• Title/Summary/Keyword: covalent-crosslinking

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Review for Immobilization Methods of Biosorbent (생물흡착제의 고정화 방법에 대한 고찰)

  • Jeon, Choong
    • Journal of the Korea Organic Resources Recycling Association
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    • v.19 no.2
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    • pp.16-21
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    • 2011
  • Immobilization of biosorbent is very important for application to real wastewater treatment process because biosorbent itself does not have enough tough structure. Therefore, resent research on heavy metal biosorption using biomass has been focused on its efficient immobilization method. To improve the mechanical strength of freely biosorbent, many immobilization methods have been suggested for applications to the biosorbent such as microorganisms or polysaccharides. In this study, various immobilization methods such as adsorption, covalent binding, entrapment, encapsulation, and crosslinking will be introduced.

Fabrication and Characteristics of Partially Covalent-crosslinked Poly(arylene ether sulfone)s for Use in a Fuel Cell (고분자 전해질 연료전지용 부분 공유 가교된 술폰화 폴리아릴렌에테르술폰 막의 제조 및 특성)

  • Byun, Hong-Sik;Yoon, Kyung-Seok;Choi, Jong-Ho;Choi, Jun-Kyu;Hong, Sung-kwon;Hong, Young-Taik
    • Membrane Journal
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    • v.18 no.4
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    • pp.274-281
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    • 2008
  • Covalent-crosslinked sulfonated poly(arylene ether sulfone) (SPAES) copolymers were synthesized copolymerization technique and additionally crosslinked with divinylbenzene (DVB). To optimize the reaction condition, a concentration of crosslinking agent and a reaction time were varied in the ranges of $30{\sim}90\;v/v%$ and $30{\sim}720\;min$. The properties of the crosslinked membranes were investigated by SEM, TGA and the measurement of proton conductivity. It was found that the proton conductivity of crosslinked membranes decreased depending on a degree of crosslinking while water uptake and methanol permeability reduced.

Stabilization of a Raw-Starch-Digesting Amylase by Multipoint Covalent Attachment on Glutaraldehyde-Activated Amberlite Beads

  • Nwagu, Tochukwu N.;Okolo, Bartho N.;Aoyagi, Hideki
    • Journal of Microbiology and Biotechnology
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    • v.22 no.5
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    • pp.628-636
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    • 2012
  • Raw-starch-digesting enzyme (RSDA) was immobilized on Amberlite beads by conjugation of glutaraldehyde/polyglutaraldehyde (PG)-activated beads or by crosslinking. The effect of immobilization on enzyme stability and catalytic efficiency was evaluated. Immobilization conditions greatly influenced the immobilization efficiency. Optimum pH values shifted from pH 5 to 6 for spontaneous crosslinking and sequential crosslinking, to pH 6-8 for RSDA covalently attached on polyglutaraldehyde-activated Amberlite beads, and to pH 7 for RSDA on glutaraldehyde-activated Amberlite. RSDA on glutaraldehyde-activated Amberlite beads had no loss of activity after 2 h storage at pH 9; enzyme on PG-activated beads lost 9%, whereas soluble enzyme lost 65% of its initial activity. Soluble enzyme lost 50% initial activity after 3 h incubation at $60^{\circ}C$, whereas glutaraldehyde-activated derivative lost only 7.7% initial activity. RSDA derivatives retained over 90% activity after 10 batch reuse at $40^{\circ}C$. The apparent $K_m$ of the enzyme reduced from 0.35 mg/ml to 0.32 mg/ml for RSDA on glutaraldehyde-activated RSDA but increased to 0.42 mg/ml for the PG-activated RSDA derivative. Covalent immobilization on glutaraldehyde Amberlite beads was most stable and promises to address the instability and contamination issues that impede the industrial use of RSDAs. Moreover, the cheap, porous, and non-toxic nature of Amberlite, ease of immobilization, and high yield make it more interesting for the immobilization of this enzyme.

Synthesis of Self-Assembled Peptide Nanoparticles Based on Dityrosine Covalent Bonds (다이타이로신 공유결합으로 자기조립된 펩타이드 나노입자의 합성)

  • Hur, Yun-Mi;Min, Kyoung-Ik
    • Korean Chemical Engineering Research
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    • v.59 no.1
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    • pp.112-117
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    • 2021
  • In this study, a method of self-assembly of peptides based on irreversible covalent bonds was studied by mimicking a biological covalent bond, dityrosine bond. A tyrosine-rich short peptide monomer having the sequence of Tyr-Tyr-Leu-Tyr-Tyr (YYLYY) was selected to achieve a high-density of dityrosine bond. The peptide nanoparticles covalently self-assembled with dityrosine bonds were synthesized by one-step photo-crosslinking of a peptide using a ruthenium catalyst under visible light. The effect of the concentration of each component for the size of the peptide nanoparticle was studied using dynamic light scattering, UV-Vis spectroscopy, and transmission electron microscopy. As a result, the synthesis conditions for size of the peptide nanoparticles ranging from 130 nm to 350 nm were optimized.

