• Korean journal of food and cookery science
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• v.9 no.1
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• pp.43-51
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• 1993

Buckwheat protein isolate was tested for the effects of pH, addition of sodium chloride and heat treatment on solubility, emulsion capacities, emulsion stability, surface hydrophobicity, foam capacities and foam stability. The solubility of buckwheat protein isolate was affected by pH and showed the lowest value at pH 4.5, the isoelectric point of buckwheat protein isolate. The solubility significantly as the pH value reached closer to either ends of the pH, i.e., pH 1.0 and 11.0. The effects of NaCl concentration on solubility were as follows; at pH 2.0, the solubility significantly decreased when NaCl was added; at pH 4.5, it increased above 0.6 M; at pH 7.0 it increased; and at pH 9.0 it decreased. The solubility increased above $80^{\circ}C$, at all pH ranges. The emulsion capacity was the lowest at pH 4.5. It significantly increased as the pH approached higher acidic or alkalic regions. At pH 2.0, when NaCl was added, the emulsion capacity decreased, but it increased at pH 4.5 and showed the maximum value at pH 7.0 and 9.0 with 0.6 M and 0.8 M NaCl concentrations. Upon heating, the emulsion capacity decreased at acidic pH's but was maximised at pH 7.0 and 9.0 on $60^{\circ}C$ heat treatment. The emulsion stability was the lowest at pH 4.5 but increased with heat treatment. At acidic pH, the emulsion stability increased with the increase in NaCl concentration but decreased at pH 7.0 and 9.0. Generally, at other pH ranges, the emulsion stability was decreased with increased heating temperature. The surface hydrophobicity showed the highest value at pH 2.0 and the lowest value at pH 11.0. As NaCl concentrationed, the surface hydrophobicity decreased at acidic pH. The NaCl concentration had no significant effects on surface hydrophobicity at pH 7.0, 9.0 except for the highest value observed at 0.8 M and 0.4 M. At all pH ranges, the surface hydrophobicity was increased, when the temperature increased. The foam capacity decreased, with increased in pH value. At acidic pH, the foam capacity was decreased with the increased in NaCl concentration. The highest value was observed upon adding 0.2 M or 0.4 M NaCl at pH 7.0 and 9.0. Heat treatments of $60^{\circ}C$ and $40^{\circ}C$ showed the highest foam capacity values at pH 2.0 and 4.5, respectively. At pH 7.0 and 9.0, the foam capacity decreased with the increased in temperature. The foam stability was not significantly related to different pH values. The addition of 0.4 M NaCl at pH 2.0, 7.0 and 9.0 showed the highest stability and the addition of 1.0 M at pH 4.5 showed the lowest. The higher the heating temperature, the lower the foam stability at pH 2.0 and 9.0. However, the foam stability increased at pH 4.5 and 7.0 before reaching $80^{\circ}C$.

• Preventive Nutrition and Food Science
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• v.2 no.4
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• pp.333-337
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• 1997

Trans-cinnamic acid-4-hydroxylase(tC4H) is the first cytochrome P450-dependent monooxygenase of the phenylpropanoid pathway. The roots of avocado seedlings were wounded and examined to determine whether the tC4H would be activated in response to wounding and/or whether tC4H activity be modulated by the application of exogenous p-coumarate. At the specified length of times, the wounded and treated roots were either frozen in liquid nitrogen or used immediately to extract microsomal proteins. The microsomal proteins were subjected to immunoblot analysis using polyclonal antibodies against CYP73 of tC4H gene. In this study, tC4H was induced in wounded roots sealed in bags within 6 hours, and in low level({TEX}$10^{-8}${/TEX}M) of p-coumarate solution within 24 hours, whereas the olution without p-coumarate and high levels of p-coumarate solution repressed tC4H induction in wounded roots. These results indicate that tC4H is induced by wounding in the root of avocado, and is inhibited by the application of exogenous p-coumarate.

• 한국신재생에너지학회:학술대회논문집
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• 2009.06a
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• pp.31-31
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• 2009

