• Title/Summary/Keyword: hydrophobic acid

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Characteristics of Removal of Perfluorinated Compounds (PFCs) Using Magnetic Ion Exchange Resin (MIEX®) in Water (자성체 이온교환수지(MIEX®)를 이용한 수중의 과불화화합물(PFCs) 제거 특성)

  • Son, Hee-Jong;Yoom, Hoon-Sik;Kim, Kyung-A;Ryu, Sang-Weoun;Kwon, Ki-Won
    • Journal of Environmental Science International
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    • v.22 no.8
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    • pp.1009-1017
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    • 2013
  • Perfluorooctanoic acid (PFOA) and perfluorooctyl sulfonate (PFOS) is a new persistent organic pollutants of substantial environmental concern. This study investigated the potential of magnetic ion exchange resin (MIEX$^{(R)}$) as the adsorbent for the removal of PFOA and PFOS from Nakdong River water. In our batch experiments, we studied the effect of some parameters (pH, temperature, sulfate concentration) on the removal of PFOA and PFOS. The results of sorption kinetics on MIEX$^{(R)}$ show that it takes 90 min to reach equilibrium but the economical contact time and dosage were 30 min and 10 mL/L. An increase in pH (pH 6~10) leads to a decrease in PFOA (2.0%) and PFOS (3.6%) sorption on MIEX$^{(R)}$. The sorption of both PFOA and PFOS decreases with an increase in ionic strength for sulfate ion (${SO_4}^{2-}$), due to the competition phenomenon. An increase in water temperature ($8^{\circ}C{\sim}28^{\circ}C$) in water leads to a increase in PFOA (2.8%) and PFOS (4.3%) sorption on MIEX$^{(R)}$. Based on the sorption behaviors and characteristics of the adsorbents and adsorbates, ion exchange and hydrophobic interaction were deduced to be involved in the sorption, and hemi-micelles possibly formed in the intraparticle pores.

Nutritional Value and Bioactive Properties of Enzymatic Hydrolysates prepared from the Livers of Oncorhynchus keta and Oncorhynchus gorbuscha (Pacific Salmon)

  • Yoon, Ho Dong;Karaulova, Ekaterina P.;Shulgina, Lilia V.;Yakush, Evgeni V.;Mok, Jong Soo;Lee, Su Seon;Xie, Chengliang;Kim, Jeong Gyun
    • Fisheries and Aquatic Sciences
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    • v.18 no.1
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    • pp.13-20
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    • 2015
  • Calculated chemical scores (computed in relation to the FAO/WHO reference protein) for salmon liver protein hydrolysates indicated that all amino acids (other than methionine and threonine) were present in adequate or excess quantities; thus, the raw liver material is a good source of essential amino acids. The hydrophobic amino acids contents in hydrolysates prepared from Oncorhynchus keta and O. gorbuscha were 38.4 and 39.1%, respectively. The proportion of released peptides exceeding 500 kDa was reduced when hydrolysates were treated with the commercial enzyme Alcalase, although proportions in the following MW ranges were elevated: 100-500 kDa and <50 kDa. The optimal conditions for enzymatic hydrolysis were as follows: pH 7.0, $50^{\circ}C$, and a reaction time of 1 h. Of the different proteases tested, Alcalase was the most efficient for production of salmon liver hydrolysate with the highest 1,1-diphenyl-2-picrylhydrazyl (DPPH) scavenging activity. The hydrolysates prepared from salmon liver had a balanced amino acid composition. The liver protein hydrolysates contained low molecular weight peptides, some of which may be bio-active; this bio-active potential should be investigated. Inhibition of the DPPH radical increased with increased degree of hydrolysis (DH), regardless of protease type. DPPH radical scavenging abilities, antithrombotic effects and ${\alpha}$-glucosidase enzyme inhibition effects of O. keta liver hydrolysate increased in a dose-dependent manner. Thus, salmon liver hydrolysate may be useful in functional food applications and as a source of novel products.

