• Title/Summary/Keyword: beta-Amino acids

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Changes on the Components of Lindera obtusiloba BL. Leaf Teas by Manufacturing Process (제조방법에 따른 생강나무(Lindera obtusiloba BL.) 잎차의 성분변화)

  • 황경아;김광수;김남우;신승렬
    • Food Science and Preservation
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    • v.10 no.4
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    • pp.488-492
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    • 2003
  • This study was analyzed to the components of leaf teas produced by manufature methods for which estimated food and nutritional values of Lindera obtusiloba loaves growed in Korea and had unique taste and aroma. There were identified to four kinds of free sugars in Lindera obtusiloba leaf teas and its content was the highest in the roasted tea among others. The contents of glutamic acid, aspartic acid, asparagine, and glycine were remarkably higher than other amino acids. The contentsof free amino acid in the leased tea and the androasted tea after steaming wase. 6 mg/100g had 101.5 mg/100g, respectively,had especially higher than in the others. Among the amino acid derivativer, phosphoserine, ${\alpha}$-aminobutyric acid, ${\beta}$-aminobutvic acid, and anserine contents were especially higher than others, but were not significantly difference by the manufacturing process. The volatile organic acids were composed acetic, propionic and butyric acid, and the nenvolatility organic acid were composed citric, oxalic, levulinic glutaric, lactic and pyroglutamic acid.

One-Step Enzymatic Synthesis of Blue Pigments from Geniposide for Fabric Dyeing

  • Cho, Y.J.;Kim, S.Y.;Kim, J.;Choe, E.K.;Kim, S.I.;Shin, H.J.
    • Biotechnology and Bioprocess Engineering:BBE
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    • v.11 no.3
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    • pp.230-234
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    • 2006
  • In this study, we describe a one-step chemoenzymatic reaction for the production of natural blue pigments, in which the geniposide from Gardenia extracts is transformed by glycosidases to genipin. Genipin is then allowed to react with amino acids, thereby generating a natural blue pigment. The ${\beta}-glycosidases$, most notably Isolase (a variant of ${\beta}-glucanase$), recombinant ${\beta}-glycosidases$, Cellulase T, and amylases, were shown to hydrolyze geniposide to produce the desired pigments, whereas the ${\alpha}-glycosidases$ did not. Among the 20 tested amino acids, glycine and tyrosine were associated with the highest dye production yields. The optimal molar ratio of geniposide to glycine, two reactants relevant to pigment production, was unity The natural blue pigments produced in this study were used to dye cotton, silk, and wool. The color yields of the pigments were determined to be significantly higher than those of other natural dyes. Furthermore, the color fastness properties of these dyes were fairly good, even in the absence of mordant.

Studies on the Amino Acid and Fatty Acid Compositions in the Seed and Pulpy Substance of Feral Peach (Prunus persica Batsch var. davidiana Max.) (야생 돌복숭아 씨와 과육의 아미노산 및 지방산 조성에 관한 연구)

  • Kim, Han-Soo
    • Journal of Life Science
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    • v.17 no.1 s.81
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    • pp.125-131
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    • 2007
  • Amino acid and fatty acid compositions of the physiological activity substance in the seed and pulpy substance of feral peach (Prunus persica Batsch var. davidiana Max.) were analyzed for the use as an biohealth functional processed products. The proximate compositions in the vacuum freeze dried seed and pulpy substance of feral peach were carbohydrate 63.92% and 75.11%, crude protein 27.85% and 12.77%, moisture 3.61% and 4.69%, crude fat 1.21% and 4.80%, crude ash 3.41% and 2.63%, respectively. Total amino acid contents in the protein of feral peach seed were 3,444.35 mg%, and the major amino acids were aspartic acid(681.10 mg%), glutamic acid(495.48 mg%), alanine(283.66 mg%), serine(251.36 mg%), proline(229.80 mg%), lysine(192.31 mg%) and leucine(191.34 mg%), respectively. Total amino acid contents in the protein of feral peach pulpy substance were 1,064.02 mg%, and the major amino acids followed aspartic acid(250.15 mg%), glutamic acid(129. 63 mg%), lysine, proline, leucine, alanine and serine, in a decreasing order. The richest total amino acid content contained in feral peach seed and pulpy substance was aspartic acid, followed by glutamic acid. The amount of free amino acids of feral peach seed were 6,215.34 ms%, and the major free amino acids were glutamic acid(827.25 mg%), threonine, valine and $\beta-aminobutyric$ acid, respectively. Free amino acid contents of pulpy substance were 683.82 mg%, and the major free amino acids were glutamic acid(339.49 mg%), serine proline, alanine and $\gamma-amino-n-butyric$ acid. Especially, in the case of glutamic acid, it was highest. The compositions of major total fatty acid in the lipid feral peach (Prunus persica Batsch var. davidiana Max.) seed and pulpy sabstance were linoleic acid($C_{18:2}$, n-6) and linolenic acid($C_{18:3}$, n-3), particularly.

