• 한국식품영양학회지
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• 제25권3호
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• pp.612-619
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• 2012

This study was conducted to investigate the physicochemical properties of the ethanol extracts and soluble dietary fiber from Cassia tora L. seed. The proximate composition of Cassia tora, soluble solid contents, color intensity and contents of emodin and rhein of Cassia tora extract, molecular mass distribution, sugar contents and viscosity of soluble fiber from Cassia tora were analyzed. Cassia tora contains 12.6% of moisture, 5.2% of ash, 13.4% of crude protein, 7.2% of crude fat, 8.8% of insoluble fiber and 48.3% of soluble fiber. The effects of extract condition on soluble solid contents, color intensity and contents of emodin and rhein of Cassia tora extract were investigated. The soluble solid contents were higher in 70% or 50% ethanol extracts than those in 100% ethanol extracts and showed highest value in grind sample extracts. In Hunter's color value, 100% ethanol extracts and whole Cassia tora sample extracts were higher in L and b value, but on the contrary, were lower in a value, than those of the other. The highest emodin and rhein contents were observed in 70% and 50% ethanol extracts, respectively, and showed higher value in room temperature extracts than in heating extracts. The molecular mass of soluble fiber from Cassia tora seed was estimated by gel filtration chromatography. Most soluble fiber(80%) exhibited a molecular mass range of between 50~2000 kDa. The major sugars of soluble fiber from Cassia tora seed were identified as xylose, mannose and galactose. The apparent viscosity of 0.5% soluble fiber from Cassia tora seed was 33 mPas showing a higher value than pectin or xanthan gum.

• 동아시아식생활학회지
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• 제19권1호
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• pp.45-51
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• 2009

In this study, food protein hydrolysates were prepared from six types of food protein: purified meat protein, whole egg protein, casein, isolated soy protein, concentrated rice protein, and gluten. Food proteins were hydrolyzed with pepsin and ethanol (80%)-soluble fractions of pepsin hydrolysates were employed for analysis. The products were colorless and odorless powders with low fat content and good solubility. The MW (molecular weight) of the protein hydrolysates was confirmed to be $200{\sim}1,800$ via gel filtration. Free amino acid contents accounted for less than 5% of the samples. The results of our amino acid analysis revealed that all food protein hydrolysates preserved their original amino acid compositions and nutritional values of their source proteins with highly pure oligopeptide mixtures. These results show that the food protein hydrolysates prepared in these investigations should prove excellent dietary nitrogen sources for a variety of applications.

• Asian-Australasian Journal of Animal Sciences
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• 제23권5호
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• pp.598-606
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• 2010

This study investigated the nutritional quality of soybean meal (SBM) fermented by Aspergillus ($FSBM_A$) and/or followed by Lactobacillus fermentation ($FSBM_{A+L}$). Both fermented products significantly improved protein utilization of SBM with higher trichloroacetic acid (TCA) soluble true protein content, in vitro protein digestibility and available lysine content, especially in $FSBM_{A+L}$. Moreover, $FSBM_{A+L}$ produced a huge amount of lactic acid resulting in lower pH as compared to the unfermented SBM or soybean protein concentrate (SPC) (p<0.05). $FSBM_A$ and $FSBM_{A+L}$ raised 4.14% and 9.04% of essential amino acids and 5.38% and 9.37% of non-essential amino acids content, respectively. The ${\alpha}$-galactoside linkage oligosaccharides such as raffinose and stachyose content in $FSBM_A$ and $FSBM_{A+L}$ decreased significantly. The results of soluble protein fractions and distribution showed that the ratio of small protein fractions (<16 kDa) were 42.6% and 63.5% for $FSBM_A$ and $FSBM_{A+L}$, respectively, as compared to 7.2% for SBM, where the ratio of large size fractions (>55 kDa, mainly ${\beta}$-conglycinin) decreased to 9.4%, 5.4% and increased to 38.8%, respectively. There were no significant differences in ileal protein digestibility regardless of treatment groups. SPC inclusion in the diet showed a better protein digestibility than the SBM diet. In summary, soybean meal fermented by Aspergillus, especially through the consequent Lactobacillus fermentation, could increase the nutritional value as compared with unfermented SBM and is compatible with SPC.

