• The Journal of the Korean dental association
• /
• v.11 no.3
• /
• pp.205-209
• /
• 1973

법랑질과 상아질의 타액단백의 흡착관계를 구명키 위하여 타액을 법랑질과 상아질 분말의 column에 흡착시킨후 증류수, 3M Nacl, 0.1M phosphate buffer, pH 7.1, 0.2M EDTA 함유한 phosphate buffer와 증류수를 차례로 용출시켜 용출액의 amylase, ribonuclease 및 단백양을 관찰한 결과는 다음과 같다. 1. 타액 amylase와 ribonuclease는 법랑질과 상아질 분말에 모두 흡착하였다. 2. 0.2M EDTA가 함유한 buffer에서는 단백양을 법랑질과 상아질분말에서 모두 33.5%정도 용출되었으나 효소활성은 없었다.

• Korean Journal of Food Science and Technology
• /
• v.30 no.2
• /
• pp.372-378
• /
• 1998

Two types of formaldehyde-treated soy protein isolate (SPI) films, formaldehyde-incorporated and formaldehyde-adsorbed films, and control SPI films were prepared. Cross-linking effect of formaldehyde on selected film properties such as color, tensile strength (TS), elongation at break (E), water vapor permeability (WVP), and water solubility (WS) were determined. Physical properties of formaldehyde-incorporated films were not geneally different from those of control films, while almost all of those among formaldehyde-adsorbed films were significantly different. Through cross-linking development within formaldehyde-adsorbed films, WS decreased significantly (P<0.05) from 26.1% to 16.6%, and TS increased two times while E decreased two times compared with control films. This was caused by insolubilization and hardening of protein by cross-linking most likely attributed to the significant changes in properties of protein films reacted with formaldehyde.

• Korean Journal of Food Science and Technology
• /
• v.23 no.6
• /
• pp.656-660
• /
• 1991

Heats of moisture adsorption of the sunflower nutmeat products (ground nutmeat, meal, protein concentrate and protein isolate) were determined from their isosteres at temperatures 10, 20 and $30^{\circ}C$. The changes in the heat of adsorption with moisture level were analyzed by Hunter equation. The Hunter equation was valid for representing the relationship between the heat of adsorption and the moisture content for the sunflower nutmeat products, and the accuracy-of-fit increased as protein content of the materials increased. The heat of adsorption decreased as moisture content increased, but increased as protein content increased. The heats of adsorption were 11.8-10.6 kcal/mole for the ground nutmeat at 4-12% moisture (d.b.) and 12.4-11.0 kcal/mole for the protein isolate at 6-20% moisture (d.b.).

• Korean Journal of Food Science and Technology
• /
• v.52 no.5
• /
• pp.516-523
• /
• 2020

Supercritical carbon dioxide (_SCO2) extraction was applied for the defatting of mealworm to prepare defatted powder (DP) and protein isolate (PI) and compare the process to press and hexane extraction, with respect to DP and PI physicochemical properties. _SCO2 DP was obtained by extracting 34.40% oil at 41.37 MPa, 40℃ for 180 min, and the product contained 71.66% crude protein, which is similar to that of hexane DP and higher than that of press DP. In using alkali protein extraction to prepare PI from DP, _SCO2 was as effective as hexane and better than press. _SCO2 produced brighter DP and PI than press, but not as much as hexane. Protein solubility was similar in all DP, with minimum values at pH 5. The highest water adsorption capacity was noticeable for _SCO2 PI, and _SCO2 DP showed an oil adsorption capacity comparable to that of hexane DP. _SCO2 DP and PI had better foaming capacity than press DP and PI and showed superior emulsion activity compared to others.

• Korean Journal of Food Science and Technology
• /
• v.20 no.3
• /
• pp.405-411
• /
• 1988

In this study, the treatment of $H_2O_2$, papain and acylation on the protein isolate obtained from defatted sesame oil cake for the changes in amino acids composition, color, digestibility and some functional characteristics of this protein were investigated. The results showed that $H_2O_2$, papain and papain $H_2O_2$ treatment increased the rates of the protein extraction and content of protein in protein isolates when those values were compared to the alkali treatment. Also amino acid composition of the protein isolates were comparatively good, and color, and functional properties and pepsin digestibility were markedly improved. The amount of lysine, the first limiting amino acid of this protein was increased. The solubility, bulk density, water absorption, fat absorption and emulsifying properties were remarkably improved while foaming properties and digestibility was slighly decreased.

• Journal of Chest Surgery
• /
• v.40 no.4 s.273
• /
• pp.273-279
• /
• 2007

Background: We evaluate the efficacy of ultra-hydrophilic coated bypass circuits in comparison with uncoated bypass circuits in a porcine cardiopulmonary bypass model. Material and Method: Normothermic cardiopulmonary bypass was peformed in 10 anesthetized pigs via the left atrium and ascending aorta with a centrifugal biopump. Ultra-hydrophilic coated bypass circuits wore used in 5 pigs (the study group) and uncoated bypass circuits were used for the control group. Platelet counts and platelet aggregation tests were peformed. The thrombin-antithrombin(TAT) complex level and total protein level were evaluated. Result: There were no significant changes En the platelet counts and aggregation ability of both groups. The TAT complex levels were not different between the two groups. The total protein level was significantly lower in the control group after cessation of cardiopulmonary bypass. Conclusion: The clinical effects of ultra-hydrophilic coating circuits were not remarkable, in terms of reducing inflammatory reaction and protection of platelet function. However, the effect of protection for blood protein adsorption might be acceptable.

