• Biomolecules & Therapeutics
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• 제1권1호
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• pp.31-36
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• 1993

To evaluate the feasibility of transmucosal delivery of methionine enkephalin analog, [$D-Ala^2$]-me-thionine enkephalinamide (YAGFM), the influence of pH, temperature, ionic strength and initial peptide concentration on the physicochemical stability of YAGFM in aqueous buffered solutions were investigated using a stability-indicating HPLC method. The degradation of YAGFM followed the pseudo-first-order kinetics. From the pH-rate profile, the maximum stability of YAGFM was shown to be at the pH of about 5.0. The halflife for the degradation of YAGFM was found to be 181.3 days at pH 5.0 and $37^{\circ}C.$ Arrhenius plots of the data obtained at 25~$45^{\circ}C$ were reasonably linear with a correlation coefficient greater than 0.99, and the activation energy was calculated to be 8.9 kcal/mole. A higher ionic strength and/or a higher peptide concentration in buffered solutions retarded the degradation of YAGFM.

• 한국식품영양학회지
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• 제20권4호
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• pp.349-355
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• 2007

Periodate-oxidized soluble starch was reacted with papain at pH 4.0, pH 7.0, and pH 9.7, and an oxidized soluble starch-papain conjugate was produced. When compared with native papain, the specific activity decreased to 60%, in both the modified papain reacted with 0.4% $NaBH_4$ and in the modified papain not reacted with $NaBH_4$. The specific activity decreased to 70% in the modified papains reacted with 1.5% $NaBH_4$ and 4.0% $NaBH_4$, respectively. The reduction by $NaBH_4$ did not have an effect in the thermal stability of either the modified or nonmodified papain. An activity of 54.7% remained in the papain modified at pH 4.0, which was incubated at $80^{\circ}C$ for 40 min. The papains modified at pH 7.0 and pH 9.7 and incubated for 40 min at two different temperatures, respectively, were stable to $60^{\circ}C$, and at $80^{\circ}C$ their activities at 56.3% and 44.1 %, respectively. The modified papain's thermal stability pattern was similar to that of native papain, with no increase in its statbility. In the range of pH $2.0{\sim}13.0$, the stability of the papain modified at pH 4.0 decreased greatly between pH $3.0{\sim}5.0$, but it was similar to the native papain at other pH values. The stability of the papain modified at pH 7.0 showed a similar pattern to the native papain at pH $2.0{\sim}6.0$, while its stability increased when moving into the alkali pH range. The papain modified at pH 9.7 also had increased stability, when moving into the alkali range. The results of Hammerstein milk casein, which was reacted with the papains modified at pH 4.0, pH 7.0, and pH 9.7, respectively, and analyzed by FPLC, showed different peaks according to the different modification pHs, and the greatest peak differences were observed with the modification at pH 9.7.

• 한국식품조리과학회지
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• 제7권3호
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• pp.53-59
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• 1991

This study was carried out in order to investigate the change of protein functionalities such as foaming and emulsifying properties by succinylation of protein isolates. Succinylated and unsuccinylated munghean protein isolates were tested for finding out the effects of pH, heat treatment and sodium chloride concentration on the solubility, emulsion capacity, emulsion stability, foaming capacity, and foam stability. The results are summarized as follows: 1. Succinylation enhanced the solubility of MPI except at pH 4.5. When heated, succinylation greatly increased the solubility of succinylated MPI above $60^{\circ}C$. With the addition of NaCl, succinylation increased the solubility of MPI at acidic condition. 2. Emulsion capacity of succinylated MPI showed the lowest value at pH 7 and higher values at acidic and alkaine condition. when succinylated MPI was heated, emulsion capacity showed the highest at $80^{\circ}C$. With NaCl was added, emulsion capacity of succinylated MPI lincreased at pH 7, 9 or 11 decreased at pH 3 except addition of 1.0M NaCl. 3. Emulsion stability of MPI and succinylated MPI showed the highest at pH 4.5. Succinylation enhanced the emulsion stability of MPI at acidic condition. 4. The foaming capacity of MPI was increased at pH 3, 7 or 9 by succinylation. 5. When heated, foam stability of MPI and succinylated MPI showed the highest at pH 4.5 and at pH 11, respectively. When heated, both proteins showed the highest stability at $100^{\circ}C$.

