• The Korean Journal of Food And Nutrition
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• v.25 no.3
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• pp.644-649
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• 2012

The edible barnyard millets(Echinochloa spp.) which have essentially vanished in the farmhouses environment and in agricultural germplasm were evaluated with the aim of restoration as a crop. The proximate components and mineral elements of milled millet were nutritionally similar or better than brown rice, and the vitamin contents of $B_1$ and $B_2$ exceeded those of rice by 1.3 times and 2.3 times, respectively. ${\beta}$-Carotene which is absent from brown rice was detected at levels ranging from 15~31 ${\mu}g$ in millet samples. Nine essential amino acids, including histidine and arginine and eight non-essential amino acids, such as aspartic acid were detected. The sum of all amino acids was determined to be IEC518>525>510 in the range of 69~106 mg/g. Analysis of physiological active substances via their electron donating ability(EDA) revealed values ranging from 3.4~8.2%, with the total polyphenol component being 51.1~69.4 mg/g and ${\alpha}$-glucosidase inhibition ability determined as 8.3~10.9%. In terms of agronomical characteristics and yields of barnyard millet, three millet varieties(IEC510, 518, and 525) were suitable as edible crops. IEC525 was selected as optimum variety for cultivation on the basis of nutritional ingredients, physiological active substances, and yield.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.20 no.1
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• pp.41-51
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• 1987

This study was carried out to prepare powdered smoked-dried mackerel which can be used as a soup base, and to examine storage stability and the taste compounds of Products. Raw mackerel are filleted, toiled for 10 minutes and pressed to remove lipids, and then soaked in extract solution of skipjack meat. This soaked mackerel are smoked 3 times to $10-12\%$ moisture content at $80^{\circ}C$ for 8 hours. And the smoked-dried mackerel were pulverized to 50 mesh. Finally, the powdered smoked-dried mackerel were packed in a laminated film $bag(PET/Al\;foil/CPP:\;5{\mu}m/15{\mu}m/70{\mu}m,\;15\times17cm)$ with air(product C), nitrogen(product N) and oxygen absorber(product O), and then stored at room temperature for 100 days. The moisture and crude lipid content of powdered smoked-dried mackerel was $11.3-12.3\%,\;12\%$, respectively, and water activity is 0.52-0.56. And these values showed little changes during storage. The pH, VBN and amino nitrogen content increased slowly during storage. Hydrophilic and lipophilic brown pigment formation showed a tendency of increase in product(C) and showed little change in product(N) and (O). The TBA value, peroxide value and carbonyl value of product(N) and (O) were lower than those of product (C). The major fatty acids of products were 16:0, 18:1, 22:6, 18:0 and 20:5, and polyenoic acids decreased, while saturated and monoenoic acids increased during processing and storage of products. The IMP content in products were 420.2-454.2 mg/100 g and decreased slightly with storage period. And major non-volatile organic acids in products were lactic acid, succinic acid and $\alpha-ketoglutaric$ acid. In free amino acids and related compounds, major ones are histidine, alanine, hydroxyproline, lysine, glutamic acid and anserine, which occupied $80.8\%$ of total free amino acids. The taste compounds of powdered smoked-dried mackerel were free amino acids and related compounds (1,279.4 mg/100 g), non-volatile organic acids(948.1 mg/100 g), nucleotides and their related compounds (672.8 mg/100 g), total creatinine(430.4 ntg/100 g), tetaine(86.6 mg/100 g) and small amount of TMAO. The extraction condition of powdered smoked-dried mackerel in preparing soup stock is appropriate at $100^{\circ}C$ for 1 minute. Judging from the results of taste and sensory evaluation, it is concluded that the powdered smoked-dried mackerel can be used as natural flavoring substance in preparing soups and broth.

