age, the highest level in men was 192.7 mg/dl in 51 to 60 years old, and 210.5 mg/dl in more than 60 years old in women. 4. The cut-off values of serum total cholesterol for moderate risk were 191 mg/dl in 21 to 30 years group, 195 mg/dl in 31 to 40 years, 214 mg/dl in 41 to 50 years, 227 mg/dl in 51 to 60 years, and 222 mg/dl in more than 61 years. The cut-off values of serum total cholesterol for high risk were 214 mg/dl in 21 to 30 years group, 214 mg/dl in 31 to 40 years, 239 mg/dl in 41 to 50 years, 253 mg/dl in 51 to 60 years, and 248 mg/dl in more than 61 years. 5. The mean values of serum total cholesterol were showed positive correlation with age, PIBW, BMI, systolic blood pressure and diastolic blood pressure. 6. Serum total cholesterol level of drinking group(188.9±34.5mg/dl) was showed lower than those of non-drinking group(196.0±36.0mg/dl). 7. Serum total cholesterol levels of regular excercise group(192. 1±33.3 mg/dl) was significantly lower than those of non regular excercise group(195.8± 37.0 mg/dl).

대학의 홍보가 대학 이미지 및 경쟁력 지각에 미치는 영향에 관한 연구 : 2년제 대학의 홍보전략을 중심으로

정형식,김영심,김영인 朝鮮大學校 2002 經營經濟硏究 = Management and economics research Vol.25 No.1

Evaluation of Anti-inflammatory Components in Glycyrrhizae Radix and Identification of the Active Ingredients

KIM Yeong Shik,SHIN Eun Myoung,GOO Lianyu,HONG Yoo Na,CHOI Yong Hwan,KIM Hyun Pyo,KIM Jeong Ah,LEE Seung Ho,KANG Sam Shik 大韓藥學會 2006 大韓藥學會 總會 및 學術大會 Vol.2006 No.1

Purification and Characterization of ${\beta}$-Galactosidase from Green Onion

Kim, Yeong-Shik,Park, Kyung-Shin,Kim, Jong-Goon 생화학분자생물학회 1993 한국생화학회지 Vol.26 No.7

${\beta}$-D-Galactosidase from the mature tissues of green onion was purified to homogeneity using a procedure involving gel-filtration, anion-exchange chromatography, hydroxyapatite chromatography, and affinity chromatography on ${\rho}$-aminobenzyl-1-thio-${\beta}$-D-galactopyranoside-agarose. Its molecular weight was estimated to be 52,000 Da and its isoelectric point was 6.5. The overall yield was 0.2% and specific activity was increased approximately 380 folds. Activity was maximum at pH 4 and $50^{\circ}C$. The purified enzyme was demonstrated to be specific to Gal-${\beta}$1-6 linkage using fluorescence-labeled substrates.

Identification of Chitinolytic System in Allium fistulosum

Kim, Yeong-Shik,Lee, Eun-Bang,Joo, Sun-Hee The Pharmaceutical Society of Korea 1991 Archives of Pharmacal Research Vol.14 No.3

Chitinase was partially purified from Allium fistulosum L (green onion_. Protein fraction precipitated from ammonium sulfate was passed through CM-Sepharose and Sephacryl HR-200. The specific activity of the chitinase was 6.4 units/mg and total recovery was 6.3%. The analysis of the products from the digestion of N-acetychitohexaose indicated that chitinase was endo in action, with oligerms from N-acetylchitobiose to chitotetraose. N-Acetylglucosaminidase from the same species hydrolyzed oligomers obtained from chitinase reaction to lower oligosaccharides. These data demonstrated that chitinolytic system exists in green onion.

Glycosaminoglycan lyases and acharan sulfate

Yeong Shik Kim 한국당과학회 2009 한국당과학회 학술대회 Vol.2009 No.1

Glycosaminoglycans (GAGs) are unbranched, polydisperse, acidic polysaccharides, often covalently linked to a protein core to form proteoglycans (PGs). The most common GAGs are heparin, heparan sulfate (HS), hyaluronic acid (HA), chondroitin sulfate (CS), dermatan sulfate (DS), and keratan sulfate (KS). Heparin, an anticoagulant isolated from animal tissue, is an important and chemically unique polysaccharide of considerable biological significance. In order to understand the complicated structure of GAGs, GAG lyases from microorganisms have been widely used and their reaction products were analyzed using various HPLC methods. We have cloned and expressed GAG lyases of Bacteroides thetaitaomicron in E.coli. In collaboration with Dr Mirek Cygler’s group, the tertiary structures of recombinant chondroitinases ABC and heparinase have been solved. These things will be presented. Acharan sulfate (AS), isolated from the giant African snail Achatina fulica, primarily consists of the repeating disaccharide structure a-D-N-acetylglucosaminyl (1→4) 2-sulfoiduronic acid. Its structure is related to heparin and heparan sulfate but is distinctly different from all known members of these classes of glycosaminoglycans. Because of its structural similarities to heparin, a diverse array of biological activities and functions have been studied. Because of its high molecular weight and copper binding affinity, specific proteins in the plasma could be purified by affinity chromatography.

