• Korean Journal of Veterinary Research
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• v.13 no.1
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• pp.17-21
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• 1973

Free amino acid extracts of musculus brachiocephalicus and musculus glutaeus of cattle, swine, goats and rabbits are analyzed to see the composition and the contents of free amino acids by thin layer chromatography and automatic amino acid analyzer. The results obtained are summarized as follows: 1. Meats of cattle, swine, goats and rabbits analyzed by thin layer chromatography have 6 kinds of free amino acids such as glycine, histidine, methionine, lysine, alanine and leucine, and the spots of glycine in chromatogram of meats of cattle, swine and goats and the ones of methionine in chromatogram of meats of rabbits are the largest and the most denes of all other ones. 2. Distribution curves of free amino acids in meats of cattle, swine, goats and rabbits showed significant differences, but differences on distribution curves of free amino acids between musculus-brachiocephalicus and musculus glutaeus of the same tested animal are not significant. 3. Contents of free amino acids in meats of cattle, swine, goats and rabbits showed significant differences, but differences on contents of free amino acids between musculus brachiocephalicus and musculus glutaeus of the same tested animal are not significant.

• Journal of the Korean Society of Tobacco Science
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• v.32 no.2
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• pp.70-76
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• 2010

A simple and sensitive automatic amino acid analyzer method for the determination of free amino acids in tobacco was described. Sample preparation consisted of a single step of extraction with 0.1 mol HCl at ambient temperature in 60 min by sonication, followed by filtration of an aliquot. Automated amino acid analyzer was used to construct a post-column ninhydrin reaction unit to monitor amino acids separated by liquid chromatography using a series of eluting buffers. By optimization of sample preparation, separation of 19 amino acids was achieved. Limits of quantitation was 0.01 mg/g, coefficients of variation ranged from 0.5 % to 8.9 % and recoveries range from 85 % to 106 %. The method was applied to the analysis of amino acids contents of tobacco leaves in different varieties.

• YAKHAK HOEJI
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• v.28 no.1
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• pp.21-23
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• 1984

High performance amino acid analyzing method has been developed for the routine analysis of taurine in preparations. Ion-exchange resin #2619 Hitachi Custom Ion-Exchange Resin, $2.6(I.D.){\times}150$(length)mm was used as column, buffer I, pH 3.3 as mobile phase. The retention time of taurine was 7 minutes. Calibration curve by peak height for standard taurine was linear from 2.5ppm to 25ppm. The reproducibility showed relative standard deviation $\pm$1.9% when analyzed 10 times for standard solution. The samples could be continuously analyzed without regenerating the resin between samples. Five samples were applied to column every 12 min. and then the resin was regenerated for 30 min. during one analyzing cycle time, 90 min. The automatic amino acid analyzer has made it possible to assay multiple samples in a relatively short period of time using the analytical magnetic program card. The high sensitivity and specificity of the analytical column of the automatic amino acid analyzer permits the routine analysis of taurine in preparations.

• Journal of the Korean Society of Food Science and Nutrition
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• v.21 no.3
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• pp.286-290
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• 1992

From the leaves of Allium tuberosum (Liliaceae), . the purine nucleoside, adenosine was isolated and its structure was characterized on the basis of spectral data. Besides this nucleoside, the composition and relative content of free amino acids and related compounds, compared to standards determined under identical conditions was also investigated using automatic amino acid analyzer. Major free amino acids were alanine, glutamic acid, aspartic acid and valine.

• Preventive Nutrition and Food Science
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• v.19 no.3
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• pp.220-226
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• 2014

In the present report, the effects of blanching, steaming, and high temperature/high pressure processing (HTHP) on the amino acid contents of commonly consumed Korean root vegetables, leaf vegetables, and pulses were evaluated using an Automatic Amino Acid Analyzer. The total amino acid content of the samples tested was between 3.38 g/100 g dry weight (DW) and 21.32 g/100 g DW in raw vegetables and between 29.36 g/100 g DW and 30.55 g/100 g DW in raw pulses. With HTHP, we observed significant decreases in the lysine and arginine contents of vegetables and the lysine, arginine, and cysteine contents of pulses. Moreover, the amino acid contents of blanched vegetables and steamed pulses were more similar than the amino acid contents of the HTHP vegetables and HTHP pulses. Interestingly, lysine, arginine, and cysteine were more sensitive to HTHP than the other amino acids. Partial Least Squares-Discriminate Analyses were also performed to discriminate the clusters and patterns of amino acids.