• Animal cells and systems
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• v.4 no.2
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• pp.157-163
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• 2000

Yeast pheromone a-factor is a 13-amino acid peptide hormone that is synthesized as a part of a larger precursor, prepro-$\alpha$-factor, consisting of a signal peptide and a proregion of 64 amino acids. The carboxy-terminal half of the precursor contains four tandem copies of mature $\alpha$-factor. To investigate the molecular basis of intracellular sorting, proteolytic processing, and storage of the peptide hormone, yeast prepro-$\alpha$-factor precursors were heterologously expressed in rat pituitary $GH_3 cells. When cells harboring the precursor were metabolically labeled, a species of approximately 27 kD appeared inside the cells. Digestion with peptide: N-glycosidase F (PNG-F) shifted the molecular mass to a 19 kD, suggesting that the 27 kD protein was the glycosylated form as in yeast cells. The nascent polypeptide is efficiently targeted to the ER in the $GH_3 cells, where it undergoes cleavage of its signal peptide and core glycosylation to generate glycosylated pro-a-factor. To look at the post ER intracellular processing, the pulse-labelled cells were chased up to 2 hrs. The nascent propeptides disappeared from the cells at a half life of 30 min and only 10-25% of the newly synthesized, unprocessed precursors were stored intracellularly after the 2 h chase. However, about 20% of the pulse-labeled pro-$\alpha$-factor precursors were secreted into the medium in the pro-hormone form. With increasing chase time, the intracellular level of propeptide decreased, but the amount of secreted propeptide could not account for the disappearance of intracellular propeptide completely. This disappearance was insensitive to lysosomotropic agents, but was inhibited at $16^{circ}C or 20^{\circ}C$, suggesting that the turnover of the precursors was not occurring in the secretory pathway to trans Golgi network (TGN) or dependent on acidic compartments. From these results, it is concluded that a pan of these heterologous precursors may be processed at its paired dibasic sites by prohormone processing enzymes located in TGN/secretpry vesicles producing small peptides, and that the residual unprocessed precursors may be secreted into the medium rather than degraded intracellularly.

• The Korean Journal of Food And Nutrition
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• v.23 no.4
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• pp.516-525
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• 2010

Flaxseed has recently gained attention as a functional food. In this paper, physicochemical analyses of flaxseed and its oil were performed. Crude fat content ranged from 37~43%, moisture 0.2~6.8%, carbohydrate 30~35%, crude protein 18~23%, and crude ash 3~4%. Flaxseed is also an important source of dietary fiber. The TDF(total dietary fiber) contents of the flaxseed samples were 28~31%, and the SDF(souble dietary fiber) content of roasted flaxseeds was higher than that of raw flaxseeds. The major minerals found in flaxseed were calcium, potassium, magnesium, and phosphate. The flaxseeds were rich in ${\gamma}$-tocopherol with 234.3 mg/kg in raw brown flaxseed and 134.1 mg/kg in raw gold flaxseed, respectively. Roasted flaxseeds showed slightly lower vitamin and amino acid contents than those of the raw samples. The iodine, saponification, and acid values of brown flaxseed oil were 204.1 g/100 g, 193.6 mg/g, and 1.59 mg/g, and for gold flaxseed oil were 203.0 g/100 g, 189.9 mg/g, and 2.35 mg/g, respectively. ${\alpha}$-Linolenic acid(ALA, C18:3n-3) was highly concentrated in the flaxseed oil, which constituted about 55.5~56.1% of total fatty acids. Thus, flaxseed oil is a good source of omega-3 fatty acids and beneficial for the heart. Flaxseed contains high levels of dietary fiber including lignans, as well as minerals and vitamins, which may have antioxidant actions and help protect against certain cancers.

