• Journal of Korean Society of Environmental Engineers
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• v.31 no.5
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• pp.332-340
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• 2009

This study was conducted to analyze and determine formation potentials for chlorination disinfection by-products (DBPs) from twenty amino acid compounds with or without $Br^-$. Two of twenty amino acid compound were tryptophan and tyrosine that were relatively shown high for formation of trihalomethanes (THMs)/dissolved organic carbon (DOC) whether or not $Br^-$ presented. Other 18 compounds were shown low for formation of THMs/DOC whether or not $Br^-$ presented. Five amino acid compounds that were tryptophan, tyrosine, asparagine, aspartic acid and histidine were shown high for formation of haloacetic acids (HAAs)/DOC whether or not $Br^-$ presented. Although formation of dichloroacetic acid (DCAA) was dominated in asparagine, aspartic acid and histidine, trichloroacetic acid (TCAA) was dominated in tryptophan and tryptophan. The formation of haloacetnitriles (HANs)/DOC whether or not $Br^-$ presented was high in Aspartic acid, histidine, asparagine, tyrosine and tryptophan. Specially, aspartic acid was detected 660.2 ${\mu}$g/mg (HAN/DOC). Although the formation of chloralhydrate (CH)/DOC was shown high in asparagine, aspartic acid, histidine, methionine, tryptophan and tyrosine, the formation of Chloropicrin (CP)/DOC was low (1 ${\mu}$g/mg) in twenty amino acid compounds. The formations of THM, HAA and HAN were also investigated in functional groups of amino acids. The highest formation of THM was shown in amino acids compounds (tryptophan and tyrosine) with an aromatic functional group. Highest, second-highest, third-highest and fourth-highest functional groups for formation of HAA were aromatic, neutral, acidic and basic respectively. In order of increasing functional groups for formation of HAN were acidic, basic, neutral and aromatic.

• Journal of Nutrition and Health
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• v.15 no.1
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• pp.22-29
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• 1982

As sugar and amino acid were added to the ascorbic acid solution the content of ascorbic acid was quantitatively determined by 2, 4-dinitrophenyl hydrazine method. The residual ascorbic acid was shown to increase slightly when sorbose, rhamnose or mannose was added to the ascorbic acid solution whereas residual ascorbic acid was shown to decrease in time to the addition of other sugars. The effects of amino acid to the ascorbic acid solution were found that monoamino-mono, or dicarboxylic acids and aromatic amino acids increased the residual ascorbic acidity whereas diamino-monocarboxylic acids and sulfur containing amino acids decreased the residual ascorbic acidity.

• Archives of Pharmacal Research
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• v.28 no.4
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• pp.421-432
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• 2005

In order to understand the renal reabsorption mechanism of neutral amino acids via amino acid transporters, we have isolated human L-type amino acid transporter 2 (hLAT2) and human T-type amino acid transporter 1 (hTAT1) in human, then, we have examined and compared the gene structures, the functional characterizations and the localization in human kidney. Northern blot analysis showed that hLAT2 mRNA was expressed at high levels in the heart, brain, placenta, kidney, spleen, prostate, testis, ovary, lymph node and the fetal liver. The hTAT1 mRNA was detected at high levels in the heart, placenta, liver, skeletal muscle, kidney, pancreas, spleen, thymus and prostate. Immunohistochemical analysis on the human kidney revealed that the hLAT2 and hTAT1 proteins coexist in the basolateral membrane of the renal proximal tubules. The hLAT2 transports all neutral amino acids and hTAT1 transports aromatic amino acids. The basolateral location of the hLAT2 and hTAT1 proteins in the renal proximal tubule as well as the amino acid transport activity of hLAT2 and hTAT1 suggests that these transporters contribute to the renal reabsorption of neutral and aromatic amino acids in the basolateral domain of epithelial proximal tubule cells, respectively. Therefore, LAT2 and TAT1 play essential roles in the reabsorption of neutral amino acids from the epithelial cells to the blood stream in the kidney. Because LAT2 and TAT1 are essential to the efficient absorption of neutral amino acids from the kidney, their defects might be involved in the pathogenesis of disorders caused by a disruption in amino acid absorption such as blue diaper syndrome.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.50 no.spc1
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• pp.191-195
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• 2005

