• Title/Summary/Keyword: Isoelectric Point

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Yielding behaviour of organically treated anatase $TiO_2$ suspension

  • Guo, J.;Tiu, C.;Uhlherr, P.H.T.;Fang, T.N.
    • Korea-Australia Rheology Journal
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    • v.15 no.1
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    • pp.9-17
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    • 2003
  • The rheological behaviour of anatase $TiO_2$ with organic coating has been investigated extensively in this study. The yield stress was measured over a wide range of solids concentration and pH using stress-controlled and speed-controlled rheometers. The organic treatment leads to a shift of the isoelectric point (IEP) from around pH 5.5 to pH 2.4. A maximum yield stress occurs in the vicinity of the isoelectric point determined by electrokinetic measurements. The transition of rheological behaviour between elastic solid and viscous liquid is represented by a stress plateau in a plot of stress against strain. It is hypothesised that the slope of the stress plateau reflects the uniformity of the structure, and hence the distribution of bond strength. Altering the concentration and the surface chemistry can vary the bond strength and its distribution. therefore, resulting in different type of failure: "ductile-type" or "brittle-type". pH and volume fraction dependence of yield stress could be described quantitatively using existing models with reasonable agreement.easonable agreement.

Foaming Capacity and Foaming Stability of Protein Recovered from Red Crab Processing Water (홍게 가공회수 단백질의 거품 형성력 및 안정성)

  • Kim, Yong-Jin;Sin, Tae-Seon;O, Hun-Il
    • The Korean Journal of Food And Nutrition
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    • v.9 no.3
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    • pp.325-330
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    • 1996
  • Foaming capacity (FC) and stability (FS) of protein recovered from red crab (Chitinonecetes opilio) processing in water and soybean protein isolate were determined at pH 2.0~10.0 in water and NaCl solution. The FC values for both proteins showed the lowest values at the isoelectric point (pH 4.0) and increased nth an increase in pH above the isoelectric point. FC of RCP was higher than that of SPI at pH 10.0 in water and both NaCl solutions. FC of SPI increased with an increase in NaCl concentration at pH 4.0 and 6.0, but FC of RCP was not affected. The highest FS values for both proteins were obtained at pH 4.0 in water. At pH 2.0, FC of RCP decreased with NaCl concentration increase, but FS increased. NaCl concentration had little effect on FS of RCP at pH 4.0 and 6.0, but the FS decreased at pH 10.0. FS of SPI was similar to that of RCP at pH 2.0 and increased with NaCl concentration Increase from 0.1 to 0.5M NaCl at pH 10.0.

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Purification and Characterization of Cop, a Protein Involved in the Copy Number Control of Plasmid pE194

  • Kwak, Jin-Hwan;Kim, Jung-Ho;Kim, Mu-Yong;Choi, Eung-Chil
    • Archives of Pharmacal Research
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    • v.21 no.3
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    • pp.291-297
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    • 1998
  • Cop protein has been overexpressed in Escherichia coli using a T7 RNA polymerase system. Purification to apparent homogeneity was achieved by the sequential chromatography on ion exchange, affinity chromatography, and reverse phase high performance liquid chromatography system. The molecular weight of the purified Cop was estimated as 6.1 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). But the molecular mass of the native state Cop was shown to be 19 kDa by an analytical high performance size exclusion chromatography, suggesting a trimer-like structure in 50 mM Tris-HCI buffer (pH 7.5) containing 100 mM NaCl. Cop protein Was calculated to contain $39.1% {\alpha}-helix, 16.8% {\beta}-sheet$, 17.4% turn, and 26.8% random structure. The DNA binding property of Cop protein expressed in E. coli Was preserved during the expression and purification process. The isoelectric point of Cop was determined to be 9.0. The results of amino acid composition analysis and N-terminal amino acid sequencing of Cop showed that it has the same amino acid composition and N-terminal amino acid sequence as those deduced from its DNA sequence analysis, except for the partial removal of N-terminal methionine residue by methionyl-aminopeptidase in E. coli.

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Studies on Xanthine Oxidase from Bovine Thyroid Glands -[Part 2] Composition and Some Properties- (소의 갑상선에 있는 크산친 옥시다아제에 관한연구 [제2보] 효소의 조성과 특성-)

  • Lee, Hyo-Sa
    • Applied Biological Chemistry
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    • v.21 no.3
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    • pp.137-143
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    • 1978
  • Xanthine oxidase from bovine thyroid glands was found to contain FAD, molybdenum and iron in a ratio 1:0. 36:1. 6. The molecular weight of the thyroid enzyme was similar to that of the milk enzyme when estimated by gel filtration and polyacrylamide gel electrophoresis. The optimum pH for the enzyme activity was 7.8. The pH of the isoelectric point was determined to be 6.2 by electrofocusing. Sodium dodecyl sulfatepolyacrylamide gel electrophoresis experiment indicated that the enzyme was dissociated into subunits and that the molecular weight for the smallest subunit was 65,000 daltons. Absorption spectra were dissimilar between milk and thyroid xanthine oxidase.