PECVD를 이용하여 제조된 미세결정질 p-i-n 실리콘 박막 태양전지에서, p 층은 태양전지의 윈도우 역할 및 그 위에 증착될 i ${\mu}c-Si:H$ 층의 'seed'층 역할을 수행하기 때문에, p층의 구조적 및 전기적, 광학적 특성은 태양전지의 전체 성능에 큰 영향을 미칠 수 있다. 본 연구에서는 $SiH_4$ 농도를 변화시켜 각기 다른 결정 특성을 갖는 p ${\mu}c-Si:H$층을 제조하고 그 위에 i ${\mu}c-Si:H$ 층을 증착하여 p층의 결정 특성변화와 그에 따른 i ${\mu}c-Si:H$ 층 및 'superstrate' p-i-n 미세결정질 실리콘 박막 태양전지의 특성 변화를 조사하였다. P층의 경우, $SiH_4$ 농도가 증가함에 따라 결정분율 (Xc)이 감소하여 비정질화되었으며 그에 따라 dark conductivity가 감소하는 경향을 나타내었다. 각기 다른 결정분율을 가지는 p 'seed' 층 위에 증착된 태양전지는, p 'seed' 층의 결정분율이 증가함에 따라 개방전압, 곡선인자, 변환효율이 경향적으로 감소하였다. 이는 p 층 결정분율 변화에 따른 p/i 계면특성 저하 및 그 위에 증착되는 i ${\mu}c-Si:H$ 층의 결함밀도 증가 등에 따른 태양전지 특성 감소 때문인 것으로 판단되며, 이를 분석하기 위하여 i ${\mu}c-Si:H$ 층의 전기적, 구조적 특성 분석 및 태양전지의 dark I-V 특성 등을 분석하고자 한다.

• Food Science and Biotechnology
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• v.18 no.4
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• pp.954-958
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• 2009

Effects of controlled- and uncontrolled-pH operations on phenylalanine ammonia lyase (PAL) production by a recombinant Escherichia coli strain were investigated at uncontrolled-pH ($pH_{UC}$) and controlled-pH ($pH_C$) of 5.5, 6.0, 6.5, 7.0, 7.5, 8.0, and 8.5 in bioreactor systems. The results showed that the recombinant PAL activity was improved significantly by controlled pH strategy. Among the $pH_C$ operations, the highest PAL activities were obtained under $pH_C$ 7.5 strategy where cell mass ($OD_{600\;nm}$) and PAL activity was 1.3 and 1.8 fold higher than those of $pH_{UC}$, respectively. The maximum PAL activity reached 123 U/g. The $pH_C$ 7.5 strategy made recombinant plasmid more stable and therefore allowed easier expression of PAL recombinant plasmid, which increased PAL production. It was indicated that the new approach (controlled-pH strategy) obtained in this work possessed a high potential for the industrial production of PAL, especially in the biosynthesis of L-phenylalanine.

• Microbiology and Biotechnology Letters
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• v.20 no.6
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• pp.647-654
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• 1992

In order to study the physiological properties of the intestinal bacteria, we isolated the intestinal bacteria of Koreans and tested the enzymatic patterns. Isolated Bifidobacterium sp. Int-57 had the higher activity of $\alpha$-glucosidase, $\beta$-glucosidase, $\alpha$-galactosidase, $\beta$-galactosidase. $\beta$-xylosidase and $\alpha$-arabinofuranosidase than other intestinal microorganisms. The effect of the carbon sources on the production of each enzymes of Bijidobacterium sp. Int-57 was investigated. The most suitable carbon source for the production of $\beta$-glucosidase was maltose, for a-glucosidase cellobiose, for $\alpha$-galactosidase raffinose, for $\beta$-galactosidase lactose, and for $\beta$-xylosidase and $\alpha$-arabinofuranosidase xylose, respectively. In addition, we investigated the optimal conditions and pH stability of each crude enzymes. The optimal condition of a-glucosidase was pH 6.0 and $40^{\circ}C$. that of Jj-glucosidase pH 7.0 and 50oe, that of $\beta$-galactosidase pH 7.0 and $50^{\circ}C$, that of $\beta$-xylosidase pH 6.0 and $40^{\circ}C$ , and that of $\alpha$-arabinofuranosidase pH 5.0 and $50^{\circ}C$. respectively. a-Glucosidase was stable at pH 4.0-9.0. Jj-glucosidase at pH 4.0-7.0. $\beta$-galactosidase at pH 4.0-9.0, $\beta$-xylosidase at pH 4.0-6.0, and /3-arabinofuranosidase at pH 7.0-9.0, respectively.

• Bulletin of the Korean Chemical Society
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• v.26 no.8
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• pp.1185-1189
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• 2005