Experiment was conducted to establish the standard of quality evaluation in Korean cultivated peony roots. free sugars, free amino acids, organic acids and aromatic components, which were generally considered to be information components of five sensory test in peony roots, were examined. As free sugars, sucrose, glucose and fructose were identified in peony roots. $\gamma-aminoisobuturic$ acid, arginine and other 16 kinds of free amino acids were found in peony roots. The major organic acids of peony roots were oxalic acid, citric acid and malic acid. Eugenol and other 10 aromatic components were identified in peony roots by GC/MSD.

• Bulletin of the Korean Chemical Society
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• v.9 no.4
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• pp.255-255
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• 1988

• Korean Journal of Agricultural Science
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• v.9 no.2
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• pp.576-583
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• 1982

The variation of free amino acids during the tomato producing was studied using a tomato variety, Kagome 77. The concentration of free amino acids in fresh and heated pulp, and in puree and paste was analyzed by using automatic amino acid analyzer, Hitachi model KLA-5. 1. A significant difference in decomposition rate of glutamine and asparagine among amide group was recognized. For instance, the glutamine decomposed fast and no glutamine was found in the paste, while 56% of asparagine was found in the paste. 2. The diminishing quantity of glutamic acid among acid group was highest among all free amino acids. The quantity of aspartic acid was next to the glutamine. The percents of glutamic acid and aspartic acid left over were 38% and 24%, respectively. 3. Glycine, alanine, valine, isoleucine and leucine of neutral amino acids tended to be reduced a little during the heating, concentrating process. 4. No apparent variation was found for the lysine and histidine belonging to basic amino acids. while arginine increased a little. 5. Tyrosine, phenylalanine and tryptophane of aromatic group seemed to increase a little during the heating process. But the variations of them during the concentrating process were not recognized. 6. The methionine content, sulfur containing amino acid decreased a little throughout the process. But the decrease of ${\gamma}-amino$ butyric acid of non-protein was not apparently recognized. 7. The amino acid contents of fresh pulp were found as following order: glutamic acid>${\gamma}$-amino butyric acid>glutamine>aspartic acid>asparagine. The amino acid contents of paste were as glutamic acid>${\gamma}$-amino butyric acid>aspartic acid and aspargine. The percent distribution of aromatic and basic amino acids increased, even it was not great. 8. When amino acids were analyzed by Hitachi KLA-5, unknown peak which was never app eared in the fresh pulp before tryptophane was appeared when processed. The peak became greater when heated and concentrated. Later it was known that the peak was not due to lysinoalanine or ornithine.

• Korean Journal of Soil Science and Fertilizer
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• v.21 no.3
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• pp.301-306
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• 1988

Contents and distribution of amino acids in the hydrolysates of humic acids extracted from straw of rice and barley at three different dates during decomposition were examined. The results obtained from this study may be summed up as the following: 1. There are differences between the humic acid hydrolysates from rice straw and barley straw in regards of composition of humic acids and distribution of amino acids. 2. Neutral amino acids as a group occupy the largest share, followed by acidic amino acids and basic amino acids. 3. The total amount of amino acids per gram of humic acid is greater in straw of rice than in straw of barley. 4. With the humification progressing the content of lysine increases, but the content of histidine decreases. In general glycine, glutamic acid, aspartic acid, alanine and leucine constitute the 5 predominant amino acids in all hydrolysates. 5. Arginine is not detected at all in any of the hydrolysates of humic acids obtained from humified materials. 6. The presence of phenylalanine and tyrosine is an evidence for the aromatic characteristics of humic acids.

