• Journal of Nutrition and Health
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• 제29권8호
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• pp.861-866
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• 1996

Tannins in plant foods and beverages may produce antinutritional or toxic effects although some proteins with high affinity for tannins seem to function as defense mechanism to tannin toxicity. Our objectives were to investigate of tea tannins, iron and protein and to evaluate the role of proteins in tannin effects on iron solubility. Iron solubility in vitro was measured using tea with and without proteins. Mixtures of tea, protein in varying concentrations(either gelatin or bovine serum albumin), and iron(eithe 10 or 50ug/mL) were prepared. Controls contained water in place of tea. Iron bioavailability was assessed by measuring iron solubility in the simulated gastric condition with pepsin digestion. Bound iron was removed by centrifugation and soluble in tea alone. When iron concentratin was 10ug/mL, addition of small amounts of protein to tea dramatically reduced iron solubility, but solubility of iron increased in the tea mixturea as the concentration of protein was increased. The percnetage of iron that precipitated was much greater at 10ug Fe/mL than the values at 50ug Fe/mL suggesting that the iron binding sites on the tea-protein complex was saturated. These results suggest that interactions of iron with tea tannins are influenced by the concentratins of protein and iron.

• 한국식품과학회지
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• 제22권3호
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• pp.343-349
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• 1990

pH를 달리한 수용액 및 농도를 달리한 염류수용액에서 들깨종실의 단백질과 phytate의 용해도를 측정하여 단백질로부터 phytate를 제거할 수 있는 조건을 검토하였다. 들깨종실단백질의 용해도는 pH4.0에서 가장 낮은 9.5%로 등전점을 보였고, 그보다 산성 또는 알칼리성쪽으로 갈수록 증가되었다. 반면에 phytate의 용해도는 pH5.0에서 가장 높았으며 그보다 산성 또는 알칼리성쪽으로 갈수록 감소되었다. NaCl 수용액을 처리하였을 때 단백질의 용해도는 pH $3.0{\sim}4.0$ 범위에서 가장 낮았고 pH 6.0 이상에서는 현저히 증가되었다. Phytate의 용해도는 pH$2.0{\sim}5.0$ 범위에서는 약 90%내외로 높았으나 pH6.0 이상에서는 급격히 감소되었다. $Na_2SO_3$ 수용액처리에서는 단백질 용해도가 $pH2.0{\sim}3.0$ 범위에서 가장 낮았고 phytate의 용해도는 $pH5.0{\sim}6.0$에서 최대치를 보였고, 3%의 경우는 전 pH 구간에 걸쳐서 낮았으나 5%와 7%에서는 전 구간에서 높았다. $CaCl_2$ 수용액처리에서는 단백질 용해도가 3% 수용액에서는 전 pH 구간에서 낮았으나 5%와 7%에서는 $pH5.0{\sim}10.0$에서 높은 값을 보였으며 phytate의 용해도는 $pH2.0{\sim}3.0$ 사이에서 최대값을 나타내고 pH4.0이상에서는 급격히 감소하였다. 이상의 결과에서 3% NaCl 용액을 사용하여 pH9.0에서 단백질을 추출하고 pH4.0에서 침전시켰을 때 단백질 수율이 좋고 phytate 잔존량이 가장 적어, 저(低)phytate 분리단백질을 만드는 가장 좋은 조건이었다..

• Asian-Australasian Journal of Animal Sciences
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• 제29권8호
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• pp.1159-1165
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• 2016

The nutritional value of feed proteins and their utilization by livestock are related not only to the chemical composition but also to the structure of feed proteins, but few studies thus far have investigated the relationship between the structure of feed proteins and their solubility as well as digestibility in monogastric animals. To address this question we analyzed soybean meal, fish meal, corn distiller's dried grains with solubles, corn gluten meal, and feather meal by Fourier transform infrared (FTIR) spectroscopy to determine the protein molecular spectral band characteristics for amides I and II as well as ${\alpha}$-helices and ${\beta}$-sheets and their ratios. Protein solubility and in vitro digestibility were measured with the Kjeldahl method using 0.2% KOH solution and the pepsin-pancreatin two-step enzymatic method, respectively. We found that all measured spectral band intensities (height and area) of feed proteins were correlated with their the in vitro digestibility and solubility ($p{\leq}0.003$); moreover, the relatively quantitative amounts of ${\alpha}$-helices, random coils, and ${\alpha}$-helix to ${\beta}$-sheet ratio in protein secondary structures were positively correlated with protein in vitro digestibility and solubility ($p{\leq}0.004$). On the other hand, the percentage of ${\beta}$-sheet structures was negatively correlated with protein in vitro digestibility (p<0.001) and solubility (p = 0.002). These results demonstrate that the molecular structure characteristics of feed proteins are closely related to their in vitro digestibility at 28 h and solubility. Furthermore, the ${\alpha}$-helix-to-${\beta}$-sheet ratio can be used to predict the nutritional value of feed proteins.