• 한국식품과학회지
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• 제26권5호
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• pp.603-608
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• 1994

대두식품의 가공 및 발효에 따른 phytate 함량의 변화, 그 함량이 pepsin과 pancreatin에 의한 단백질 소화에 미치는 영향, 그리고 전기영동법에 의한 단백질 분획의 변화를 조사하였다. 황색콩의 phytate 함량은 2.4%이었고 가공 및 발효에 따라 감소하여 두유 0.2%, 두부 0.7%, 비지 0.4%로, 청국장 0.9%, 메주 1.4%, 간장 0.2%, 된장 1.0%로 나타났다. Phytate/protein 비율은 pepsin에 의한 단백질 소화율과 상관성이 없었으나 pancreatin에 의한 단백질 소화율과는 부(負)의 상관관계를 나타냈다(p<0.01, r= -0.73). 전기영동 결과 콩을 물에 불리면 수용성 분획이 변화되었고 두유 제조시 비지에는 주로 저분자량 밴드들이 새로이 나타났다. 발효 과정에서는 단백질이 분해되어 밴드가 거의 나타나지 않았다.

• 한국미생물·생명공학회지
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• 제23권3호
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• pp.316-321
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• 1995

Some properties of $\beta$-1, 3-glucan synthase system in Saccharamyces cerevisiae were investigated. By extraction with detergent and salt, the membrane preparations could be dissociated into two components, one soluble, the other still membrane bound. Both components, in addition to GTP, were necessary for the activity of $\beta$-1, 3-glucan synthase like other fungi. The protective effect of guanosine nucleotides on the soluble factor pointed to the possibility that this fraction contained a GTP-binding protein. Addition of increasing amounts of soluble factor to a constant amount of insoluble catalytic factor, vice versa, gave rise to a saturation curve. These results, including different types of evidence, indicate that the soluble factor and the catalytic factor form a complex.

• Animal Systematics, Evolution and Diversity
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• 제19권2호
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• pp.217-225
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• 2003

한국산 초파리과의 계통학적 연구의 일환으로, 초파리아속에 속하는 10종을 대상으로 동위효소와 수용성 단백질 분석을 실시하였다. 동위효소와 수용성 단백질 분석결과 D.(D.) angularis와 D.(D.) brachynephros가 유전학적으로 가장 가까운 종이었으며, D.(D.) curvispina와 D.(D.) tsigana 사이는 유전적 거리가 가장 먼 종으로 분석되었다. 그리고. 초파리아속 10종은 D.(D.) virilis, D. (D.) tsigana, D. (D.) lacertosa의 제1군과 D. (D.) angularis와 D. (D.) hrachynephros, D. (D.) unispina와 D. (D.) curvispina, D. (D.) takadai와 D. (D.) kuntzei. 그리고 D (D.) nigromaculata의 4개의 아군으로 이루어진 제 2군으로 나눌 수 있다.

• 한국식품과학회지
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• 제31권1호
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• pp.62-67
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• 1999

과요오드산 산화 가용성전분 및 말토올리고당을 고구마 ${\beta}-amylase$, 밀 ${\beta}-amylase$, aldolase, bovine serum albumin, catalase, carboxypeptidase, ferritin, pronase와 반응시켜서 전기영동하였다. 이들 단백질은 전기영동상의 이동도가 달라지고, 단백질 밴드와 같은 위치에서 PAS 염색 밴드를 나타내어 당이 부가된 것으로 확인되었다. 당의 부가는 과요오드산 산화당의 알데히드기가 단백질 분자 표면 리신의 ${\varepsilon}-NH_2$기와 Schiff 염기를 형성하여 일어난다. 변형효소는 자외흡광곡선에 변화를 나타내지 않았다.