Sodium Dependent Taurine Transport into the Choroid Plexus, the Blood-Cerebrospinal Fluid Barrier

  • Chung, Suk-Jae;Ramanathan, Vikram;Brett, Claire M.;Giacomini, Kathleen M.
    • Journal of Pharmaceutical Investigation
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    • v.25 no.3
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    • pp.7-20
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    • 1995
  • Taurine, a ${\beta}-amino$ acid, plays an important role as a neuromodulator and is necessary for the normal development of the brain. Since de novo synthesis of taurine in the brain is minimal and in vivo studies suggest that taurine dose not cross the blood-brain barrier, we examined whether the choroid plexus, the blood-cerebrospinal fluid (CSF) barrier, plays a role in taurine transport in the central nervous system. The uptake of $[^3H]-taurine$ into ATP depleted choroid plexus from rabbit was substantially greater in the presence of an inwardly directed $Na^+$ gradient taurine accumulation was negligible. A transient in side-negative potential gradient enhanced the $Na^+-driven$ uptake of taurine into the tissue slices, suggesting that the transport process is electrogenic, $Na^+-driven$ taurine uptake was saturable with an estimated $V_{max}$ of $111\;{\pm}\;20.2\;nmole/g/15\;min$ and a $K_M\;of\;99.8{\pm}29.9\;{\mu}M$. The estimated coupling ratio of $Na^+$ and taurine was $1.80\;{\pm}\;0.122.$ $Na^+-dependent$ taurine uptake was significantly inhibited by ${\beta}-amino$ acids, but not by ${\alpha}-amino$ acids, indicating that the transporter is selective for ${\beta}-amino$ acids. Since it is known that the physiological concentration of taurine in the CSF is lower than that in the plasma, the active transport system we characterized may face the brush border (i.e., CSF facing) side of the choroid plexus and actively transport taurine out of the CSF. Therefore, we examined in vivo elimination of taurine from the CSF in the rat to determine whether elimination kinetics of taurine from the CSF is consistent with the in vitro study. Using a stereotaxic device, cannulaes were placed into the lateral ventricle and the cisterna magna of the rat. Radio-labelled taurine and inulin (a marker of CSF flow) were injected into the lateral ventricle, and the concentrations of the labelled compounds in the CSF were monitored for upto 3 hrs in the cisterna magna. The apparent clearance of taurine from CSF was greater than the estimated CSF flow (p<0.005) indicating that there is a clearance process in addition to the CSF flow. Taurine distribution into the choroid plexus was at least 10 fold higher than that found in other brain areas (e. g., cerebellum, olfactory bulb and cortex). When unlabelled taurine was co-administered with radio-labelled taurine, the apparent clearance of taurine was reduced (p<0.0l), suggesting a saturable disposition of taurine from CSF. Distribution of taurine into the choroid plexus, cerebellum, olfactory bulb and cortex was similarly diminished, indicating that the saturable uptake of taurine into these tissues is responsible for the non-linear disposition. A pharmacokinetic model involving first order elimination and saturable distribution described these data adequately. The Michaelis-Menten rate constant estimated from in vivo elimination study is similar to that obtained in the in vitro uptake experiment. Collectively, our results demonstrate that taurine is transported in the choroid plexus via a $Na^+-dependent,saturable$ and apparently ${\beta}-amino$ acid selective mechanism. This process may be functionally relevant to taurine homeostasis in the brain.