• Korean journal of food and cookery science
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• v.23 no.1 s.97
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• pp.150-155
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• 2007

This work was conducted to obtain a rapid, accurate, and precise procedure for free amino acids analysis in Doenjang with HPLC-OPA (high performance liquid chromatography using-phthalaldehyde) and AAA (automatic amino acid analyzer) methods. Different sample extraction procedures among water, 0.1 M perchloric acid, and 0.1% meta-phosphoric acid were also compared. The optimal extraction solvent was 0.1% meta-phosphoric acid for both the HPLC-OPA and AAA methods. Good recoveries for glycine and methionine were observed using the 0.1% meta-phosphoric acid extraction with HPLC-OPA method. Method precisions (% relative standard deviation) for the free amino acids ranged for 1.62% to 8.27%, in which the HPLC-OPA method with water extraction showed the lowest value at 1.62%. Inhibition rates of the free amino acids in Doenjang were greatest with an addition of NaCI at a 1% concentration.

• Korean Journal of Food Science and Technology
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• v.5 no.2
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• pp.71-77
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• 1973

The results, which was analytically surveyed the free amino acids by the automatic amino acid analyzer adding the enzyme on the Korean cow's fore shank muscles, are as follows: 1. The content of free amino acids in the fore shank muscles, without addition of the enzyme orderly contains alanine, glutamic acid, lysine, glycine, histidine, leucine, threonine, arginine, cystine, serine, proline, isoleucine, phenylalanine, tyrosine, methionine, aspartic acid and valine. 2. In accordance with the addition of the enzyme, by 0.01%, 0.05% and 0.1% the nine free amino acids of glutamic acid, glycine, alanine, cystine, valine, isoleucine, leucine, lysine and arginine were continuosly increased. 3. Proline and histidine were decreased at the enzyme addition of 0.01% after showing the high content at the control, but the quantity of free amino acids was increased according to the increase of the quantity of the enzyme. 4. Aspartic acid, threonine, serine, methionine, tyrosine and phenylalanine were increased till the enzyme addition of 0.05% and remarkably decreased from 0.1%. 5. At cooking the meat, the quantity of the enzyme addition was most effective at 0.05% of meat weight.

• Journal of Nutrition and Health
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• v.3 no.2
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• pp.87-94
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• 1970

The amino acid composition of human and cow's milk represents a standard of reference in infantnutrition. The amino acid compositions determined by automatic amino acid analyzer, Yanagimote Model LC-5. Protein in the human and cow's milk were found to be hydrolyzed to yield free amino acids. Qualitative data for free amino acids in the milk are as follows: 1) Amounts of acidic amino acids such as glutamic and aspartic acid in cow's milk were obserbed to be about 2 times compared with human milk and it is considered that the abundance in these amino acids may contribute significantly to the specific flavor of cow's milk. 2) It is much interesting that in the human milk the contents of sulfur-containing amino acids were high comparatively better than cow's milk; cystine was found to be 3 times ana methionine, 2 times. 3) In the human milk a high content of some essential amino acids such as threonine, isoleucine and leucine was demonstrated and a specific flavor sweet amino acids. 4) Large amounts of basic amino acid such as histidine was found to occur in human milk and arginine in cow's milk.

• Journal of the Korean Society of Food Science and Nutrition
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• v.21 no.3
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• pp.296-301
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• 1992

From the leaves of Ixeris sonchifolia (Compositae), luteolin and its glucoside and apigenin glucuronide were isolated and their structures were characterized on the basis of spectral data. Besides these flavonoids, the composition and relative content of free amino, acids and related compounds, compared to standards determined under identical conditions was also investigated using automatic amino acid analyzer. Major free amino acids were glutamic acid, aspartic acid, serine, proline, valine and arginine.

• Applied Biological Chemistry
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• v.23 no.1
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• pp.14-22
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• 1980

White and black sesame produced in Korea were defatted with ethyl ether or n-hexane. Defatted sesame meal was extracted with water and salt solution, and protein extraction was precipitated at various pH 1 through 12, with trichloro acetic acid (TCA), tannic acid and ammonium sulfate, respectively. Protein was purified by Sephadex A-25, G-75, G-100 and G-200, and identified its protein fraction by polyacrylamide gel electrophoresis. Amino acids composition of protein in white sesame was analyzed by automatic amino acid analyzer. Protein contents of white sesame, black sesame and sesame meal are 20.5%, 19.2%, and 44.7%, respectively. n-Hexane was the most suitable solvent for extraction of oil from sesame. Crude protein precipitation was better in higher pH. The protein extraction was more effective with the solution containing sodium chloride tinder the pH 8. Globulin in total protein was high and prolamin was less than in other cereal proteins. Glutamic acid contents of white sesame and sesame globulin were 17.1%, and 20%, respectively. Both proteins contained relatively high levels of essential amino acids. 12-13 bands were found in water soluble protein and 2 bands in salt soluble protein were detected by the disc gel electrophoresis, and were identified in both of white and black sesame. The salt soluble protein of white sesame could be purified by Sephadee G-100 and G-200.