• 한국식품영양과학회지
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• 제27권3호
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• pp.448-454
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• 1998

Meju for doenjang and kochujang was prepared as a model at Sunchang areaand monitored with major changes. Kochujang meju was prepared on September 12 and doenjang meju on November 12, 1995. Kochjang meju was found to be naturally fermented at 80~90% RH, 15~2$0^{\circ}C$ and doenjang meju was at 80~90% RH and 0~5$^{\circ}C$. The shapes of kochujang meju and doenjang meju were doughnut-type and rectangular, respectively. Weight losses during fermentation were 48% and 28%, respectively. The pH drop and acip production of kochujang meju were negligible. However, pH of doenjang meju decreased from 6.29 to 5.88 and acidity increased from 0.08 to 0.23% as lactic acid. Protein in meju was found to be rapidly solubilized during the early stage of fermentation. Soluble protein cotents of kochujang meju after 7 days and 60 days were 8.23%, respectively. The doenjang mejus were 2.15% after 20 days and 5.72% after 60 days. Soluble suger content increased with the fermentation time. The soluble sugar content was higher in kochjang meju. Acidic protease was highly produced during meju fermentation. $\alpha$-Amylase and $\beta$-amylase were detected in the kochujang meju, of which glutinous rice consisted, but negligible in doenjang meju. Lipase was detected in kochujang meju, but was, negligible in doenjang meju. Microbial population increased drastically after 7 days of fermentation in kochujang meju and 20 days of fermentation in doenjang meju.

• 한국식물병리학회지
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• 제10권4호
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• pp.305-313
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• 1994

Typically susceptible lesions were developed on pepper (cv. Hanbyul) leaves inoculated with the compatible strains Ds 1 of Xanthomonas campestris pv. vesicatoria. The lesions appeared first water-soaked and then turned yellow with a chlorotic area. In contrast, the leaves inoculated with the incompatible strain 81-23 initially turned yellow and then developed local necrosis. Multiplication of x. c. pv. vesicatoria in pepper leaves also were distinctly different between the two strains. The strain Ds 1 multiplied more greatly than did the strain 81-23 in the infected leaves. X. c. pv. vesicatoria infection of pepper leaves induced the synthesis of soluble proteins, especially more greatly in the compatible than in the incompatible interactions. Some pathogenesis-related (PR) proteins were detected in the intercellular washing fluid (IWF) and extracts of the infected pepper leaves. In particular, the 32 kDa protein on SDS-PAGE gels appeared intensely in the incompatible interaction. In contrast, some proteins with moluecular masses of 65, 71, and 75 kDa disappeared in the infected pepper leaves. Isoelectric focusing could identify the pIs of soluble proteins in infected pepper leaves. The accumulation of the IWF from infected leaves was more conspicuous in the incompatible than the compatible interaction. These results suggest that some extremely acidic and basic proteins were induced and accumulated in the intercellular spaces of infected pepper leaves.

• KSBB Journal
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• 제14권4호
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• pp.429-433
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• 1999

$\beta$-Glucosidaes from Cellvibrio gilvus(CG) was successfully overproduced in soluble form in E. coli with the coexpression of GroEL/ES/. Without the GroEL/ES protein, the $\beta$-glucosidase overexpressed in E. coli constituted a huge amount(80%) of total cellular protein, but was localized in the insoluble fraction, and little activity was detected in the soluble fraction. Coexpression of the E. coli GroEL/ES had a drastic impact on the proper folding of the $\beta$-glucosidase; 20% of the overexpressed enzyme was recovered in the soluble fraction in active form. Similar effects of GroEL/ES were also observed on the overexpressed $\beta$-glucosidase from Agrobacterium tumefaciens(AT). And pET28(a)-RGRAR, partially deleted mutant lacking 5-amino acid residues at carboxy teminus also could be folded into an active form when expressed with the molecular chaperonin GroEL/ES, and its activity was higher than that of the without GroEL/ES system, In addition, the synergistic effect of GroEL/ES and the low induction temperature were important factors for solubilization of the inclusion body from overproduced $\beta$-glucosidases.