• 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)

• 한국식품과학회지
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• 제33권6호
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• pp.769-773
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• 2001

두유에서 발생되는 비지와 대두의 일반성분과 단백질의 추출률을 비교하기 위해 시간, 온도, pH별로 분석하였고, 단백질 분자들 사이의 상호작용에 관여하는 물질 urea, SDS, 2-mercaptoethanol를 사용하여 비지단백질의 insolubilization mechamism을 조사하였다. 또한 enzyme modification으로 기능성을 향상시켜 식품소재로서의 이용 가능성에 대해 분석하였다. 비지와 대두는 각각 37.3%, 42.5%의 단백질을 함유하고 있으며 비지는 생산공정 증의 과도한 열처리에 의하여 극히 낮은 용해도를 나타냈다. 비지단백질의 낮은 용해도는 주로 disulfide bonding에 의한 cross linking에 기인하는 것으로 밝혀졌다. 비지단백질과 대두단백질은 pH 3, pH 4에서 가장 낮은 용해도를 보였다. Carbohydrase와 protease를 첨가하여 단백질의 추출츌을 비교한 결과는 비지와 대두는 carbohydrase에서 미세한 반응을 보여 단백질의 용해도에 큰 영향을 주지 못하였으나 여러 protease 가운데 Alcalase는 비지단백질의 용해도를 급격히 증가시켰다.

• 한국식품과학회지
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• 제24권3호
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• pp.279-283
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• 1992

식물성 식품중의 영양 저해 인자로 알려진 phytate를 제거한 분리 유채단백(low-phytate rapeseed protein isolate)을 제조하여 pH 및 phytate 첨가량이 이들 분리 유채단백의 용해성과 소화율에 미치는 영향을 살펴보았다. 분리 유채단백의 phytate 함량은 1.5%로서 탈지 유채분말보다 66%가 감소되었으며 protein : phytate ratio는 58 : 1이었다. 분리 유채단백의 용해도는 pH 2.0과 pH 11.5에서는 매우 높았으나 pH 5.0에서는 매우 낮았다. 그 용해도에 미치는 phytate 첨가량의 영향을 보면 pH 5.0과 pH 11.5에서는 별 차이가 없었으나 pH 2.0에서는 phytate 첨가량이 많을수록 그 용해도가 감소하였다. 분리 유채단백의 pepsin 소화율에 미치는 phytate의 저해적 영향은 phytate 함량이 증가할수록 더 커졌다. 소화기간 초기에는 그 영향이 매우 컸으나 소화시간이 길어짐에 따라 그 영향은 점점 감소되었으며 평균소화율은 24%가 감소하였다. 따라서 유채단백을 식품소재로 이용하기 위해서는 phytate 함량이 낮은 제품을 제조함으로써 그의 기능성과 영양가를 향상시킬 수 있을 것이다.

• 한국축산식품학회지
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• 제21권3호
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• pp.192-199
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• 2001

The objective of this study was to investigate the effects of hot- and cold-boning on sarcomere length, drip loss and protein solubility of post-rigor porcine longissimus muscle. A total of ten pigs(borrow, 100$\pm$5 kg) were randomly selected at a commercial plant and the carcasses were split in half after slaughter. The longissimus muscle of the left side was dissected and chilled at 0$^{\circ}C$ after trimming of subcutaneous fat whereas the right side carcasses were served for cold-boning after chilling for 24 hrs. The temperature, pH and sarcomere length of porcine longissimus muscle were measured at postmortem 1, 3, 6, 12 and 24 hours. Drip loss, cooking loss, Minolta L*a*b*, shear force and protein solubility were measured at postmortem 24 hrs. The pH of cold-boning samples was rapidly decreased whereas temperature and sarcomere length of hot-boning samples were rapidly decreased during 24 hrs of chilling. Hot-boning muscles showed significantly (P<0.05) higher pHu and shorter sarcomere compared with cold boning muscles because of cold shortening. However, there were no significant differences in drip loss, cooking loss and shear force value between hot- and cold boned samples. The samples of hot-boning showed lower Minolta L* value and higher sarcoplasmic protein solubility compared with cold boned samples. These results suggest that the pale color changing of porcine longissimus muscle could be inhibited by hot-boning due to rapid chilling of the muscle although sarcomere length could be shortened because of cold shortening. Also these results show that hot-boning of porcine carcass could have a high protein solubility without negative effects of drip loss or tenderness of porcine longissimus muscle.