• Journal of Animal Science and Technology
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• 제47권5호
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• pp.851-856
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• 2005

본 연구는 살균온도, pH 및 소화효소의 처리에 따른 anti-H. pylori IgY의 안정성을 평가하였다. 열 안정성 실험시 모든 처리구에서 anti- H. pylori IgY 함량은 대조구에 비해서 유의적으로 감소되었다(p＜0.05). 그러나 저온살균 처리구(63$^{\circ}C$, 30분)와 초고온살균 처리구(130$^{\circ}C$, 2초)에서 WSF 중 anti-H. pylori IgY 함량은 각각 76%와 78% 이었다. pH의 안정성은 pH를 7.0에서 1.5로 감소시킴에 따라 anti-H. pylori IgY의 함량은 감소되는 경향을 보였다. pH 5.0으로 조정한 WSF를 37$^{\circ}C$에서 1시간 처리한 후 anti-H. pylori IgY의 함량은 84.4%인데 비해서 pH 2.5에서는 28.6%의 anti-H. pylori IgY 함량을 보였다. 그리고 pepsin과 trypsin을 처리한 후 anti-H. pylori IgY의 안정성도 평가하였다. 100 unit의 pepsin에서 1시간과 2시간 처리시에는 시간에 따른 항체의 함량은 차이가 없었으나, 200 unit의 pepsin 처리구에서는 시간에 따른 항체 함량이 유의적으로 차이가 있었다(P＜0.05). 그러나 pepsin의 농도나 반응시간에 관계없이 pH 4.0에서 항체는 비교적 안정하였다. pH 7.0, 37 $^{\circ}C$에서 trypsin을 처리한 후 난황액과 WSF 중 anti-H. pylori IgY의 함량은 반응시간의 증가에 따라서 유의적으로 감소되었다(P＜0.05). 난황액 중 항체 함량은 120분 처리시 85%가 잔존하였으나, WSF 중 항체 함량은 30분 처리시 62%로 감소하였다. Trypsin을 처리한 후 난황중의 항체의 안정성은 WSF 보다 유의적으로 높았다(P＜0.05).

• 미생물학회지
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• 제13권2호
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• pp.59-63
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• 1975

When the enzyme preparations were at various temperatures for 1 hour, the thermal stability for the enzyme was maximum at $30{\circ}C.$ The optimum temperature for the enzyme activity was at $40{\circ}C.$ When the enzyme preparations were exposed to various pHs for 22 hours, the enzyme stability was maximum at pH 3.8, and it was decreased gradually as the pH rose up to 4.8, above which the stability was greatly restored. When the exposure period was extended from 22 to pH's 3.0 and 5.9, but the stability tended to rise at pH's below 3.0 and above 5.9. The optimum pH for the enzyme activity was obtained at 4.8.

• 한국식품조리과학회지
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• 제6권4호통권13호
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• pp.9-14
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• 1990

The emlsifying properties of small red bean protein isoates were evaluated through their emulsion capacity and stability of the resulting emulsions. The influence of pH, Sodium Chloride and heat treatment on the efficiency of small red bean protein isolates as emulsifying agents was studied. The surface hydrophobicity (So) of small red bean protein islates also examined. The results were obtained as follows; 1. The emusion capacity of small red bean protein isolates was high at pH 11, low at pH 3 and decreased by heat treament. With addition of NaCl, emulsion capacity decreased steadily and showed lowest value when 0.2M NaCl was added. 2. The emulsion stability at pH 4.5 and heat treatment over $60^{\circ}C$ decreased emulsion stability at pH 4.5. When NaCl was added, emulsion stability was generally increased. 3. The surface hydrophobicity of small red bean protein isolates showed the highest value at pH 3 and lowest at pH 11 and increased as the heating temperature increased When 0.2 M NaCl was added, surface hydrophobicity also increased at pH 4.5.