Characteristics of α-Tocopherol-loaded Nanostructured Lipid Carriers and their Stabilization Effect (α-Tocopherol을 함유한 Nanostructured Lipid Carriers의 특성과 안정화 효과)

  • Jun, Yoon Kyung;Lim, Yoon Mi;Jin, Byung Suk
    • Applied Chemistry for Engineering
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    • v.26 no.6
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    • pp.659-665
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    • 2015
  • Loading of hydrophobic ${\alpha}$-tocopherol into nanostructured lipid carrier (NLC) was performed for improving its oxidative stability. First, various NLCs with different constituents and mixing ratios were prepared and their characteristics were investigated. While the stable NLCs were made when cetyl palmitate (CP) or glyceryl monosterate (GMS) was used as a solid lipid, the phase separation occurred in the NLCs consisting of stearic acid. Particle sizes of the NLCs were several hundreds of nanometers and the size decreased with increasing the ratio of solvent to lipid. It was examined from DSC thermogram and anisotropy test that the degree of crystallinity of the lipid phase decreased and the lipid matrix became less ordered when octyldodecanol, a long chain fatty alcohol, was added into the solid lipid. The oxidative stability of ${\alpha}$-tocopherol in NLC was remarkably improved compared to that in solution or emulsion under high temperature ($45^{\circ}C$) and UV radiation, which was verified through DPPH test and peroxide value measurement.

Synthesis, Characterization and DNA Interaction Studies of (N,N'-Bis(5-phenylazosalicylaldehyde)-ethylenediamine) Cobalt(II) Complex

  • Sohrabi, Nasrin;Rasouli, Nahid;Kamkar, Mehdi
    • Bulletin of the Korean Chemical Society
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    • v.35 no.8
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    • pp.2523-2528
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    • 2014
  • In the present study, at first, azo Schiff base ligand of (N,N'-bis(5-phenylazosalicylaldehyde)-ethylenediamine) ($H_2L$) has been synthesized by condensation reaction of 5-phenylazosalicylaldehyde and ethylenediamine in 2:1 molar ratio, respectively. Then, its cobalt complex (CoL) was synthesized by reaction of $Co(OAc)_2{\cdot}4H_2O$ with ligand ($H_2L$) in 1:1 molar ratio in ethanol solvent. This ligand and its cobalt complex containing azo functional groups were characterized using elemental analysis, $^1H$-NMR, UV-vis and IR spectroscopies. Subsequently, the interaction between native calf thymus deoxyribonucleic acid (ct-DNA) and CoL complex was investigated in 10 mM Tris/HCl buffer solution, pH = 7 using UV-vis absorption, thermal denaturation technique and viscosity measurements. From spectrophotometric titration experiments, the binding constant of CoL complex with ct-DNA was found to be $(2.4{\pm}0.2){\times}10^4M^{-1}$. The thermodynamic parameters were calculated by van't Hoff equation.The enthalpy and entropy changes were $5753.94{\pm}172.66kcal/mol$ and $43.93{\pm}1.18cal/mol{\cdot}K$ at $25^{\circ}C$, respectively. Thermal denaturation experiments represent the increasing of melting temperature of ct-DNA (about $0.93^{\circ}C$) due to binding of CoL complex. The results indicate that the process is entropy-driven and suggest that hydrophobic interactions are the main driving force for the complex formation.

Nucleotide Sequence Analyses of p10 Gene and its Promoter of Hyphantria cunea Nuclear Polyhedrosis Virus (Hyphantria cunea Nuclear Polyhedrosis Virus p10유전자와 프로모터의 염기서열 결정)

  • Park, Sun-A;Cha, Sung-Chul;Chang, Jae-Hyeok;Lee, Hyung-Hoan
    • The Journal of Korean Society of Virology
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    • v.26 no.1
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    • pp.131-137
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    • 1996
  • The sequences of p10 gene its promoter of Hyphantria cunea NPV were determined. According to the sequence analysis, the putative p10 gene ORF has 285 bp. The 5'-non-coding leader sequence of the p10 gene promoter contained the TATA box and the putative transcription initiation site TAAG motif. Poly (A) tail signals, AATAAA sequence was at site 65 base upstream from the 3' terminus. The deduced amino acid sequence of p10 protein was 95 with a predicted molecular weight of 10.26 kDa. In the p10 protein sequence, a hydrophobic region was present at the N-terminus of the protein, whereas the C-terminus was highly hydrophilic. The p10 protein of H. cunea NPV did not contain cysteine, histidine, trytophan, tryptophane, tyrosine, glutamine and asparagine residues.

