• Journal of the Korean Society of Food Culture
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• v.14 no.5
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• pp.477-485
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• 1999

This study was conducted to improve the functional properties of soybean protein isolate by dimethylglutarylation and acetylation. Amino acid composition and solubility of modified soybean protein by dimethylglutarylation were not changed, but lysine and trypsin inhibitor activity was decreased an isoelectric point was moved from pH5 to pH4 as a result of modification. Emulsification capacity and stability, foaming capacity and thermal stability were increased by the modification. In that 91% dimethylglutarylated protein did not coagulate when heating at $100^{\circ}C$ for 20 min. while its foaming stability was decreased. Whereas specific gravity was decreased by the modification of the soybean protein, relative viscosity and whiteness were improved. Generally, dimethylglutarylation produced more conformational changes in protein system than did in acetylation.

• Korean Journal of Microbiology
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• v.29 no.3
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• pp.167-171
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• 1991

An intracellular protease from cells of Pseudomonas carboxydohydrogena grown on nutrient broth was purified to better than 95% homogeneity in five steps using azocaseine as a substrate. The molecular weight of the native enzyme was determined to be 125, 000. Sodium dodecyl sulfate-gel electrophoresis revealedat least two non-identical subunits of molecular weight 70, 000 and 56, 000. The enzyme activity was completely ingibited by phenylmethylsulfonyl fluoride and diisopropyl fluorophosphate. The enzyme was also inhibited by $Mg^{2+}$ , $Zn^{2+}$ , $Cd^{2+}$, $Cu^{2+}$ , and $Fe^{2+}$ , but was stimulated by iodoacetamide. Maximal reaction rate of the enzyme was observed at pH8.0 and 30.deg.C. The isoelectric point of the enzyme was found to be 7.5. The enzyme was unable to hydrolyze carbon monoxide dehydrogenase.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.34 no.3
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• pp.270-273
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• 1989

This study was carried out to know the physiological characteristics related to flooding tolerance of rice plants. Peroxidase specific activities and banding pattern of peroxidase isozyme of 24 days old seedlings were analyzed after 3 days of flooding treatment in the artificial flooding tank. Peroxidase activities of japonica rice varieties which were relatively susceptible to submergence were higher in comparison to those of Tongil and indica rice varieties. And a peculier band of peroxidase isozyme which was not shown in any part of rice plant if not flooded, was appeared at the around 9 of isoelectric point in the leaf blade of japonica rice varieties when flooded.

• Journal of Biomedical Engineering Research
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• v.6 no.2
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• pp.53-62
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• 1985

The position and time interval of wave components of the electrocardiogram are used as important data for physician's diagnosis. In case of using the existing definition of the onset of the wave component of the electrocardiogram, they have some problems of defining the precise position of the isoelectric line, of defining the limit of the gradient accepted as the onset, and of the gradient being changed by noise. Therefore, in this paper all time intervals and positions of wave components needed for data of diagnosis were obtained correctly by turning point data reduction algorithm and linear regression intersection algorithm, and the viability of the method of intersecting lines was established in comparison to the four methods of calculating the PR interval.

• The Korean Journal of Zoology
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• v.35 no.4
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• pp.466-473
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• 1992

Storage protein-1 (SP-1) of Gallerio mellonella was identified in hemolvmph and fat body by electrophoresis. SP-1 was purified from hemolvmph by KBr density gradient ultracentrifugation , DEAE-cellulose (DE52) ion-exchange chromatography, and gel permeation chromatography (Sephadex G-200). Purity of SP-1 was confirmed by Non-SDS PAGE and electron microscope. SP-1 is 9.4 nm in diameter and regular octahedron in shape. SP-1 has isoelectric point of 5.7 and native molecular weight of 365 K dalton and is composed of one type of subunit with molecular weight of 82 K dalton. Ttiacylslvcerol and phospholipid were found to be maior lipid components in SP-1.