• 대한화학회지
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• 제28권1호
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• pp.14-19
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• 1984

메트미오글로빈의 압력에 의한 변성의 $H_2O$와 $D_2O$에서의 차이를 pH 5.7과 pH 7.0에서 연구하였다. 메트미오글로빈은 $D_2O$에서 $H_2O$보다 더 작은 압력에서 변성하였다. 그 차이가 pH 5.7에서가 pH 7에서 보다 더 컸다. $H_2O$와 $D_2O$에서 이 안정도의 차이가 단백질에 대한 $H^+$와 $D^+$의 결합에 차이가 있기 때문이며 또한, 수소가 중수소로 바뀜에 따르는 구조 변화 때문인 것으로 사료된다.

• 대한가정학회지
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• 제28권2호
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• pp.37-45
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• 1990

The purpose of this study was to determine the foaming properties of two small red bean protein isolates at various conditions. Data concerning the effects of pH, temperature, MaCl concentration, sugar concentration and protein concentration on the properties such as solubility, foam expansion, foam stability were presented. The results were summarized as follows : 1. The crude protein contents of two small red beans were 26.14% and 22.71%. The percentage of nonpolar amino acid group was the highest and that of sulfur containing amino acid group was the lowest. 2. Protein solubility showed the minimum at pH 4.5 which is isoelectric point of small red bean protein isolate adn heat treatment lowered solubility(P<0.05). At pH 4.5, solubility increased sighificantly as 0.4M NaCl was added. However, the effect of sugar concentration in the solubility was not significant. 3. Foam expansion of two small red bean protein isolates was high at pH 4.5 and heat treatment at 10$0^{\circ}C$ lowered foam expansion(P<0.05). While addition of NaCl, sugar did not affect the foma expansion, gradual increment of the protein isolates concentration up to 9% decreased the foma expansion slightly. 4. Foam stability was significantly high at pH 4.5 and heat treatment at 10$0^{\circ}C$ lowered foam stability. Addition of sugar caused slight decrease in foam stability. From 1% to 9% suspension, foma stability increased significantly as protein concentration increased(P<0.05)

• 한국식품조리과학회지
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• 제12권1호
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• pp.54-59
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• 1996

Immunoglobulins (IgY) were isolated from egg yolk of hens immunized with bovine serum albumin(BSA). The stability of anti-BSA IgY against heat and pH was investigated. Antibody activity was measured by enzyme linked immunosorbent assay. IgY was relatively heat-stable and most of the antibody activity remained after heating up 65$^{\circ}C$ for 30 minutes. IgY was stable at pH 5-11. However, inactivation of IgY was observed below pH 4, or above pH 12. Inactivation of IgY proceeded rapidly at low pHs(pH 2-3). Most of the antigen binding activity was lost at low pHs probably because of some conformational changes.

• 한국식품영양학회지
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• 제9권3호
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• pp.247-252
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• 1996

$\beta$-Amylase was purified from sweet potato by acetone fractlonatlon, Sephadex A-50 ion exchange chromatography and Sepgadex G-200 gel chromatographyl The higher enzyme concentration was, the higher heat stability of enzyme became. After 1 hour 30 minute. At 6$0^{\circ}C$ in pH 5, enzyme under concentration of 30$\mu$l/ml lost its activity completely and over the concentration of 100$\mu$g/ml remained 25% of activity. The enzyme was stabilized at range of pH 4~10 and pH stability was increased by glycerol. Five moles of NaCl inhibited completely of the enzyme activity. SDS of 0.05% inhibited the enzyme completely after 12 hours at 37$^{\circ}C$ in pH5. One mole guanidine-HCl and 8M urea inhibited the entire enzyme after 13 hours at 37$^{\circ}C$ in pH 5.