• 한국식품영양과학회지
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• 제24권5호
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• pp.811-815
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• 1995

BSA, egg albumin (EA), 그리고 분리대두단백질(SPI)의 Neutrase에 의한 탈아미드화가 용해도에 미치는 영향을 조사하여 보았다. BSA는 탈아미드화로 pH 4~8 사이의 물에 대한 용해도가 천연 BSA에 비하여 98~83%로 감소하였으며, pH 6 부근에서 가장 낮은 용해도를 보았다. 천연 BSA와 탈아미드화된 BSA 모두 0.2M NaCl 용액에서는 100%의 용해도를 보였으나, 산성 1.0M NaCl용액에서는 용해도가 모두 크게 떨어졌다. EA의 용해도는 탈아미드화로 pH3 이하와 6 이상의 수용액에서는 증가하였으나, 산성 NaCl용액에서는 크게 감소하였다. SPI는 탈아미드화로 수용액에서의 용해도가 모든 pH 범위에서 크게 증가하였으나, NaCl용액에 대한 용해도는 pH 6 이상에서는 증가하였고, pH 5 이하에서는 변화가 없었다.

• 한국축산식품학회지
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• 제23권1호
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• pp.63-69
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• 2003

본 연구는 단백질분해효소로 whey protein을 가수분해하여 얻은 가수분해물의 용해도와 유화특성의 변화를 측정하기 위해 실시하였다. Whey protein concentrates를 porcine trypsin(E : S=1 ; 3,000)으로 pH 8.0, 37$^{\circ}C$에서 6시간 동안 가수분해한 whey protein 가수분해물의 유화활성은 분해 4시간째에 가장 높게 나타났으며, 이 때 가수분해도는 5.50%이었다. whey protein의 효소가수분해로 whey protein 중의 $\alpha$-lactalbumin은 분해가 잘 일어나지 않으나 $\beta$-lactoglobulin은 분해 초기부터 급속히 분해되며 유화력 상승에 관여하는 여 러개의 저분자량 peptide를 생성하였다. 가수분해물의 용해도는 가수분해시간이 지남에 따라 증가세를 보이다가 5시간부터 조금씩 감소 추세를 보였으며, pH에 따라서는 등전점 부근인 pH4~5에서 용해도가 가장 낮았으나 가수분해시간이 증가함에 따라 이 부근의 용해도가 현저히 증가하였으며 pH 6이상에서는 pH가 증가함에 따라 용해도도 증가하였다. 유화활성은 용해도의 결과와 거의 비슷한 결과를 나타내었다. 유화 안정성은 분해시간이 지남에 따라 조금씩 증가함을 보여주었으나, 가수분해 4시간부터 pH 8 이상의 PH에서 급격한 증자를 나타내었다.

• 한국식품조리과학회지
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• 제9권4호
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• pp.278-283
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• 1993

This study was attempted to investigate the effects of enzymatic modification of milk protein with protease on functional properties. The selected functional properties were solubility, emulsifying activity (EA), emulsion stability(ES), foam expansion(FE), and foam stability(FS). These properties were measu-red from pH 3.0 to pH 8.0. The proteases used in this study were iaolated from Meju(fermemted soybean) and had specific activity of 250 units/㎎ protein at pH 7.0, 1600 units of pretense was used for 1gr. of skim milk protein. Skim milk showed 30.5％ degree of hydrolysis for 1 hr. and 36.4% degree of hydrolysis for 3.5 hrs. of protease treatment at pH 7.0. Solubility of native skim milk, control, 1 hr. and 3.5 hrs. groups were 3.37, 3.64, 10.21, 14.34％o at pH 4.0 respcetively. The emulsifying activity of native skim milk, control, 1 hr. and 3.5 hrs. groups were 38.8,42.0,43.0,46.7ft at pH 4.0, respectively. Enzymatic modification resulted in the increase of solubility and emulsifying activity at pH 4.0. However at pH 5.0 emulsifying activity of 1 hr. and 3.5 hr. group were lower than native skim milk and control groups. 1 hr. protease treatment was found to be most effective way of increasing foam expansion at pH 4.0 to 6.0. It was supported that, protease treated skim milk can be used to improve solubility, emulsifying activity, foam expansion at acid pH. meju protease. skim milk, solubility, emulsion, foam.