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Amino acid substitution on β and α of Cyt2Aa2 affects molecular interaction of protoxin

  • Thammachat, Siriya;Pungtanom, Nuanwan;Kidsanguan, Somruathai;Pathaichindachote, Wanwarang;Promdonkoy, Boonhiang;Krittanai, Chartchai
    • BMB Reports
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    • v.43 no.6
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    • pp.427-431
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    • 2010
  • Cyt2Aa2 is a mosquito-larvicidal protein produced as a 29 kDa crystalline protoxin from Bacillus thuringiensis subsp. darmstadiensis. To become an active toxin, proteolytic processing is required to remove amino acids from its N- and C-termini. This study aims to investigate the functional role of amino acid residues on the N-terminal ${\beta}1$ and C-terminal ${\alpha}F$ of Cyt2Aa2 protoxin. Mutant protoxins were constructed, characterized and compared to the wild type Cyt2Aa2. Protein expression data and SDS-PAGE analysis revealed that substitution at leucine-33 (L33) of ${\beta}1$ has a critical effect on dimer formation and structural stability against proteases. In addition, amino acids N230 and I233-F237 around the C-terminus ${\alpha}F$ demonstrated a crucial role in protecting the protoxin from proteolytic digestion. These results suggested that ${\beta}1$ and ${\alpha}F$ on the Nand C-terminal ends of Cyt2Aa2 protoxin play an important role in the molecular interaction and in maintaining the structural stability of the protoxin.

Structure Determination of Antifungal KRF-001 Produced by Bacillus subtilis subsp. krictiensis (Bacillus subtilis subsp. krictiensis가 생산하는 항진균 물질 KRF-001의 구조 결정)

  • 김성기;이남경;정태숙;김영국;최진자;복성해
    • Microbiology and Biotechnology Letters
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    • v.19 no.6
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    • pp.598-603
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    • 1991
  • An antifungal mixture of six members (component A to F), KRF-001 produced by Bacillzts subtilis subsp. krictiensis was isolated from the fermentation broth. Molecular weight of component A to F was determined by FAB-MS to be 1042, 1056, 1056, 1070, 1070 and 1084 respectively. Various instrumental analyses (amino acid analysis, GC-MS, $^1H-NMR, ^1HH$ COSY NMR) revealed that the mixture was a homologous cyclic peptide composed of each one mole of glutamine, proline, tyrosine, serine, unusual $\beta$-amino acid and three moles of asparagine. The structural differences of component A to F were found in carbon number and terminal structure of the unusual $\beta$-amino acid. After determination of the sequence and stereochemistry of those amino acids, the tentative structure of KRF-001 was determined.

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Xylan Hydrolysis by Treatment with Endoxylanase and $\beta$-Xylosidase Expressed in Yeast

  • Heo, Sun-Yeon;Kim, Joong-Kyun;Kim, Young-Man;Nam, Soo-Wan
    • Journal of Microbiology and Biotechnology
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    • v.14 no.1
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    • pp.171-177
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    • 2004
  • The endoxylanase (642 bp; 213 amino acids) and $\beta$-xylosidase (1,602 bp; 533 amino acids) genes from Bacillus sp. were amplified by PCR and separately inserted into the downstream of the yeast ADH1 promoters, resulting in the pAEDX-1 (7.63 kb) and pAEX (8.47 kb) plasmids, respectively. When the yeast transformants, S. cerevisiae SEY2102 harboring pAEDX-1 or pAEX, were grown on YPD medium, the total activities of the enzymes were approximately 9.8 unit/ml for endoxylanase and 2.9 unit/m1 for $\beta$-xylosidase. When the three kinds of xylan from oat spelts, birch wood, and corncob were hydrolyzed by treating with recombinant endoxylanase and $\beta$-xylosidase, it was found that xylose, xylobiose, and xylotriose were produced. To efficiently hydrolyze xylan, various reaction conditions such as amount of enzymes, substrate type, substrate concentration, temperature, and reaction time were examined. The optimized conditions for the hydrolysis of xylan were as follows: amount of endoxylanase, 10 units; amount of $\beta$-xylosidase, 10 units; temperature, $50^\circ{C}$; substrate type, oat spelts xylan; substrate concentration, 6%; reaction time, 1 h. Under the optimal condition, xylose was mainly produced from oat spelts xylan by cooperative action of endoxylanase and $\beta$-xylosidase.

