• Proceedings of the Korean Biophysical Society Conference
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• 2003.06a
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• pp.57-57
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• 2003

In growing number of diseases it has been shown that aggregation of specific proteins has an important role in pathogenesis of the disorder. This has been demonstrated in structural details with the liver cirrhosis of ${\alpha}$$_1$-antitrypsin deficiency, and it is now believed that similar protein aggregation underlies many neurodegenerative disorders such as autosomal dominant Parkinson disease, prion diseases, Alzheimer disease, and Huntington disease. ${\alpha}$$_1$-Antieypsin, a member of serine pretense inhibitor (serpin) family, functions as an inhibitor of neutrophil elastase.

• Journal of the Korean Society of Food Science and Nutrition
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• v.6 no.1
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• pp.27-33
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• 1977

The alkaline protease was isolated from the culture of Penicillium species (P-46) grown in the wheat bran media. The crude purification of this enzyme was carried out by extraction with distilled water and precipitated with 0.7-saturated ammonium sulfate, then dialysis for 3days. The activity of this enzyme was determined by Folin's colorimetric method. The results were as follows; 1. The optimum pH and temperature of this enzyme were pH 8.4 and $45^{\circ}C$. 2. This enzyme was stable at pH $7.0{\sim}9.0$. 3. This enzyme was not inactivated by treatment in lower temperature than $30^{\circ}C$. 4. The activity of this enzyme was strongly inhibited by $Hg^{++}$ and $Cu^{++}$, but slightly by $Ag^+$ 5. This enzyme was not inhibited by cystein, thiourea, ${\varepsilon}-aminocaproic$ acid, 2, 4-DNP, EDTA but strongly inhibited by PCMB.

• Journal of Ginseng Research
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• v.14 no.1
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• pp.21-26
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• 1990

The chemical composition and stabilities of the purified ginseng invertase were investigated. The purified enzyme was found to be a glycoprotein composed of 80.2% protein and 19.7% total sugar. The protein component of the enzyme was composed of acidic amino acid (9.3%), basic amino acid (48.9%), nonpolar amino acid (21.4%), polar amino acid (20.4%) and 6.1% S-containing amino acid. It showed especially high contents of histidine and serine. The enzyme was inactivated almost completely by the treatment with some proteases (papain, pepsin. trypsin, pancreatin and microbial alkaline pretense) and protein denatllrants (8M urea and 6M guanidine-HC1), bolt not with glyrosidase (${\alpha}$-amylase, ${\beta}$-amylase. glcoamylese and cellullase). btonosaccharides sllch as glilrose, fructose, galactose and mannose did not exert any influence on the enzyme activity. The activity of the enzyme was inhibited by Ag+, Mn2+, Hg2+, Zn2+ and Al3+, whereas Ca2+, Mg2+, Ba2+ and Fe3+ gave rather activating effects on the enzyme activity. The enzyme was relatively stable in the VH range of VH 6 and 8, and at the temperatures below 35$^{\circ}C$.

• The Korean Journal of Food And Nutrition
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• v.7 no.2
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• pp.87-94
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• 1994

A protease, actinidin, was isolated from Cheju kiwi fruit Actinidia chinesis. The enzyme was purified about 8.5 fold with the yield of 25% by column chromatographies of DEAE-Toyopearl and Sphadex. G-100. Purified enzyme gave a single protein band on polyacrylamide gel electrophoresis and its molecular weight estimated by SDS-PAGE was about 27, 000. The optimum pH and temperature were 7.0 and 4$0^{\circ}C$, respectively. This enzyme was stable at the ranges of pH 5.0~9.0 and below 5$0^{\circ}C$. It was also found that Fe+2, Fe+3, and Na+ ions increased enzyme activity, whereas Hg+2 and Co+2 ions decreased. The enzyme was inhibited by phenylmercuric acetate and leupeptin, which indicated that active center of the emzyme had thiol-group. The enzyme reaction followed the Michaelis-Men-ten dkinetics with the Km value of 0.32 mM for casein.

• Korean Journal of Food Science and Technology
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• v.36 no.3
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• pp.448-455
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• 2004

Changes in quality characteristics of Bijijang (fermented soybean curd residus) prepared at $35^{\circ}C\;and\;40^{\circ}C$ for 0, 12, 24, 36, and 48 hr were investigated. Acidity of Bijijang increased, whereas pH and Hunter's color values decreased during fermentation. Immediately after Bijijang preparation, ${\alpha}-and\;{\beta}-amylase$ activities were very low, ${\beta}-Amylase$ activity during fermentation increased rapidly, with those fermented at $40^{\circ}C$ higher than at $35^{\circ}C$. Neutral pretense activity was significantly higher than acidic pretense activity, and increased gradually after 12 hr. Change in total nitrogen content in Bijijang was insignificant, whereas contents of amino-type and water-soluble nitrogens increased significantly during fermentation. Major free amino acids of Bijijang were Arg, Pro, Glu, Thr, Ser, and Lys at initial fermenting stage, and, as fermentation progressed, contents of Cys, Met Glu, Ile, Leu, and Phe increased. Reducing sugar contents of Bijijang fermented at $40^{\circ}C$ were higher than those fermented at $35^{\circ}C$. Sucrose content decreased and glucose content increased. Glucoside (genistin and daidzin) contents decreased and aglycone (genistein and daidzein) contents increased during preparation of Biji and fermentation of Bijijang. Contents of free sugars and isoflavones were higher in Bijijang fermented at $40^{\circ}C$ than at $35^{\circ}C$. Based on these results, fermentation at $40^{\circ}C$ for 48 hr was determined to be optimum fermentation condition for Bijijang.