• Journal of the Korean Chemical Society
• /
• v.52 no.1
• /
• pp.57-65
• /
• 2008

are nanometer or micrometer scale vesicles that can be used as drug delivery carriers. However, plain liposomes are plagued by rapid opsonization, making their circulation time in bloodstream be shortened. In this study, model protein, bovine serum albumin (BSA)-coated liposomes were prepared by coating cationic liposomes with BSA molecules at higher pH than isoelectric point of BSA. The BSA molecules coated on the liposomal surface were denatured by thermal treatment at above 60oC. While both plain and cationic liposomes had about mean particle diameter of 1041 nm, BSA-coated cationic liposomes (BCL) had mean particle diameter of 1091 nm. Encapsulation of model drug, doxorubicin (DOX), in liposomes were carried out by using remote loading method and the loading efficiency of DOX to liposomes was about 90%. The mean particle diameter of BCL did not increase in blood plasma and adsorption of plasma protein was much less than plain or cationic liposomes. These results suggest that BCL can be used as a long-circulating liposomes in bloodstream.

• Journal of Korean Ophthalmic Optics Society
• /
• v.21 no.2
• /
• pp.109-117
• /
• 2016

Purpose: The study was aimed to figure out the effect of materials and pigmentation of soft contact lens on the adherence of Staphylococcus aureus upon soft contact lenses deposited with tear components. Methods: The number of adherent S. aureus on clear and circle soft contact lenses made of etafilcon A, hilafilcon B, nelfilcon A was measured before and after incubation in artificial tear. Furthermore, the denaturalization level of tear protein with time after incubation in artificial tear was estimated by electrophoresis. Results: The adherence of S. aureus was significantly different according to the lens materials. The pattern of bacterial adherence on clear and circle contact lenses was different. That is, the adherent amount of S. aureus was somewhat larger on circle lens made of etafilcon A however, amount on circle lenses made of hilafilcon B and nelfilcon A was 89.3% and 71.3% of the number on clear lenses. When the tear protein was deposited on contact lenses, the number of adherent bacteria decreased and its degree was varied according to the lens material. The degree of decrease was the biggest in clear soft lens made of etafilcon A. Anti-bacterial effect of tear protein decreased with time after deposition of tear protein on soft contact lens and the amount of lysozyme also decreased. The reduction of anti-bacterial effect and quantity of lysozyme was different according to contact lens materials and pigmentation. Conclusions: It was revealed that the adherence of S. aureus depends on contact lens materials and pigmentation, and the specification of lens material affects more on adherence of S.aureus than pigmentation. It was further figured out the denaturalization level of anti-bacterial protein on soft contact lens varies according to lens materials and pigmentation, which produces an effect on the quantity of bacterial adherence.

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.35 no.9
• /
• pp.1251-1255
• /
• 2006

To improve the water resistance and physical properties of soy protein isolate (SPI)-coated paper, effects of concentrations of soy protein isolate and plasticizer were examined. Physical properties such as elongation strength (ES), elongation rate (E), water vapor permeability (WVP), and water solubility (WS) were evaluated. The film made from 5% soy protein isolate (SPI) and 40% glycerol (plasticizer) suggested a good application for a film preparation. SPI coated paper showed the highest ES (21.62 MPa) and the lowest WVP $(2.06ng{\cdot}m/m^2{\cdot}s{\cdot}Pa)$ and WS (1.17%). This study suggested that soy protein isolate (SPI) can be used as a coating material for the coated paper to improve the water resistance.

• Korean Journal of Food Science and Technology
• /
• v.18 no.6
• /
• pp.468-474
• /
• 1986

The emulsifying properties of soy protein isolate were measured at various conditions, and the relationships between the emulsifying properties and solubility, viscosity, hydrophobicity, protein adsorption, the tension at water-oil interface were investigated. The emulsifying properties are minimum at the isoelectric point(pI), and the effect of pH parallels its effect on protein solubility. The emulsifying activity is increasing up to $50^{\circ}C$ and then is somewhat decreasing above that temperature, while the emulsion stability is continuously decreasing. Except for phosphates, the salts cause the decrease of the emulsifying properties. The hydrophobicity is increasing as the temperature increases and decreasing somewhat as pH gets lower. However, it is increasing substantially at pH below the pI. The maximum protein adsorption at the water-oil interface is 0.78, 0.47, and $0.33mg/m^2$ at pH 2, 7, and 4, respectively. The tension at water-oil interface is 19.76 dyne/cm in the absence of soy protein, whereas it is decreasing to 11.45-18.08 dyne/cm in the presence of the protein.