• Title/Summary/Keyword: beta-Amino acids

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Isolation and Characterization of Parvalbumin Beta Gene from Channel Catfish (Ictalurus punctatus)

  • Kim, Soon-Hag
    • Journal of Aquaculture
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    • v.16 no.2
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    • pp.124-127
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    • 2003
  • Our previous studies of both microarray analysis in channel catfish muscle gene expression of 2 different ages and channel catfish muscle expressed sequence tag profiles demonstrated parvalbumin beta is one of the highly expressed muscle transcriptome. We have cloned and sequenced complementary DNA encoding the channel catfish parvalbumin which encode 109 amino acids. The deduced amino acid sequences of the catfish parvalbumin are highly conserved with those cloned from other teleosts. The availability of the catfish parvalbumin provides the opportunity of studying fish epitopes.

Design and Expression of High Nutritional Peptide (HEAAE) in E. coli

  • Kim, Jae-Ho;Lee, Chang-Kook;Hong, Bum-Shik
    • Journal of Microbiology and Biotechnology
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    • v.7 no.2
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    • pp.132-137
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    • 1997
  • A novel protein (HEAAE, High Essential Amino Acid Encoding Protein), rich in essential amino acids ($75{\%}$ of total), was designed and constructed in our laboratory. The designed peptides were analyzed by SYBLE and stable secondary and tertiary structures were predicted. The monomeric form (HEAAE-1) of the protein consists of 20 amino acid residues with four additional amino acids comprising a potential ${\beta}$-turn (HEAAE-4). Size exclusion analysis demonstrated that the monomer is self-aggregates in aqueous solution to form higher ordered multimeric structures, which are very reminiscent of natural plant storage proteins. The DNA encoding this amino acid sequence was synthesized, and from this monomeric gene fragment (heaae-1), the stable tetrameric form of the gene (heaae-4) was generated by subcloning into the E. coli expression vector pKK223-3. A clear 6 kDa polypeptide band corresponding to the molecular weight of the dimeric form (HEAAE-2) was detected. The smeared band which appeared around the molecular weight corresponding to HEAAE-4 of 11 kDa suggested that the tetramer form of this protein might be processed into smaller size products.

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Changes of Components of Citrus Sudachi Juice Heated at Various Temperatures (가열온도에 따른 영귤 과즙의 성분 변화)

  • Kim, Young-Dong;Lee, Young-Chul;Oh, Young-Ju;Kang, Young-Joo
    • Korean Journal of Food Science and Technology
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    • v.33 no.2
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    • pp.238-244
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    • 2001
  • The study was performed to investigate the changes of components and volatiles in citrus sudachi juice heated at 40, 50, 60, 70, 80 and $90^{\circ}C$. Total acidity, $^{\circ}Brix$, pH, organic acids, free amino acids, vitamin C, naringin, hesperidine, neohesperidin and volatiles were analyzed in fresh and heated citrus sudachi juices. The major organic acids were citric, malic and oxalic acids and their total contents were 5.27-5.48%. Citric acid content exceeded 92%, malic and oxalic acids were 3.6 and 3.2% in total orgainc acids. The organic acids decreased as heating temperature increased, but the their decreasing contents were 0.3% of total oraganic acids. Sixteen kinds of free amino acids presented in citrus sudachi juice. Major free amino acids were alanine, threonine, proline, aspargine, aspartic acid, serine, tyrosine, and trytophane and minor free amino acids were arginine, valine, glycine, lisoluecine, leucine and histidine. Free amino acids contents decreased as heating temperature increased. Vitamin C contents also decreased from 21.3 mg% to 17.3 mg% as heating temperature increased. Naringin, hesperidine and neohesperidin also slightly decreased from 304 mg% to 297.0 mg% as heating temperature increased. In the fresh and heated juices, a total of 50 volatiles were separated, of which 31 were identified. Limonene dominated in volatiles, followed by ${\gamma}-terpinene,\;{\alpha}-phellandrene$, myrcene and ${\alpha}-pinene$. ${\alpha}-Thujene$ presented in the fresh jucie but did not present in the heated juice above $50^{\circ}C$. However, ${\alpha}-Terpinolene$, terpinene-1-ol, ${\beta}-terpineol$, $cis-{\beta}-terpineol$, ${\alpha}-muurolene$, bicyclo(3.2.0)hept-6-ene, and mentha-1.4.8-triene did not presented in the fresh jucie but newly formed in the juice heated at $90^{\circ}C$.

