• Asian-Australasian Journal of Animal Sciences
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• v.23 no.5
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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.

• Journal of Ginseng Research
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• v.17 no.3
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• pp.203-209
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• 1993

This study was conducted to investigate the effects of ginseng extracts and their fractions on the 9rowth of Escherichia coli and its glucose consumption. Considerable amount of impurities such as sugar, Protein, lipids and minerals other than saponins were contained in n-butanol extracts which are generally referred to be crude saponins. Sucrose and maltose were contained as major sugars In ginseng extracts and their water soluble fractions. Arginine and potassium were also contained as major amino acid and mineral in those fractions, respectively. Though the glucose consumption and growth of Escherichia coli were enhanced by ginseng extracts and their water soluble fractions those were retarded by ether soluble fractions and n-butanol fractions.

• Food Science and Preservation
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• v.20 no.3
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• pp.435-439
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• 2013

As byproducts of chicken slaughtering, chicken feathers are produced and mostly discarded without proper treatment, which results in serious environment pollution. Therefore, the appropriate treatment and utilization of chicken feathers are needed. In particular, chicken feathers can be used as protein sources for the preparation of protein hydrolysates, considering that chicken feathers have a large amount of proteins. In this study, chicken feather protein hydrolysates were prepared and their iron-binding peptides were isolated. Chicken feather protein was extracted from feathers of slaughtered chicken, and its hydrolysates were prepared via hydrolysis with Flavourzyme for 8 h. Then the chicken feather protein hydrolysates were ultra-filtered to obtain small peptide fractions and fractionated using Q-Sepharose and Sephadex G-15 columns to isolate their iron-binding peptides. Two major fractions were produced from each of the Q-Sepharose ion exchange chromatography and the Sephadex G-15 gel filtration chromatography. Among the fractions, the peptide fraction with a high iron-binding activity level, F12, was isolated. These results suggest that chicken feather protein hydrolysates can be used as iron supplements.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.51 no.4
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• pp.351-361
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• 2018

This study investigated the potential of collagenous protein fractions (CPFs) as functional foods. The specific CPFs studied were recovered from the roe of bastard halibut (BH), Paralichthys olivaceus; skipjack tuna (ST), Katsuwonus pelamis; and yellowfin tuna (YT), Thunnus albacares through the alkaline solubilization process at pH 11 and 12. The buffer capacity, water-holding capacity and solubility of CPFs with pH-shift treatment were significantly better at alkaline pH (10-12) than at acidic pH (2.0). At pH-shift treatment (pH 2 and 12), the foaming capacities of CPFs from ST and YT were improved compared to those of controls, but they were unstable compared to BH CPFs. The emulsifying activity index (EAI, $m^2/g$ protein) of CPFs (controls) was 16.0-21.1 for BH, 20.1-23.9 for ST and 9.3-13.7 for YT (P<0.05). CPFs adjusted to pH 12 showed improved EAI and YT CPFs showed significantly greater emulsifying ability than those from BH and ST. CPFs recovered from fish roe are not only protein sources but also have a wide range of food functionalities, confirming the high availability of fish sausage and surimi-based products as protein or reinforcing materials for functional foods and alternative raw materials.

• Korean Journal of Veterinary Research
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• v.38 no.2
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• pp.328-335
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• 1998

Outer membrane proteins(OMPs) of Brucella abortus 1119-3 strain were extracted by Triton X-100 treatment, and fractionated by DEAE-cellulose column chromatography and Sephacryl S-300 column chromatography. The antigenic proteins in these fractions were identified by Western blot analysis. In Western blot analysis, a single band(38kDa) was observed in the DEAE fractions from 36th fraction to 38th fraction against sera of cattle infected with B abortus. And other fractions have several bands. However, the Sephacryl S-300 fractions exhibited a total of 3 peaks of proteins with a broad range from about 30 to 116kDa. In order to characterize further, the extracted OMPs and the DEAE fractions were analyzed by two dimensional polyacrylamide gel electrophoresis(2-DE) and Western blot using serum from naturally infected cattle with Brucella spp. The 2-DE immunoblots of DEAE fraction showed immunoreactive spots more than twenty two. The major protein spots have ranging from about 32 to 47kDa. The pI values of the spots were detected from pH 4.7 to 5.4. Among the major protein spots, the 38kDa protein which is a specific antigen, located at the point of approximately a pI 4.8.