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Molecular Cloning and Nucleotide Sequence of Connexin 35 cDNA in the Ovary from the Sweetfish, Plecoglossus altivelis (은어, Plecoglossus altivelis 난소에서 발현하는 Connexin 35 cDNA의 해석)

  • Choi, Cheol-Young;Chang, Young-Jin
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.33 no.6
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    • pp.565-571
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    • 2000
  • Mixed primers based on the high sequence homology of selected regions of known connexins (Cxs) was used for PCR reaction. A full-length connexin cDNA of sweetfish (Plecoglossus altivelis) was cloned by rapid amplification of cDNA 5'and (5'RACE) and 3'RACE method. When compared to other known Cx sequences, homology of sweetfish Cx cDNA to Atlantic croaker, Mycropogonias undulatus Cx32.7, bovine, Bos taurus Cx44 and Atlantic croaker Cx32.2 were $63.8{\%},\;61.6{\%}\;and\;56.7{\%}$, respectively. This cDNA encoded 308 amino acids (35,028 dalton) and named as sweetfish Cx35. Hydropathicity analysis of predicted amino acid sequences indicated that sweetfish Cx35 have four major hydrophobic regions and four major hydrophilic regions, suggesting its topology is similar to that of known Cxs. The presence of a tfical Cx consensus sequences were identified in each of the extracellular loops (first loop and second loop).

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Designing Signal Peptides for Efficient Periplasmic Expression of Human Growth Hormone in Escherichia coli

  • Jeiranikhameneh, Meisam;Moshiri, Farzaneh;Falasafi, Soheil Keyhan;Zomorodipour, Alireza
    • Journal of Microbiology and Biotechnology
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    • v.27 no.11
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    • pp.1999-2009
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    • 2017
  • The secretion efficiency of a protein in a Sec-type secretion system is mainly determined by an N-terminal signal peptide and its combination with its cognate protein. Five signal peptides, namely, two synthetic Sec-type and three Bacillus licheniformis alpha-amylase-derived signal peptides, were compared for periplasmic expression of the human growth hormone (hGH) in E. coli. Based on in silico predictions on the signal peptides' cleavage efficiencies and their corresponding mRNA secondary structures, a number of amino acid substitutions and silent mutations were considered in the modified signal sequences. The two synthetic signal peptides, specifically designed for hGH secretion in E. coli, differ in their N-terminal positively charged residues and hydrophobic region lengths. According to the mRNA secondary structure predictions, combinations of the protein and each of the five signal sequences could lead to different outcomes, especially when accessibility of the initiator ATG and ribosome binding sites were considered. In the experimental stage, the two synthetic signal peptides displayed complete processing and resulted in efficient secretion of the mature hGH in periplasmic regions, as was demonstrated by protein analysis. The three alpha-amylase-derived signal peptides, however, were processed partially from their precursors. Therefore, to achieve efficient secretion of a protein in a heterologous system, designing a specific signal peptide by using a combined approach of optimizations of the mRNA secondary structure and the signal peptide H-domain and cleavage site is recommended.

