• Korean Journal of Food Science and Technology
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• v.37 no.3
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• pp.389-396
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• 2005

Physico-chemical properties of ssamjang prepared by industrial process were investigated. Overall experiments were planned by central composite design for five independent variables, kochujang mash aging period $(X_{1})$, doenjang aging period $(X_{2})$, doenjang content $(X_{3})$, sterilization temperature $(X_{4})$, and storage temperature $(X_{5})$. Storage period had no consistent effect on moisture content of ssamjang. Doenjang having longer aging period showed lower moisture content than that having shorter aging period. Titratable acidity and pH of ssamjang gradually increased and decreased with storage period, respectively, with pH of ssamjang significantly affected by aging period of doenjang and kochujang mashes, and sterilization and storage temperatures. Amino nitrogen contents of ssamjang increased during storage and were more affected by sterilization temperature than by aging period and content of doenjang, and storage temperature. Crude protein content of ssamjang irregularly changed during storage, and was slightly affected by content of doenjang.

• Microbiology and Biotechnology Letters
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• v.26 no.4
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• pp.290-296
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• 1998

Interspecific hybrids between Aspergillus oryzae var. oryzae and Penicillium chrysogenum (Tyr$\^$-/), high alkaline protease producing fungi, were obtained by nuclear transfer technique. Nuclei isolated from the wild type Aspergillus oryzae var. oryzae strain were transferred into auxotrophic Penicillium chrysogenum mutants and selected the new strains showing an increased protein degrading capability. Maximum production of protoplasts were obtained by 1% Novozym 234 at $30^{\circ}C$ for 3 hours and the most effective osmotic stabilizers for the isolation of protoplasts were 0.6M KCl. Frequencies of hybrid formation by nuclear transfer were 1.3${\times}$10$\^$-3/∼2.8${\times}$10$\^$-3/. They could be suggested as an aneuploid by the observation of genetic stability, conidial size, DNA content, and nuclear strain. The hybrids showed 1.1～2.2 fold higher alkaline pretense activities than parental strains.

• Parasites, Hosts and Diseases
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• v.44 no.4 s.140
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• pp.321-330
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• 2006

The pathogenic mechanism of granulomatous amebic encephalitis (GAE) and amebic keratitis (AK) by Acanthamoeba has yet to be clarified. Pretense has been recognized to play an important role in the pathogenesis of GAE and AK. In the present study, we have compared specific activity and cytopathic effects (CPE) of purified 33 kDa serine proteinases from Acanthamoeba strains with different degree of virulence (A. healyi OC-3A, A. lugdunensis KA/E2, and A. castelianii Neff). Trophozoites of the 3 strains revealed different degrees of CPE on human corneal epithelial (HCE) cells. The effect was remarkably reduced by adding phenylmethylsulfonylfluoride (PMSF), a serine proteinase inhibitor. This result indicated that PMSF-susceptible proteinase is the main component causing cytopathy to HCE cells by Acanthamoeba. The purified 33 kDa serine proteinase showed strong activity toward HCE cells and extracellular matrix proteins. The purified proteinase from OC-3A, the most virulent strain, demonstrated the highest enzyme activity compared to KA/E2, an ocular isolate, and Neff, a soil isolate. Polyclonal antibodies against the purified 33 kDa serine proteinase inhibit almost completely the proteolytic activity of culture supernatant of Acanthamoeba. In line with these results, the 33 kDa serine proteinase is suggested to play an important role in pathogenesis and to be the main component of virulence factor of Acanthamoeba.