• Food Science and Preservation
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• v.24 no.2
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• pp.187-195
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• 2017

This study evaluated quality characteristics of soybean fermented by selected lactic acid bacteria, which were the enzyme strains with high antimicrobial activities isolated from traditionally prepared soybean paste. We determined total aerobic and lactic acid bacteria counts, protease and amylase activities, reducing sugar and amino-type nitrogen contents, and the amounts of amino acids, organic acids, and aroma-compounds. The total aerobic bacteria counts in soybean fermented with strain I13 ($7.75{\times}10^9CFU/mL$) were the highest among all the strains analyzed. Lactic acid bacteria numbers were $2.85{\times}10^9$ to $4.35{\times}10^9CFU/mL$ in soybean fermented with isolates. Amylase and protease activities of the JSB22 sample were the highest among all sample. Reducing sugar and amino-type nitrogen contents of soybean fermented with JSB22 (1.23%, 94.52 mg%) were highest. Total amino acid content of the samples was 15.88-17.62%, and glutamic acid, aspartic acid, leucine, lysine, and arginine were the major amino acids. Lactic acid (0.82-3.65 g/100 g), oxalic acid (22.74-63.57 mg/100 g), and fumaric acid (2.88-6.33 mg/100 g) were predominant organic acids. A total of 39 volatile aroma-compounds were identified, including 2 esters, 5 ketones, 7 alcohols, 14 hydrocarbons, 2 heterocyclic compounds, 4 acids, and 5 miscellaneous compounds. These results represent useful information for the development of a starter (single or complex) and will be used for production of functional fermented soybean foods.

• Journal of Life Science
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• v.15 no.5 s.72
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• pp.734-738
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• 2005

A gene coding for xylanase from alkali-tolerant Bacillus alcalophilus AX2000 was cloned into Escherichia coli $DH5\alpha$ using pUC19. Among 2,000 transformants, one transformant showed clear zone on the detection agar plate containing oat-spells xylan. Its recombinant plasmid, named pXTY99, was found to carry 7.0 kb insert DNA fragment. When the nucleotide sequence of the cloned xylanase gene (xynT) was determined, xynT gene was found to consist of 1,020 base-pair open reading frame coding for a poly-peptide of 340 amino acids with a deduced molecular weight of 40 kDa. The coding sequence was preceded by a putative ribosome binding site, and the transcription initiation signals. The deduced amino acid sequence of xylanase is similar to those of the xylanases from Bacillus sp. Nl37 and B. stearothermophilus 21 with $61\%$ and $59\%$ identical residues, respectively.

• BMB Reports
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• v.32 no.5
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• pp.480-485
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• 1999

Tyrosine phenol-lyase of thermophilic Symbiobacterium sp. SC-1, which is obligately and symbiotically dependent on thermophilic Bacillus sp. SK-1, was purified and characterized. The enzyme is composed of four identical subunits and contains approximately 1 mol of pyridoxal 5'-phosphate (PLP) per mol subunit as a cofactor. The enzyme showed absorption maxima at 330 and 420 nm, and lost this absorption profile by treatment with phenylhydrazine. The apparent dissociation constsnt, $K'_D$, for PLP was determined with the apoenzyme to be about $1.2\;{\mu}M$. The isoelectric point was 4.9. The optimal temperature and pH for the $\alpha,\beta$-elimination of L-tyrosine were found to be $80^{\circ}C$ and pH 8.0, respectively. The substrate specificity of the enzyme was very broad: L-amino acids including L-tyrosine, 3,4-dihydroxyphenyl-L-alanine (L-DOPA), L-cysteine, L-serine, S-methyl-L-cysteine, $\beta$-chloro-L-alanine, and S-(o-nitrophenyl)-L-cysteine all served as substrates. D-Tyrosine and D-serine were also decomposed into pyruvic acid and ammonia at rates of 7% and 31% relative to their corresponding L-enantiomers, respectively. D-Alanine, which was inert as a substrate in a, $\beta$-elimination, was the only D-amino acid racemized by the enzyme. The $K_m$ values for L-tyrosine, L-DOPA, S-(o-nitrophenyl)-L-cysteine, $\beta$-chloro-L-alanine, and S-methyl-L-cysteine were 0.19, 9.9, 0.36, 12, and 5.5 mM, respectively.