• Journal of Microbiology and Biotechnology
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• v.28 no.10
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• pp.1581-1588
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• 2018

The growth of lactic acid bacteria (LAB) generates a high number of metabolites related to aromas and flavors in fermented dairy foods. These microbial proteases are involved in protein hydrolysis that produces necessary peptides for their growth and releases different molecules of interest, like bioactive peptides, during their activity. Each genus in particular has its own proteolytic system to hydrolyze the necessary proteins to meet its requirements. This review aims to highlight the differences between the proteolytic systems of Streptococcus thermophilus and other lactic acid bacteria (Lactococcus and Lactobacillus) since they are microorganisms that are frequently used in combination with other LAB in the elaboration of fermented dairy products. Based on genetic studies and in vitro and in vivo tests, the proteolytic system of Streptococcus thermophilus has been divided into three parts: 1) a serine proteinase linked to the cellular wall that is activated in the absence of glutamine and methionine; 2) the transport of peptides and oligopeptides, which are integrated in both the Dpp system and the Ami system, respectively; according to this, it is worth mentioning that the Ami system is able to transport peptides with up to 23 amino acids while the Opp system of Lactococcus or Lactobacillus transports chains with less than 13 amino acids; and finally, 3) peptide hydrolysis by intracellular peptidases, including a group of three exclusive of S. thermophilus capable of releasing either aromatic amino acids or peptides with aromatic amino acids.

• Bulletin of the Korean Chemical Society
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• v.19 no.10
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• pp.1105-1109
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• 1998

A chiral stationary phase derived from (S)-N-(3,5-dinitrobenzoyl)leucine N-phenyl N-alkyl amide (CSP 2) was applied in separating the two enantiomers of various π-basic aromatic derivatives of leucine N-propyl amide in order to evaluate π-basic aromatic groups as an effective derivatizing group for the resolution of a-amino acids. Subsequently N-(3,5-dimethoxybenzoyl) group was found to be very effective as a π-basic aromatic derivatizing group. Based on these results, N-(3,5-dimethoxybenzoyl) derivatives of various a-amino N-propyl amides, N,N-diethyl amides and esters were resolved on the CSP derived from (S)-N-(3,5-dinitrobenzoyl) leucine N-phenyl N-alkyl amide (CSP 2) and the resolution results were compared with those on the CSP derived from (S)-N-(3,5-dinitrobenzoyl)leucine N-alkyl amide (CSP 1). The enantioselectivities exerted by CSP 2 were much greater than those exerted by CSP 1. In addition, racemic N-(3,5-dimethoxybenzoyl)-a-mino N,Ndiethyl amides were resolved much better than the corresponding N-(3,5-dimethoxybenzoyl)-a-mino N-propyl amides and esters on both CSPs. Based on these results, a chiral recognition mechanism utilizing the π-π donor-acceptor interaction and the two hydrogen bondings between the CSP and the analyte was proposed.

• Journal of Microbiology and Biotechnology
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• v.24 no.10
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• pp.1389-1396
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• 2014

The entire nucleotide sequence of the TKL1 gene encoding transketolase (TKL) in an erythritol-producing yeast of Candida magnoliae was determined by degenerate polymerase chain reaction and genome walking. Sequence analysis revealed an open reading frame of C. magnoliae TKL1 (CmTKL1) that spans 2,088 bp and encodes 696 amino acids, sharing 61.7% amino acid identity to Kluyveromyces lactis TKL. Functional analysis showed that CmTKL1 complemented a Saccharomyces cerevisiae tkl1 tkl2 double mutant for growth in the absence of aromatic amino acids and restored transketolase activity in this mutant. An enzyme activity assay and RT-PCR revealed that the expression of CmTKL1 is induced by fructose, $H_2O_2$, and KCl. The GenBank accession number for C. magnoliae TKL1 is KF751756.