• Microbiology and Biotechnology Letters
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• v.2 no.1
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• pp.13-17
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• 1974

A strain of Streptomyces sp. which producing a metal containing proteolytic enzyme was isolated from soil and some properties of this enzyme were investigated. The following results were obtained. 1. Optimal pH and temperature of this enzyme were pH7.0 and 37$^{\circ}C$ 2. This enzyme was easily inactivated with heat treatment: for example, by the treatmentat 37$^{\circ}C$ for 100 minutes the activity of the enzyme was decreased to about 50 per cent of intial actively but this enzyme was stable at neutral pH. 3. The activity of this enzyme was not inhibited by $Mg^{＋＋}$, $_Mn^{＋＋}$, $Ca^{＋＋}$, Pb$^{＋＋}$, or $Ba^{＋＋}$ ect. but strongly inhibited by Hg$^{＋＋}$, Co$^{＋＋}$, Ag$^{＋}$, Cu$^{＋＋}$, or Cd$^{＋＋}$. 4. This enzyme was strongly inhibited by EDTA but was not inhibited by oxalic acid, citric acid, 2, 4-dinitrophenol, $\varepsilon$-aminocaproic acid, cysteine, or thiourea.

• Korean journal of food and cookery science
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• v.9 no.4
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• pp.278-283
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• 1993

This study was attempted to investigate the effects of enzymatic modification of milk protein with protease on functional properties. The selected functional properties were solubility, emulsifying activity (EA), emulsion stability(ES), foam expansion(FE), and foam stability(FS). These properties were measu-red from pH 3.0 to pH 8.0. The proteases used in this study were iaolated from Meju(fermemted soybean) and had specific activity of 250 units/㎎ protein at pH 7.0, 1600 units of pretense was used for 1gr. of skim milk protein. Skim milk showed 30.5％ degree of hydrolysis for 1 hr. and 36.4% degree of hydrolysis for 3.5 hrs. of protease treatment at pH 7.0. Solubility of native skim milk, control, 1 hr. and 3.5 hrs. groups were 3.37, 3.64, 10.21, 14.34％o at pH 4.0 respcetively. The emulsifying activity of native skim milk, control, 1 hr. and 3.5 hrs. groups were 38.8,42.0,43.0,46.7ft at pH 4.0, respectively. Enzymatic modification resulted in the increase of solubility and emulsifying activity at pH 4.0. However at pH 5.0 emulsifying activity of 1 hr. and 3.5 hr. group were lower than native skim milk and control groups. 1 hr. protease treatment was found to be most effective way of increasing foam expansion at pH 4.0 to 6.0. It was supported that, protease treated skim milk can be used to improve solubility, emulsifying activity, foam expansion at acid pH. meju protease. skim milk, solubility, emulsion, foam.

• Journal of the Korean Society of Clothing and Textiles
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• v.20 no.4
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• pp.655-666
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• 1996

The effect of protease (subtilisin Carlsberg) on the removal of hemoglobin as protein soil was studied. The relation between the renloval and the hydrolysis of hemoglobin by subtilisin Carlsberg was discussed. The soiled babric was prepared by spotting of hemoglobin solution evenly on the cotton fabric and was denatured by steaming. The soiled fabric was washed by using Terg-0-Tometer at various conditions. The removal efficiency was evaluated by analysis of protein on the fabrics before and after washing by means of copper-Folin method. 1. The removal of hemoglobin was increased in proportion to increasing of the enzyme concentration up to a certain point, but it began to decrease above the point. 2. The hemoglobin was removed effectively by adding of subtilisin Carlsberg, and more effectively removed by adding of AOS in the enzyme solution. 3. The removal of hemoglobin deviated from the first order reaction in detergency. 4. The renloval of hemoglobin was highest at $50^{\circ}C$ in detergency, Even at low temperature the removal efficiency of enzyme was relatively higher compared with the hydrolysis of hemoglobin by the enzyme. However the removal of hemoglobin was apparently decreased with the increase of temperature over $60^{\circ}C$. 5. The removal of hemoglobin was relatively high at pH 7.0~8.0 and increased continuously with the increase of pH in detergency 6. In detergency, the removal mechanism of hemoglobin by subtilisin Carlsberg could be explained as follows: Fisrt of all, the enzyme hydrolyzed hemoglobin substrates partially by forming E-S complex at the surface of hemoglobin on the cotton fiber, and decomposed cooperative binding of hemoglobin. Subsequently, the fragments of hemoglobin were easily removed by washing. According as the enzyme penetrated to inner part of hemoglobin gradually, the hemoglobin on the cotton fiber was effectively removed by the repetition of these process. The removal of hemoglobin was more effectively increased by adding both the enzyme and AOS in the washing solution. Therefore, it was regarded that AOS molecules were adsorbed at the hydrophobic surface of denatured hemoglobin, subsequently, decomposed more effectively cooperative binding of hemoglobin, and the fragments of hemoglobin were removed more efficiently by means of the interfacial reaction of AOS.