Two new copper vanadium borophosphate compounds, $(NH_4)(C_2H_{10}N_2)_{5.5}[Cu(C_2H_8N_2)_2]_3[V_2P_2BO_{12}]_6{\cdot}17H_2O,\;Cu-VBPO1\;and\;(NH_4)(C_2H_{10}N_2)_{3.5}[Cu(C_2H_8N_2)_2]_5[V_2P_2BO_{12}]_6{\cdot}18H_2O$, Cu-VBPO2 have been hydrothermally synthesized and characterized by single crystal X-ray diffraction, thermogravimetric analysis, IR spectroscopy, and elemental analysis. The structure of Cu-VBPO1 contains a layer anion, {$[Cu(C_2H_8N_2)_2]_3[V_2P_2BO_{12}]_6$}$^{12-}$, whereas Cu-VBPO2 has an open framework anion, {$[Cu(C_2H_8N_2)_2]_5[V_2P_2BO_{12}]_6$}$^{8-}$. Crystal Data: $(NH_4)(C_2H_{10}N_2)_{5.5}[Cu(C_2H_8N_2)_2]_3[V_2P_2BO_{12}]_6{\cdot}17H_2O$, monoclinic, space group I2/m (no. 12), $\alpha$ = 15.809(1) $\AA$, b = 31.107(2) $\AA$, c = 12.9343(8) $\AA$, $\beta$ = 104.325(1)$^{\circ}$, Z = 2; $(NH_4)(C_2H_{10}N_2)_{3.5}[Cu(C_2H_8N_2)_2]_5[V_2P_2BO_{12}]_6{\cdot}18H_2O$, tetragonal, space group $P4_2$/mnm (no.136), $\alpha$ = 26.832(1) $\AA$, c = 18.021(1) $\AA$, Z = 4.

• Journal of Nutrition and Health
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• v.8 no.1
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• pp.65-69
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• 1975

Human chorionic gonadotropin hormone(H.C.G.) is secreted from the villus tissues of the placenta and excreted in lange amount into the urine. Its isolation is chiefly made from the urine of a pregnant woman. Recently, Matsushima attempted isolation of H.C.G. directly from the placenta itself. In order to prepare H.C.G. from human placenta, general method of extractiag and purifying proteins was applied. Its way was as follow: Crude H.C.G. was extracted from placenta with pH 9.0 and pH 5.0 aqua ammonia, and purified with pH 8.0 ammonia and 50% ethanol at pH 4.8. The purified H.C.G. showed two moving bands on the anode by paper electrophoresis. On the other hand, the H.C.G. from pregnancy urine (Standard. Pharm. Co.) showed same two bands but their moving ratio were different. The purified H.C.G. showed gonadotropin effect when it was injected young fomale rats 40r/cc per day for 5 days and weighted the increased ovary weight.

• Korean Journal of Food Science and Technology
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• v.33 no.1
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• pp.19-23
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• 2001

Physicochemical properties including viscosity, temperature and pH stability, color turbidity and moisture retention power of xylooligosaccharide(XO) as food material were investigated to apply to food process. The viscosity of 70 bx XO was 930 cP at $20^{\circ}C$ and 90 cP at $60^{\circ}C$, which was higher than that of sugar but lower than that of other oligosacchrides. XO remained stable after heat treatment for 1hr at $100^{\circ}C$ and pH 2.5 to 8.0 indicating excellent heat and pH stability. The pH of XO was measured $5.0{\pm}0.1$ and the color turbidvity of XO was very low at pH $2.5{\sim}4.0$. The color turbidity of XO increased as pH increased, but it was not high enough to affect food process. When heated with 1% glycine the color turbidity of XO was very low and changed little with pH changes. To measure moisture retention power XO was stored at $25^{\circ}C$ and 75% relative humidity for 71 day. XO retained more than 95% of the original weight; whereas sugar lost 28%. These results suggest that XO has useful physicochemical properties for various food process to improve the functionality of food.

• Microbiology and Biotechnology Letters
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• v.19 no.4
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• pp.383-389
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• 1991

In order to produce alkaline protease, psychrotrophic bacterium which have high enzyme activity at low temperature, was isolated by using enrichment culture from various samples and identified as genus alkalopsychrotropic Pseudomonas sp. RP-222. The optimal culture conditions for enzyme production were pH- 10.0, temperature-$20^{\circ}C$ and culture time-4 days. The optimum pH and temperature for the enzyme activity were pH 10.5 and $40^{\circ}C$, respectively and the enzyme was relatively stable at pH 7.0~13.0 and below $50^{\circ}C$. The enzyme was inhibited by ethylenediaminetetraacetate and phenylmethylsulfonylfluoride, indicating that the enzyme was a serine metalloenzyme, but considerably stable in the presence of surface active agents. Activity of the enzyme was increased by the addition of 0.05% Na-$\alpha$-olefin sulfonate.

• Solar Energy
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• v.20 no.1
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• pp.11-20
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• 2000

To get more insight into the buffering effects of the p-${\mu}c$-Si:H Inserted at the p-a-SiC:H/i-a-Si:H interface, we present a systematic numerical simulation using Gummel-Schafetter method. The reduced recombination loss at the p/i interface due to a constant bandgap buffer is analysed in terms of the variation of the p/i Interface region with a short lifetime and the characterisitics of the buffer such as mobility bandgap, acceptor concentration, and D-state density. The numerical modeling on the constant bandgap buffer demonstrates clearly that the buffering effects of the thin p-${\mu}c$-Si:H originate from the shrinkage of highly defective region with a short lifetime in the vicinity of the p/i interface.