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Changes in Chemical Compositions of Pumpkin(Cucurbita moschata DUCH.) Seed Sprouts (호박(Cucurbita moschata DUCH.)종실의 발아 성장 과정 중 성분 변화)

  • 이병진;장희순;이규희;오만진
    • Food Science and Preservation
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    • v.10 no.4
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    • pp.527-533
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    • 2003
  • This study was performed for increasing the consumption and developing the function of pumpkin(Cucurbita moschata DUCH.) seed. The changes of the contents of general chemical compositions, fatty acids, amino acids, ascorbic acid and ${\beta}$-carotene during sprouting were analyzed. Also, the bitter taste, which was produced during sprouting, were purified by using thin layer chromatography and preparative high pressure liquid chromatography. The purified bitter compound was identified by mass spectrum and nuclear magnetic resonance($^1$H '||'&'||' $\^$13/C-NMR). Weight of pumpkin seed sprout was increased to 348.4% and the length of stem was dramatically increased at 8 days. In each head and stem parts of the pumpkin seed sprout, the contents of protein and lipid were decreased, however, the contents of fiber, ash and soluble inorganic nitrogen were increased. The fatty acids of the pumpkin seed sprout were mainly represented as linoleic acid, oleic acid, palmitic acid and stearic acid. During sprouting, palmitic acid was gradually increased, reversely, linoleic acid was gradually decreased. The general amino acids of head part in the pumpkin seed sprout grown at 23$^{\circ}C$ during 8 days were orderly more contained glycine, alanine, arginine, cystein and proline. Those of free amino acids were orderly more contained arginine, threonine, alanine and glutamine. The contents of L-ascorbic acid and ${\beta}$-camtene of the pumpkin seed sprout were gradually increased with increasing sprouting days. The bitter taste material of head part of the pumpkin seed sprout was detected at Rf value 0.72 on silicagel TLC plate and separuted as one peak by HPLC. The chemical structure of the puified bitter compound was identified as a cucurbitacin glycoside by MS and NMR. The content of bitter compound at 8 days was contained 42.2 mg per 1kg sprout head.

Isolation and Molecular Analysis of Methanol Oxidation Genes in an Obligate Methylotrophic Bacterium, Metheylobacillus sp. Strain SK-5

  • Choi, Hack-Sun;Kim, Jin-Kwon;Ahn, Yeong-Hee;Koh, Moon-Joo;Kim, Si-Wouk
    • Journal of Microbiology and Biotechnology
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    • v.12 no.5
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    • pp.819-825
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    • 2002
  • Methanol dehydrogenase (MDH) is a key enzyme in the process of methanol oxidation in methylotrophic bacteria. However, information on MDH genes from genus Methylobacillus is limited. In this study, a 6.5-kb HindIII DNA fragment of Methylobacillus sp. SK-5 chromosomal DNA was isolated from the genomic library of the strain by using a degenerate oligonucleotide probe that was designed based on JV-terminal amino acid sequence of the MDH $\alpha$ subunit purified from the strain. Molecular analysis of the fragment revealed four tightly clustered genes (mxaFJGI) involved in the methanol oxidation. The first and fourth genes were very similar to mxaF (77% identity for nucleotides an 78% identity for amino acids) and mxaF (67% Identity for nucleotides and 68% Identity for amino acids) genes, respectively, from Methylovorus sp. SSI. Genes mxaF and mxaI encode $\alpha$ and $\beta$ subunits of MDH, respectively. The two subunits were identified from purified MDH from Methylobacillus sp. SK-5. A dendrogram constructed by comparison of amino acid sequences of MDH u subunits suggests that MxaF from Methylobacillus sp. SK-5 belongs to a subfamily cluster of MDH u subunits from $\beta$-subgroup Proteobacteria. The subfamily cluster is separated from the other subfamily that consists of $\beta$- and $\gamma$-subgroup Proteobacteria. This study provided information on mn genes from a methylotrophic bacterium in $\beta$-subgroup Proteobacteria, which would aid to better develop a gene probe to detect one-carbon metabolizing bacteria.

Screening and Purification of a Novel Transaminase Catalyzing the Transamination of Aryl ${\beta}-Amino$ Acid from Mesorhizobium sp. LUK

  • Kim, Ju-Han;Kyung, Do-Hyun;Yun, Hyung-Don;Cho, Byung-Kwan;Kim, Byung-Gee
    • Journal of Microbiology and Biotechnology
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    • v.16 no.11
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    • pp.1832-1836
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    • 2006
  • Mesorhizobium sp. LUK, which utilizes 3-amino-3-phenylpropionic acid as the sole source of nitrogen with high enantioselectivity (E(S)>100), was isolated using enrichment culture. The enzyme involved in the utilization of (S)-3-amino-3-phenylpropionic acid was confirmed to be a transaminase and was purified by 235-folds with a specific activity of 0.72 U/mg. The molecular weight of the purified protein was ca. 47 kDa and the active enzyme was determined as a dimer on gel filtration chromatography. The N-terminal sequence was obtained from the purified protein. Spontaneous decarboxylation of produced ${\beta}-keto$ acids was observed during the chiral resolution of 3-amino-3-phenylpropionic acid.