Cloning and Expression of β1-Adrenergic Receptor Genes in Adipose Tissues from Korean Native Cattle (Hanwoo)

  • Ha, S.H.;Chung, M.I.;Baik, M.G.;Choi, Y.J.
    • Asian-Australasian Journal of Animal Sciences
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    • v.14 no.1
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    • pp.13-16
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    • 2001
  • Bovine ${\beta}1$-adrenergic receptor (AR) cDNA was cloned using degenerative primers. Bovine ${\beta}1$-AR coded for 467 amino acids and the comparison of the deduced amino acid sequence with that of sheep showed 93.4% identity. Northern blot analysis indicated that transcript size for the bovine ${\beta}1$-AR was 3.6 kb in the adipose tissue. The expression level of three $\beta$-ARs (1, 2, and 3) in bovine abdominal, subcutaneous, and perirenal adipose tissues were examined using reverse transcription-polymerase chain reaction (RT-PCR), and the levels of ${\beta}1$- and ${\beta}3$-AR mRNA were found to be lower in the subcutaneous adipose tissue than in the abdominal and perirenal adipose tissues. These results suggest that the expression of $\beta$-ARs mRNA are differentially regulated among the adipose tissues.

Molecular Characterization of Rockbream (Oplegnathus fasciatus) Cytoskeletal β-actin Gene and Its 5'-Upstream Regulatory Region

  • Lee, Sang-Yoon;Kim, Ki-Hong;Nam, Yoon-Kwon
    • Fisheries and Aquatic Sciences
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    • v.12 no.2
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    • pp.90-97
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    • 2009
  • The cytoskeletal $\beta$-actin gene and its 5'-upstream region were isolated and characterized in the rockbream (Oplegnathus fasciatus). Complementary DNA of the rockbream $\beta$-actin represented a 1,125 bp of an open reading frame encoding 375 amino acids, and the rockbream $\beta$-actin cDNA and deduced amino acid sequences were highly homologous to those of other vertebrate orthologs. At the genomic level, the $\beta$-actin gene also exhibited an organization typical of vertebrate cytoskeletal actin genes (2,159 bp composed of five translated exons interrupted by four introns) with a conserved GT/AG exon-intron splicing rule. The putative non-translated exon predicted in the rockbream $\beta$-actin gene was much more homologous with those of teleostean $\beta$-actin genes than those of mammals. The 5'-upstream regulatory region isolated by genome walking displayed conserved and essential elements such as TATA, CArG and CAAT boxes in its proximal part, while several other immune- or stress-related motifs such as those for NF-kappa B, USF, HNF, AP-1 and C/EBP were in the distal part. Semi-quantitative RT-PCR assay results demonstrated that the rockbream $\beta$-actin transcripts were ubiquitously but different-tially expressed across the tissues of juveniles.

A Gene Encoding $\beta$-amylase from Saprolegnia parasitica and Its Expression in Saccharomyces cerevisiae

  • Kim, Hee-Ok;Park, Jeong-Nam;Shin, Dong-Jun;Lee, HwangHee Blaise;Chun, Soon-Bai;Bai, Suk
    • Journal of Microbiology and Biotechnology
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    • v.11 no.3
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    • pp.529-533
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    • 2001
  • The ${\beta}$-Amylase cDNA fragment from the oomcete Saprolegnia parasitica was cloned by reverse transcription-polymerase chain reaction (RT-PCR) using degenerate oligonucleotide primers derived from conserved ${\beta}$-amylase sequences. The 5'and 3'regions of the $\beta$-amylase gene were amplified using the rapid amplification of cDNA ends (rACE) system. It consisted of an open reading frame of 1,350 bp for a protein of 450 amino acids. Comparison between the genomic and cDNA sequences revealed that the intron was not present in the coding region. The deduced amino acid sequence of the ${\beta}$-amylase gene had a 97% similarity to the ${\beta}$-amylase of Saprolegnia ferax, followed by 41% similarity to those of Arabidopsis thaliana, Hordeum vulgare, and Zea mays. The ${\beta}$-amylase gene was also expressed in Saccharomyces cerevisiae by placing it under the control of the alcohol dehydrogenase gene (ADC1) promoter.

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