• The Korean Journal of Zoology
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• v.37 no.4
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• pp.495-503
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• 1994

Hemolymph SHBP (hJHBP) was partially purified from last instar larvae of Bombyx zori by gel filtration and their optimal reaction conditions of dextrin coated charcoal binding assay were determined. Dissociation constant (KD) of hJHBP for JH III was calculated to be 1.45 $\times$ 10-7 M at $4^{\circ}C.$ The molecular weight of hJHBP was estimated to be 30 kDa by gel filtration on a calibrated Sephadex G-100 column and 33 kDa by SDS-PAGE. These results indicate that hSHBP consists of a single polvpeptide chain. Isoelectric point of hJHBP was found to be pH 5.1 and 19 of the first 20 amino acid residues were determined from N-terminus of purified hJHBP.

• Proceedings of the Membrane Society of Korea Conference
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• 1994.10a
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• pp.72-73
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• 1994

Whey는 일명 lactoserum 이라고도 하며 치즈제조시 우유를 응고시키는 과정에서 Casein과 지방으로부터 분리되어 나오는 액상의 부산물로 본래 우유 부피의 약 90%를 차지하며, 용해성 단백질, 유당, 비타민과 무기질 등을 함유하고 있다. 유청에 함유되어 있는 단백질은 건조고형분의 약 13%가 되는데, 주요 단백질은 $\beta$-lactoglobulin(50%), $\alpha$-lactalbumin(22%), Serum albumin(5%), Immunoglobulin(12%), Proteose-peptone(10%) 등이 있다. 유청단백질중 가장 많이 함유되어 있는 $\beta$-lactoglobulin은 구형의 단백질로 단량체의 분자량은 약 18,400이며, pH 3.5~7 범위내에서는 해리되지 않는 이량체(dimer)를 형성한다. pH 3.5 이하에서 이량체는 해리되고 다량체의 형성으로 재평성한다. pH 7.0 이상의 알칼리 영역에서는 Conformational Change가 일어나는 것으로 알려져 있으며, 등전점(isoelectric point)은 pH 5.2이다. $\alpha$-lactalbumin은 14,200의 분자량을 가지는 구형의 단백질로 등전점은 pH 4.8이다.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.27 no.5
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• pp.673-674
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• 1994

• Journal of the Korean Society of Food Science and Nutrition
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• v.20 no.6
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• pp.621-628
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• 1991

Heat-stable enterotoxin(ST) from enterotoxigenic E. coli eKT-53($ST^{+}\;LT^{-}$, transformant from isolate KM-7) that was produced in succinate salts medium. The culture supernatant(crude ST) was purifed by mulitpled steps and investigated some characterization of the ST. The heatstability of purified ST activity was completely lost by treating at $100^{\circ}C$ for 30minutes. ST activity was lost by treatment at pH 1 and 12 conditions, while the activity was not reduced by treatment at pH 2~10, and then the ${\alpha}-amylase$ and pepsin was not decreased activity but disulfide reducing agnets was lost the activity. The molecular weight of the purified ST was approximately 4,200, the isoelectric point was about 4.0.

• Journal of the East Asian Society of Dietary Life
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• v.10 no.5
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• pp.394-403
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• 2000

The functional properties of sesame protein concentrate(SPC) using different size of ultrafiltration(UF) membranes were examined and compared with those of conventional acid-precipitated sesame protein concentrate. The protein contents of SPC by UF with molecular size of 10K, 30K and look dalton membranes were 84.2%, 82.7%, and 76.4%, respectively, and that of acid-precipitated SPC was 88.7%. The nitrogen solubility of SPC by UF was higher than that of conventional SPC at various pH levels. Especially, it showed three-fold increase at near isoelectric point. However, water absorption capacity and fat absorption capacity of SPC by UF were decreased. For emulsion and foam properties, there were no significant differences between SPC by acid precipitation and SPC by UF method. At various pH levels, SPC by membrane with pore size of 30K dalton showed the highest emulsion properties. The SPC by UF had slightly higher viscosity than defatted sesame flour and SPC by acid precipitation.