• Korean Journal of Agricultural Science
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• v.46 no.2
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• pp.369-379
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• 2019

Alzheimer's disease (AD) is the most common neurodegenerative disease associated with age, and amyloid beta ($A{\beta}$) is known to cause Alzheimer's disease. In the present study, we investigated the protective effects of Cirsium japonicum var. maackii extract and its fractions against $A{\beta}$-induced neurotoxicity in C6 glial cells. The cells treated with $A{\beta}_{25-35}$ showed a decrease in cell viability and an increase in reactive oxygen species (ROS) production compared with the non-treated cells. However, the cells treated with the C. japonicum var. maackii extract and its fractions increased the cell viability and inhibited the $A{\beta}$-induced ROS production. These results demonstrate the neuroprotective effects of C. japonicum var. maackii against $A{\beta}$. To further examine the protective mechanism, we measured inflammation and apoptosis related protein expressions. The cells treated with extract and fractions from C. japonicum var. maackii down-regulated inflammatory related proteins such as cyclooxygenase-2, interleukin $(IL)-1{\beta}$, and IL-6, and attenuated apoptosis related proteins including B-cell lymphoma-2 (Bcl-2) associated X protein/Bcl-2 ratio. In particular, the ethanol and ethylacetate fraction exhibited higher inhibitory effect against ROS production and apoptosis-related protein expressions among the extract and the other fractions. Therefore, this study demonstrated the protective effects of C. japonicum var. maackii extract and its fractions against $A{\beta}$-induced neurotoxicity in C6 glial cells through the regulation of oxidative stress, inflammation, and apoptosis, suggesting that it might have potential as a therapeutic for AD.

• Korean Journal of Microbiology
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• v.19 no.2
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• pp.52-62
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• 1981

In order to interpret the effect of IAA on the phosphate metabolism and biosynthesis of organic compounds, Saccharomyces uvarum were cultured in the media treated with various concnetration of IAA $(10^{-3}M,\;10^{-5}M,\;10^{-7}M)$. Sampling at the beginning and intervals of culture, yeast cells fractionated were traced the contents of inorganic phosphate and organic compounds of various fractions. 1. Growth of Saccharomyces uvarum were enhanced by IAA $(10^{-3}M,\;10^{-5}M)$ and phosphate contents in DNA and RNA fractions treated with IAA were accelerated 2.3 times and 2 times in comparison with those of control. 2. Amounts of poly-P"A" and poly-p"B" were increased but poly-P"C" decreased during the culture. Therefore, it is considered that poly-P"C" play on most important role as a phosphate pool. 3. It is suggested that because phosphate contents in DNA, protein and lipid fractions increased, inorganic phosphates required phosphates required RNA were transferred from phosphates in cytoplasm, because these increased slowly during the culture. 4. Alkali-labile protein were accelerated by IAA and alkali stable protein only were inhibiction were enhanced by IAA while, ethanol : ether soluble fraction was induced by $10^{-7}M$ IAA in comparison with those control.X> IAA in comparison with those control.

• Applied Biological Chemistry
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• v.20 no.1
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• pp.156-170
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• 1977

Some of the recent developments and studies in the area of rice protein are reviewed. Protein content and amino acid composition of rice are briefly described. Emphasis is given to characterization of rice protein fractions, effects of protein content on grain properties and lysine content of rice, occurence of protein in rice grain and biosynthesis of protein during grain development.

• Korean Journal of Veterinary Research
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• v.14 no.1
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• pp.29-31
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• 1974

The total serum protein, protein fractions by paper electrophoresis and A/G ratio in pregnant rabbits were observed. The results obtained in this work were sumrnerized as follows: 1. Total serum protein and the fraction of serum albumin revealed a decrease with the advancing of gestation, especially total serum protein was decreased significantly on 3 weeks of pregnancy. There was a tendency to return tward control level on one week after delivery. 2. The fraction of ${\alpha}_1$, and ${\alpha}_2$-globulin showed little changes during the period of gestation. 3. The fraction of ${\beta}$-globulin was increased more or less during the period of gestation, and on one week after delivery showed considerable increase but the increase was statistically insignificant. 4. The fraction of ${\gamma}$-globulin revealed a variable changes during pregnancy but there was no significant differences. 5. A/G ratio was significantly decreased at 3 weeks of pregnancy and the ratio was near control level on one week after delivery.

• Korean Journal of Pharmacognosy
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• v.39 no.3
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• pp.249-254
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• 2008

An 80% EtOH extract and the solvent fractions of the seeds of Cornus officinalis were evaluated for their inhibitory activities against advanced glycation end products (AGEs) formation and AGEs-induced protein cross-linking in vitro. In vitro assay for AGEs-bovine serum albumin (BSA) formation showed that the 80% EtOH extract, n-hexane, EtOAc, n-BuOH and water fractions significantly inhibited AGEs formation with observed $IC_{50}$ values of 1.13, 17.64, 1.52, 1.24 and $3.27{\mu}g/ml$, respectively. In indirect AGEs-ELISA assay, the 800% EtOH extract, EtOAc and n-BuOH fractions exhibited more potent inhibitory activity on AGEs-BSA formation than aminoguanidine, a well know AGEs inhibitor. Furthermore, the 80% EtOH extract and all the solvent fractions inhibited concentration-dependently AGE-BSA cross-linking to collagen. The 80% EtOH extract, EtOAc, n-BuOH and water fractions also had a breaking activity against preformed AGE-BSA cross-linking concentration dependently. Thus these results suggest that the 80% EtOH extract and fractions of the seeds of C. officinalis could be an inhibitor as well as breaker of AGE-BSA cross-linking.