• Microbiology and Biotechnology Letters
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• v.31 no.3
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• pp.224-229
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• 2003

A keratinolytic protease was purified from the culture medium of Pseudomonas sp. KP-364 by use of an assay of the hydrolysis of feather keratin. Membrane ultrafiltration and DEAE-cellulose ion-exchange resin and Sephadex G-150 gel chromatographies were used to purify the enzyme. The specific activity of the purified keratinolytic protease relative to that in the original medium was approximately 72-fold high. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Sephadex G-150 chromatography indicated that the purified keratinolytic protease is monomeric and has a molecular weight of 36 kDa. The optimal pH and temperature of the keratinolytic protease activity were 6.6 and 37 C, respectively, and the keratinolytic protease was relatively stable at pH value from 3.0 to 10.0 at 37 C for 1hour. The keratinolytic protease was inhibited by EDTA and EGTA, indicating that the keratinolytic protease was a kind of metalloprotease that require Li+ for cofactor.

• Korean Journal of Food Science and Technology
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• v.36 no.1
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• pp.147-151
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• 2004

Antigenicities of ovomucoid (OM) and ovalbumin (OA) in chicken egg white (EW) before and after NaOH, heat, and pretense treatments were examined by competitive indirect enzyme-linked immunosorbent assay (ciELISA), using rabbit anti-OM and-OA antibodies, Enzymatic hydrolysis of EW did not effectively reduce antigenicity of OM, whereas that of OA was decreased to 1/5,000-1/100,000 by treatment of plant-derived or microbial pretenses. Heat treatment below $100^{\circ}C$ for 30min did not decrease antigenicity of OM, whereas that of OA in heated EW increased maximally to 100 times, Antigenicity of OM in EW effectively decreased by NaOH treatment, disappearing at over 1% NaOH, whereas that of OA increased. Additional heat treatment of NaOH-treated EW at $70^{\circ}C$ for 15min slightly reduced antigenicities of OM and OA.

• Korean Journal of Food Science and Technology
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• v.22 no.2
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• pp.172-176
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• 1990

Electrocondensation method using aluminum electrodes was developed to remove excess amount of fluoride contained in Antarctic krill. Fluoride amount was reduced differently according to fluoride forms (total, ionic and bound) and sections (whole, muscle flesh and chitinous) of the Antarctic krill during electrocondensation process. Total, ionic and bound fluoride could be reduced by 56%, 35% and 60% of the initial amount contained in the whole body, respectively and reduced by 49%, 57% and 34% of the initial amount in the muscle flesh, respectively by electro condensation process for 120 min. In the case of chitinous section of the Antarctic krill, 68% of total fluoride could be decreased by this process for 120 min.

• Microbiology and Biotechnology Letters
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• v.11 no.1
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• pp.67-74
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• 1983

The studies on the color improvement of the Doenjang (two types of fermented soybean paste : soybean Doenjang and modified Doenjang) using various Aspergillus oryzae strains (6 strains : A, B, C, D, E, F) were conducted with the series of experiments of enzymatic activities (pretense, $\alpha$-and $\beta$-amylase), browning color formation (Lovibond color), major chemical components (amino nitrogen, reducing sugar and others) and sensory evaluation (color, taste and odor). Aspergillus oryzae 2157 (C strain) had a high potential for the color improvement of Doenjang products and was identified as non-browning strain during Doenjang fermentation and storage period. And also this strain was appeared to be in good enzyme activities and flavor characteristics.