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Characteristics of protease inhibitor produced by streptomyces fradiae SMF9

  • Kim, Hyoung-Tae;Suh, Joo-Won;Lee, Key-Joon
    • Journal of Microbiology
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    • v.33 no.2
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    • pp.103-108
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    • 1995
  • Streptomyces fradiae protease inhibitor (SFI) was purified effectively by preparative isoelectric focusing and hydroxyapatite chromatography. The molecular weight of SFI was estimated to be 1.7 kDa by SDS-PAGE and 1.8 kDa by molecular sieving HPLC. One hundred and sixty amino acid residues were determined from which molecular weight of SFI was calculated to be 17.054 Da and carbohydrate residue was not detected. SFI was calculated to be 17,064 Da and carbohydrate residue was not detected. SFI was a monomeric protein with two reactive sits, of which isoelectric point was pH 4.1. N-terminal amino acid sequence of SFI had homology with SSI (Streptomyces subsilisin inhibitor) and other protease inhibitors produced by Streptomyces.

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Study on the Pattern of Isoenzymes in Pancreatic Juice, Serum and Saliva of Rabbit (정상 및 병적체액중 동종효소분획에 관한 연구)

  • Kim, Won-Joon;Kim, Hea-Young;Lee, Hyang-Woo;Hong, Sa-Suk
    • The Korean Journal of Pharmacology
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    • v.16 no.2 s.27
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    • pp.15-24
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    • 1980
  • [${\alpha}$]-Amylase catalyses the hydrolysis of starch, glycogen, and related poly- and oligosac-charide by random cleavage of ${\alpha}$-D-(l-4) glucan linkage. In man large amounts of amylase are secreted into the digestive tract by the salivary and exocrine pancreatic gland, minimal amount being produced also in other tissues. It has been known that ${\alpha}$-amylase exists in multiple molecular forms, isoenzyme which can be separated from each other because of difference in their physicochemical properties. By using various methods, several groups of investigator have separated the many isoenzyme in serum, saliva and pancreatic juice. Furthermore, changes of the normal serum isoenzyme pattern is diagnostically useful even when the total serum enzyme activity is noninformative, such as the clinical use of isoenzyme of serum lactate dehydrogenase. Procarboxypeptidase-A which is one of the pancreatic enzymes is also present as isoenzymes. Four forms of procarboxypeptidase-A haye been found in the bovine enzyme and three forms of the porcine enzyme. In human pancreatic juice four forms of procarboxypeptidase-A isoenzyme were found by isoelectric focusing method. Recently, the so-called isoamylase analysis was developed for the diagnostic use of amylase in pancreatic diseases. In alcohotic patients, the serum concentration of pancreatic isoamylase is subnormal and this lowered activity provides strong evidence for pancreatic exocrine insufficiency. The purpose of this study was to elucidate the variations of the isoenzyme of amylase and procarboxypeptidase-A in serum, saliva and pancreatic juice of the experimental animals. The results are as follow. 1) Three main forms of isoenzyme of amylase by isoelectric focusing were found in pancreatic juice of normal rabbit. However, many new bands were appeared in the pancreatic juice of cholic acid administered animal intravenously while the infusion of cholic acid or elastase into pancreatic duct produced the decrease of number of the fractions on the isoelectric focusing. In the case of serum isoenzyme from normal animal, two major and a few minor isoamylases were observed. By injecting alcohol intravenousely the fractions of serum isoamylase were significantly decreased and in contrary to the pattern in the pancreatic juice the infusion of cholic acid or elastase into pancreatic duct exhitited a significant decrease of the isoenzyme of amylase fractions. In saliva from normal animal three main isoamylase were produced of the administration of alcohol. 2) In the case of procarboxypeptidase-A isoenzyme, two major fractions which have isoelectric point at 6.2 and 6.4 and other two minor bands were observed in the pancreatic juice of normal rabbit. By the treatment of the juice with trypsin, only one band was produced on the isoelectric focusing. No procarboxypeptidase was appeared on the electrofocusing by the infusion of cholic acid or phospholipase A into the pancreatic duct of rabbit. However, a single major fraction of procarboxypeptidase-A was appeared at 3 hr after simple ligation of the pancreatic duct. No significant changes were observed in the juice of the alcohol or cholic acid administered group.