Purification and Characterization of Heparin Lyase I from Bacteroides stercoris HJ-15

Kim, Wan-Seok,Kim, Byung-Taek,Kim, Dong-Hyun,Kim, Yeong-Shik Korean Society for Biochemistry and Molecular Biol 2004 Journal of biochemistry and molecular biology Vol.37 No.6

Heparin lyase I was purified to homogeneity from Bacteroides stercoris HJ-15 isolated from human intestine, by a combination of DEAE-Sepharose, gel-filtration, hydroxyapatite, and CM-Sephadex C-50 column chromatography. This enzyme preferred heparin to heparan sulfate, but was inactive at cleaving acharan sulfate. The apparent molecular mass of heparin lyase I was estimated as 48,000 daltons by SDS-PAGE and its isoelectric point was determined as 9.0 by IEF. The purified enzyme required 500 mM NaCl in the reaction mixture for maximal activity and the optimal activity was obtained at pH 7.0 and $50^{\circ}C$. It was rather stable within the range of 25 to $50^{\circ}C$ but lost activity rapidly above $50^{\circ}C$. The enzyme was activated by $Co^{2+}$ or EDTA and stabilized by dithiothreitol. The kinetic constants, $K_m$ and $V_{max}$ for heparin were $1.3{\times}10^{-5}\;M$ and $8.8\;{\mu}mol/min{\cdot}mg$. The purified heparin lyase I was an eliminase that acted best on porcine intestinal heparin, and to a lesser extent on porcine intestinal mucosa heparan sulfate. It was inactive in the cleavage of N-desulfated heparin and acharan sulfate. In conclusion, heparin lyase I from Bacteroides stercoris was specific to heparin rather than heparan sulfate and its biochemical properties showed a substrate specificity similar to that of Flavobacterial heparin lyase I.

Compositional Sugar Analysis of Antitumor Polysaccharidees by High Performance Liquid Chromatography and Gas Chromatography

Kim, Yeong-Shik,Park, Kyung-Shin,Park, Ho-Koon,Kim, Sung-Whan The Pharmaceutical Society of Korea 1994 Archives of Pharmacal Research Vol.17 No.5

Carbohydrate analysis is important in studying structure and activity of complex polysaccharides. New analytical method was applied to get an information on the composition of polysaccharides showing antitumor activity. Monosaccharides were labeled with 7-amino-1, 3-naph-thalenedisulfonic acid (7-AGA) by reductive amination and separated by HPLC. Five kinds of polysaccharides from Basidiomycetes were hydrolyzed and analyzed in combination with electrophresis and HPLC. At the same time, alditol acetate derivatives were prepared and analyzed by gas chromatography. Two different techniques using different derivatization methods showed very similar results. The monosaccharides from Coriolus versicolor and Cordyceps militaris were glucose and galactose. Phellinus linteus composed of glucose, glactose, mannose, arabinose and fucose. The HPLC method with fluorescence detector was very sensitive compared to other methods.

Biochemical Characterization of Serine Proteases with Fibrinolytic Activity from Tenodera sinensis (Praying Mantis)

Kim, Yeong-Shik,Hahn, Bum-Soo,Cho, So-Yean,Chang, Il-Moo The Korean Society of Toxicology Korea Environment 2001 Toxicological Research Vol.17 No.-

Three types of proteases (MEF-1, MEF-2 and MEF-3) were purified from the egg cases of Ten-odera sinensis using ammonium sulfate fractionation, gel filtration on Bio-Gel P-60 and affinity chromatography on DEAE Affi-Gel blue gel. The proteases were assessed homogeneous by SDS-polyacrylamide gel electrophoresis and have molecular weight of 31,500, 32,900 and 35,600 Da, respectively. The N-terminal regions of the primary structure were compared and they were found to be different each other. MEFs readily digested the $A\alpha$ - and B$\beta$-chains of fibrinogen and more slowly the ${\gamma}$-chain. The action of the enzymes resulted in extensive hydrolysis of fibrinogen and fibrin, releasing a variety of fibrinopeptides. MEF-1 was inactivated by Cu$^{2+}$ and Zn$^{2+}$ and inhibited by PMSF and chymostatin. MEF-2 was inhibited by PMSF, TLCK. soybean trypsin inhibitor. MEF-3 was only inhibited by PMSF and chymostatin. Antiplasmin was not sensitive to MEF-1 but antithrombin III inhibited the enzymatic activity qf MEF-1. MEF-2 specifically bound to anti plasmin Among the chromogenic protease substrates, the most sensitive one to the hydrolysis of MEFs was benzoyl-Phe-Val-Arg-p-nitroanilide with maximal activity at pH 7.0 and 3$0^{\circ}C$. MEF-1 preferentially cleaved the oxidized B-chain of insulin between Leu15 and Tyr16. In contrast, MEF-2 specifically cleaved the peptide bond between Arg23 and Gly24. D-dimer concentrations increased on incubation of cross-linked fibrin with MEF-1, indicating the enzyme has a strong fibrinolytic activity.ity.