• Journal of Microbiology and Biotechnology
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• v.14 no.6
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• pp.1343-1349
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• 2004

A native strain of Pasteurella multocida was isolated from pigs suffering from severe atrophic rhinitis at domestic farms in Gyeonggi Province, Korea, and was identified as capsular serogroup 'D' and somatic serotype '4' by disc diffusion decapsulation and gel diffusion precipitation tests, respectively. The P. multocida (D:4) induced atrophic rhinitis in healthy pigs by the secondary infection. The gene for outer membrane protein H (ompH) of P. multocida (D:4) was cloned in Escherichia coli DH5$\alpha$ by PCR. The open reading frame of the ompH was composed of 1,023 bp, possibly encoding a protein with 341 amino acid residues containing a signal peptide of 20 amino acids at N-terminus, and the gene product with molecular mass of ca. 38 kDa was identified by SDS-PAGE. Hydropathy profiles indicated that there are two variable domains in the OmpH. To express the ompH in E. coli, the gene was manipulated in various ways. Expression of the truncated as well as full-length forms of the recombinant OmpH was fatal to the host E. coli BL21 (DE3). However, the truncated OmpH fused with GST was consecutively expressed in E. coli DH5$\alpha$. A large quantity of the fused polypeptide was purified through GST-affinity chromatography.

• Plant Resources
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• v.1 no.2
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• pp.113-120
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• 1998

Soybean is an important crop because its seed has very high protein relative to others. The quality of soy protein is limited by the concentration of the sulfur-containing amino acids in the amino acid profile. Among the supply of various forms of 0.4mM sulfur as S nutrition during seed fill. only 0.4mM L-methionine can inhibit ${\beta}$-subunit synthesis completely and produce the highest glycinin-containing seeds. Compared to 0.4mM sulfate control, seeds supplied by 0.4mM L-methionine have lower ${\alpha}$-, no ${\beta}$-subunit, and highly increased glycinin without altering total protein concentration. Supply of 0.2mM cystine (0.4mM S) did not affect the accumulative pattern of seed storage protein (SSP) subunits. In the supply of L-methionine, 0.2mM treatment showed higher glycinin in seeds but 0.05mM resulted in lower glycinin than tile sulfate control. The relative abundance of ${\alpha}^`$-subunit was not altered by any N or S nutrition. Under 5mM nitrogen, protein concentration was increased about 3-5% by substituting ammonia for nitrate during seed fill independent of nutrition. The increase resulted in the only increase of 7S protein, mainly ${\beta}$-subunit. Our data suggest that the regulatory system of SSP genes responds to the balance between N and S assimilates supplied from mother plant. and controls the di fferential synthesis of their subunits for the maximum protein accumulation in developing soybean seed.

• Food Science and Biotechnology
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• v.16 no.6
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• pp.1006-1010
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• 2007

This study investigated changes in the chemical and functional components of germinated rough rice for the development of functional foods. The chemical components that were determined for 'Ilpum', 'Goami2', 'Keunnun', and 'Heugkwang' rough rice cultivars included dietary fiber, free sugars, free amino acids, and functional components such as tocopherols and ${\gamma}$-oryzanol. The crude protein, fat, total dietary fiber, and free sugar contents of the rough rice increased significantly after germination. The essential amino acid content was particularly increased. After the germination of the 'Ilpum', 'Goami2', 'Keunnun', and 'Heugkwang' varieties, the following increases were found: ${\gamma}$-aminobutyric acid increased 2.4, 2.5, 6.1, and 3.4 times, respectively; ${\alpha}$-tocopherol, ${\alpha}$-tocotrienols, and ${\gamma}$-tocotrienols increased significantly; and ${\gamma}$-oryzanol content increased 0.8, 1.1, 1.5, and 1.2 times, respectively. Thus, germinated rough rice has the potential to be used as a healthy and functional food ingredient.