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Recovery and Utilization of Proteins and Lipids from Washing Wastewater in Marine Manufacture by Isoelectric Point Precipitation Method 1. The Coagulation Treatment for Washing Wastewatfr of Minced Mackerel Meat (수산가공공장 폐액의 등전점 침전처리에 의한 유용성분 재회수 이용 1. 고등어 육 고기풀 제조시 발생되는 폐액의 처리장치 개발)

  • 서재수;조순영
    • KSBB Journal
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    • v.10 no.1
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    • pp.1-8
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    • 1995
  • A lot of water soluble proteins and lipids are released from minced mackerel meat and lost into the washing waste during the leaching process of Kamaboko or surimi manufacture. The removed proteins and lipids are not only an edible things but also a big burden for treating the wastewater. In order to recover the proteins from the effluent and to use as food stuff, the "pH-shifting" treatment, a modified isoelectric point precipitation method, was tried. This method is based on a myogen-aggregation phenomenon, which occurs when a solution of sarcoplasmic proteins is acidified or alkalified beyond the critical pH zone of 2∼3 or 12∼13 respectively and then neutralized. The maximum amount of precipitation was obtained by shifting the pH of the wastewater from original pH to isoelectric point (pH 4) or alkali pH 12 and then changing to neutral pH. The precipitates were easily collected by filteration or centrifuging at 10,000rpm. The oils which were only floating in the washing wastewater are easily recovered by seperating with oil separator after pouring. The recovered proteins were slightly denaturated during this pH shifting precipitation process, while the composition of amino acids was good balance as a food.

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Study on Softness of an EO Adducted Amine Oxide Zwitterionic Surfactant (EO가 부가된 아민 옥사이드 양쪽성 계면활성제의 유연력에 관한 연구)

  • Kim, JiSung;Mo, DaHee;Lee, JinSun;Park, JunSeok;Han, DongSung;Lim, JongChoo
    • Korean Chemical Engineering Research
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    • v.50 no.6
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    • pp.960-968
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    • 2012
  • In this study, the measurement of physical properties of 3 different ethylene oxide adducted zwitterionic surfactants were measured such as critical micelle concentration, surface tension, interfacial tension, contact angle, viscosity and foam stability. Also, the dual function characteristics of the zwitterionic surfactants were investigated by determining an isoelectric point, which were obtained using zeta potential measurement and QCM (quartz crystal microbalance) experiments. The isoelectric point of the synthesized zwitterionic surfactant determined by zeta potential measurement was close to that obtained by QCM experiment and both results have shown almost the same trend as that determined by the frictional property measured using an automated mildness tester. In particular, it has been observed that all three surfactants used during this study provide better softening effect at a pH of neutral condition than at an acidic or an alkaline condition. This result indicates that the synthesized surfactants act as a cationic surfactant at a pH of neutral condition and thus provide good softening effect during a rinsing cycle in the detergency process.

Recovery and Utilization of Proteins and Lipids from the Washing Wastewater in Marine Manufacture by Isoelectric Point Shifting Precipitation Method;4. Utilization of the Recovered Protein Fractions as the Alternative Feed of Fish Meal. (수산가공공장폐액의 등전점이동 응집처리에 의한 유용성분재회수이용;4. 회수단백질의 어분 대체 사료로서의 이용)

  • Kim, Gwang-Woo;Kim, Ga-Hyeon;Ueo, Myung-Hee;Kim, Ok-Seon;Cho, Soon-Yeong
    • Journal of Life Science
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    • v.18 no.6
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    • pp.832-838
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    • 2008
  • Mackerel water-soluble protein fraction produced by washing the mackerel meat were concentrated by isoelectric point shifting precipitation process, and the concentrates were utilized as the alternative feed of fish meal. In the 1st aquaculture diet experiment for Israel common carp, the feed conversion ratio decreased in proportion to the rise in the percentage of the recovered protein containing a residual lipid, which was added to the fish meal. It was supposed that the low feed efficiency was because of lipid oxidation in the recovered protein fraction. In addition, 2nd aquaculture diet experiment for Israel common carp was conducted after removing the oxidized lipid in the recovered protein fish meal. When a portion of the fish meal was substituted by the recovered protein devoid of the residual lipid, the feed conversion ratio increased in proportion to the amount of the substitute being added to the fish meal. Therefore, the recovered protein fraction of the mackerel washing wastewater from mackerel processing factory could be used as the alternative feed of fish meal.

Characterization of Endoglucanase (F-II-II) Purified from Trichoderma sp. C-4 (Trichoderma sp. C-4에서 분리한 endoglucanase(F-II-II)의 특성에 대한 연구)

  • 설옥주;최지영;손영준;신지원;한인섭;정대균;정춘수
    • Korean Journal of Microbiology
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    • v.36 no.1
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    • pp.20-25
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    • 2000
  • One of endoglucanases(F-II-II) was purified from the culture filtrate of Trichoderma sp. C-4 through two step procedures including chromatography on Sephacryl S-200 and Sephacryl S-100. The molecular weight of the enzyme was determined to be about 26,000 by SDS-PAGE and the isoelectric point as 8.0 by analytical isoelectric focusing. The optimum temperature of the enzyme was $50^{\circ}C$ and the optimum pH was 5.0. No loss of activity was observed when the enzyme was preincubated at $50^{\circ}C$ for 24 hours. The specific activity of the enzyme toward carboxymethylcellulose (CMC) was estimated to be 776.2 U/mg. The internal amino acid sequence was analysed.

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