• Microbiology and Biotechnology Letters
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• v.17 no.4
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• pp.358-364
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• 1989

A crystalline alkaline pretense- producing Streptomyce sp. YSA-130 was isolated from soil in alkaline medium(pH 10.5). The optimum culture condition of Streptomyce sp. YSA-130 for the production of alkaline protease was as follows; 2.0% soluble starch, 1.0% soytone, 0.3% $K_2$HPO$_4$, 0.02% MgSO$_4$.7$H_2O$, 0.8% Na$_2$CO$_3$, pH 10.5, 3$0^{\circ}C$, and 12 hr. The alkaline pretense from the culture broth of Streptomyce sp. YSA-130 was purified about 24 folds by ammonium sulfate precipitation , dialysis, DEAE-cellulose ion exchange chromatography, gel filtration on Sephadex G-15 and crystallization. Optimum temperature and pH of purified enzyme were 6$0^{\circ}C$, and 11.5. Temperature and pH stability of purified enzyme were 5$0^{\circ}C$, and 5.5-12.0. Calcium ion was effective to stabilize the enzyme at higher temperature. The molecular weight of the purified enzyme was approximately 30,000. The purified enzyme was inactivated by diisopropyl flurophosphate(DFP) but not affected by metal ion, EDTA, sulfhydryl reagent and stable detergent.

• Journal of the Korean Society of Food Science and Nutrition
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• v.33 no.2
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• pp.229-235
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• 2004

Soy protein was hydrolyzed by 5 different pretenses and determinated antimicrobial activity of each hydrolysate. The soy protein hydrolysate treated by pretense from Aspergillus saitoi showed the highest antimicrobial activity among the protease studied and was used for further analysis. Soy protein hydrolysate was fractionated by ultrafiltration for M.W. 10,000,3,000 and 1,000. The M.W 1,000∼3,000 showed the highest antimicrobial activity. The minimum inhibition concentrations of obtained fraction were 0.5∼0.8 mg/mL for gram positive and negative microbials, and its activity was even observed after heating at 121$^{\circ}C$ for 10 min, suggesting that hydrolyzed protein having antimicrobial activity is quite heat-stable. Reverse-phase HPLC was further applied to separate the fraction and 8 peaks were found. Each 8 peaks were separated and pooled and measured antimicrobial activity. Among them, retention time of peak at 16.02 min showed the prominent antimicrobial activity.

• Korean Journal of Food Science and Technology
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• v.36 no.1
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• pp.105-110
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• 2004

Microorganism (strain DF 218) producing thermostable pretense was isolated from Korean soil and compost. It was Gram-positive, rod-shaped, aerobic, and spore-forming with yellowish white colony color, Temperature range for growth at pH 6.5 was $30-65^{\circ}C$, with optimum growth at $60^{\circ}C$. pH range for growth at $60^{\circ}C$ was 5-7 with optimum of 6.5, which indicates strain DF 218 to be thermophilic. The 16S rDNA sequence of strain DF 218 had 95% sequence similarity with that of Bacillus flexus. Based on physiological properties and phylogenetic analysis, we proposed the isolated strain as Bacillus sp. DF 218. Pretense was produced aerobically at $60^{\circ}C$ for 32 hr in a medium (pH 6.5) containing 1% each trypton, glucose, and NaCl. Its molecular weight was estimated as 61 kDa, with optimum temperature and pH of $60^{\circ}C$ and 7.5, respectively.

• Korean journal of food and cookery science
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• v.11 no.1
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• pp.26-32
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• 1995

This study was carried out to investigate the effect of protease on the functionality of soymilk protein. The protease from Bacillus polymyxa was selected because of the least production of bitter taste and calcium-aggregation. The results are summarized as follows: 1. Solubility of SMP(soymilk protein) and SPI(soyprotein isolate) were lowest at pH 4.7 and increased as the pH value reached closer to either ends. PT-SMP(pretense treated soymilk protein) showed higher solubility at all pH range, especially at pH 4.7 than SMP, SPI. 2. Emulsion activity of three samples was lowest at pH 4.7 and significantly increased as pH approched higher acidic or alkaline regions. PT-SMP showed similar activity to other samples, but less stability. 3. Foam capacity of PT-SMP was lowest at pH 8 and increased in acidic, alkaline pH. PT-SMP showed higher foam capacity at all pH range, but lower foam stability than SMP and SPI. 4. PT-SMP showed higher heat coagulability than other samples at all pH range except pH 4.7.

• The Korean Journal of Food And Nutrition
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• v.15 no.2
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• pp.131-136
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• 2002

Protease activity in matured wax gourd sarcocarp was 0.19unit/0.5ml, immatured wax gourd sarcocarp 0.56unit, and matured wax gourd 24.35 unit, immatured wax gourd core 0.35unit. Protease activity in matured wax gourd sarcocarp to raw meat or raw pork was 13,0 unit, 7.4 unit, respectively, and that in wax gourd core to raw beef was 30.2 unit, and raw pork was 24.5 unit. Thermal stability of pretense in matured wax gourd sarcocarp was stable below 70$\^{C}$ when it was heated for 10 minutes. In case of 80$\^{C}$, the remaining activity was 21%, and at 90$\^{C}$, it was lost entirely. The absorption spectrum showed peak at 280nm. According to the HPLC analysis, casein was hydrolyzed into small size by protease in core or sarcocarp of matured was gourd and immatured wax gourd. Wax gourd diluted by 1/10 showed two peaks, one was from casein being hydrolyzed, and the other was from the increased molecular weight with coagulated casein. On the other hand, the molecular weight didin't increase in immatured wax gourd core diluted by 1/10. The result of dilution of 1/10 showed different pattern from undiluted one, but the peak of sarcocarp in matured wax gourd was 1 and the peak of core in immatured wax gourd was 5, and those of core and sarcocarp of immatured wax gourd were 3 respectively.