Effect of Surface Hydrophobicity of Soybean Peptides on the Concentration of Serum Cholesterol and Fecal Steroid Excretion in Rats (대두 펩타이드의 표면소수도가 흰쥐의 혈청 콜레스테롤 농도 및 분변 스테로이드의 배설량에 미치는 영향)

  • Han, Eung-Soo;Lee, Hyong-Joo;Shon, Dong-Hwa
    • Korean Journal of Food Science and Technology
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    • v.25 no.5
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    • pp.571-575
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    • 1993
  • Effect of surface hydrophobicity of soybean peptides on serum cholesterol in rats was investigated. Soybean protein(ISP), casein(CNP), and their peptic hydrolyzates fractionated by acid precipitations (SHT, SH8, SH6, SH4, CHT, CH6, CH5, CH4) were fed to rats and the concentration of serum cholesterol and the fecal steroid excretion were measured. And surface hydrophobicities of the peptide fractions were measured by determining by the ANS flourescence intensity and SDS binding capacity. It was found that the higher the surface hydrophobicity of peptides was, the more the fecal steroids excreted(r=0.801) and the lower the concentration of serum cholesterol became(r=-0.868). However, there was no relationship between SDS surface hydrophobicity and fecal steroids or serum cholesterol. ANS surface hydrophobicity of soybean protein was increased by enzymatic hydrolysis. These results suggest that high surface hydrophobicity of peptides formed during digestion is responsible for the hypocholestrolemic effect of soybean protein through the hydrophobic interaction between the peptides and bile salts in rats.

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Solution Dynamics Studies for the Lck SH2 Domain Complexed with Peptide and Peptide-Free Forms

  • Yoon, Jeong-Hyeok;Chi, Myung-Whan;Yoon, Chang-No;Park, Jongsei
    • Proceedings of the Korean Society of Applied Pharmacology
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    • 1995.04a
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    • pp.81-81
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    • 1995
  • It is well known that Src Homology 2(SH2) domain in many intracellular signal transduction proteins is very important. The domain has about 100 amino acid residues and bind phosphotyrosine-containing peptide with high affinity and specificity. Lck SH2 domain is a Src-like, lymphocyte-specific tyrosine kinase. An 11-residue phosphopeptide derived from the hamster polvoma middle-T antigen, EPQp YEEIPIYL, binds with an 1 nM dissociation constant to Lck SH2 domain. And it is known that the phosphotyrosine and isoleucine residues of the peptide are tightly bound by two well-defined pockets on Lck SH2 domain's surface. To investigate the conformational changes during complexation of SH2 domain with phosphopeptide we have performed the molecular dynamics simulation for Lck SH2 domain with peptide and peptide-free form at look in aqueous solution. More than 3000 water molecules were incorporated to solvate Lck SH2 domain and peptide. Periodic boundary condition has been applied in molecular dynamics simulation. Data analysis with the results of that simulation shows that the phosphopeptide makes primary interaction with the Lck SH2 domain at six central residues, The comparison of the complexed and uncomplexed SH2 domain structures in solution has revealed only relatively small change. But the hydrophilic and hydrophobic pockets in the protein surface show the conformational changes in spite of the small structural difference between the complex and peptide-free forms.

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Synthesis of Resin Derivatives and Purification of Protein - Synthesis of Benzoyl-AH-Sepharose 4B and Purification in Pleurotus cornucopiae(mushroom) - (친화성 고분자 유도체의 합성 및 단백질의 분리정제에 관한 연구 - Benzoyl-AH-Sepharose 4B의 합성 및 흰느타리버섯중 단백질의 분리정제 -)

  • Min, Tae-Jin;Chang, Hung-Bae;Choi, Won-Ki
    • The Korean Journal of Mycology
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    • v.16 no.3
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    • pp.121-127
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    • 1988
  • For selective purification of protein in Pleurotus cornucopiae (Per.) Rolland, affinity chromatography was performed by benzoyl-AH-Sepharose 4B gel synthesized using AH-Sepharose 4B with starting materials. Ligand capacity of benzoyl group was 9.3 micromole per milliliter of gel. Total apparent molecular weight of affinity protein was 255KD, which were protein complex of 29.5, 31.5 34.0, 71.0 and 89.0KD, respectively. The contents of nonpolar, polar, positively charged, and negatively charged amino acid were 45.68%, 26.93%, 11.81% and 15.58%, respectively. The nonpolar protein was selectively purified by hydrophobic ligand of benzoyl group of gel.

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