Covalent Immobilization of Trypsin on a Novel Aldehyde-Terminated PAMAM Dendrimer

  • Hamidi, Aliasghar;Rashidi, Mohammad R.;Asgari, Davoud;Aghanejad, Ayuob;Davaran, Soodabeh
    • Bulletin of the Korean Chemical Society
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    • v.33 no.7
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    • pp.2181-2186
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    • 2012
  • Dendrimers are a novel class of nonlinear polymers and due to their extensive applications in different fields, called versatile polymers. Polyamidoamine (PAMAM) dendrimers are one of the most important dendrimers that have many applications in nanobiotechnology and industry. Generally aldehyde terminated dendrimers are prepared by activation of amine terminated dendrimers by glutaraldehyde which has two problems, toxicity and possibility of crosslink formation. In this study, novel aldehyde-terminated PAMAM dendrimer was prepared and used for covalent immobilization of trypsin by the aim of finding a special reagent which can prevent crosslinking and deactivation of the enzyme. For this purpose aminoacetaldehydedimethylacetal (AADA) was used as spacer group between aldehyde-terminated PAMAM and trypsin.The findings of this study showed that immobilization of trypsin not only resulted higher optimal temperature, but also increased the thermal stability of the immobilized enzyme in comparison to the free enzyme.

Injectable hydrogels delivering therapeutic agents for disease treatment and tissue engineering

  • Lee, Jin Hyun
    • Biomaterials Research
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    • v.22 no.4
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    • pp.235-248
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    • 2018
  • Background: Injectable hydrogels have been extensively researched for the use as scaffolds or as carriers of therapeutic agents such as drugs, cells, proteins, and bioactive molecules in the treatment of diseases and cancers and the repair and regeneration of tissues. It is because they have the injectability with minimal invasiveness and usability for irregularly shaped sites, in addition to typical advantages of conventional hydrogels such as biocompatibility, permeability to oxygen and nutrient, properties similar to the characteristics of the native extracellular matrix, and porous structure allowing therapeutic agents to be loaded. Main body: In this article, recent studies of injectable hydrogel systems applicable for therapeutic agent delivery, disease/cancer therapy, and tissue engineering have reviewed in terms of the various factors physically and chemically contributing to sol-gel transition via which gels have been formed. The various factors are as follows: several different non-covalent interactions resulting in physical crosslinking (the electrostatic interactions (e.g., the ionic and hydrogen bonds), hydrophobic interactions, ${\pi}$-interactions, and van der Waals forces), in-situ chemical reactions inducing chemical crosslinking (the Diels Alder click reactions, Michael reactions, Schiff base reactions, or enzyme-or photo-mediated reactions), and external stimuli (temperatures, pHs, lights, electric/magnetic fields, ultrasounds, or biomolecular species (e.g., enzyme)). Finally, their applications with accompanying therapeutic agents and notable properties used were reviewed as well. Conclusion: Injectable hydrogels, of which network morphology and properties could be tuned, have shown to control the load and release of therapeutic agents, consequently producing significant therapeutic efficacy. Accordingly, they are believed to be successful and promising biomaterials as scaffolds and carriers of therapeutic agents for disease and cancer therapy and tissue engineering.

Polymeric Humidity Sensor Using Polyelectrolyte Derived from Poly(amide-sulfone)s

  • Jeon, Young-Min;Gong, Myoung-Seon
    • Macromolecular Research
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    • v.17 no.4
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    • pp.227-231
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    • 2009
  • New polyelectrolytes derived from poly(amide-sulfone)s and 1,5-dibromopentane were simultaneously fabricated on the electrode by the crosslinking reaction. The substrate was pretreated with a bromoalkyl-containing, silane-coupling agent to anchor the humidity-sensitive membrane to the substrate through the covalent bond. When the resistance dependence on the relative humidity of the crosslinked poly(amide-sulfone)s was measured, the resistance varied by three orders of magnitude between 20%RH and 90%RH, which was the required RH range for a humidity sensor operating at ambient humidity. Their water durability, long-term stabilities under various environments, hysteresis and response and recovery times were measured and evaluated as a humidity-sensing membrane.

Modification and inactivation of Cu,Zn-superoxide dismutase by the lipid peroxidation product, acrolein

  • Kang, Jung Hoon
    • BMB Reports
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    • v.46 no.11
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    • pp.555-560
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    • 2013
  • Acrolein is the most reactive aldehydic product of lipid peroxidation and is found to be elevated in the brain when oxidative stress is high. The effects of acrolein on the structure and function of human Cu,Zn-superoxide dismutase (SOD) were examined. When Cu,Zn-SOD was incubated with acrolein, the covalent crosslinking of the protein was increased, and the loss of enzymatic activity was increased in a dose-dependent manner. Reactive oxygen species (ROS) scavengers and copper chelators inhibited the acrolein-mediated Cu,Zn-SOD modification and the formation of carbonyl compound. The present study shows that ROS may play a critical role in acrolein-induced Cu,Zn-SOD modification and inactivation. When Cu,Zn-SOD that has been exposed to acrolein was subsequently analyzed by amino acid analysis, serine, histidine, arginine, threonine and lysine residues were particularly sensitive. It is suggested that the modification and inactivation of Cu,Zn-SOD by acrolein could be produced by more oxidative cell environments.

Covalent Interactions of Toluenediisocyanate with DNA and Proteins

  • Jeong, Yo-Chan;Park, Misun;Kim, Dong-Hyun
    • Toxicological Research
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    • v.14 no.4
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    • pp.525-533
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    • 1998
  • The covalent interactions of toluenediisocyanate (TDI) with macromolecules were investigated both in vitro and in vivo. In vitro incubations of 2,4- and 2,6-TDI with DNA or proteins resulted in dose-dependent formation of TDI-protein and TDI-DNA adducts. TDI-treated DNA was highly resistant to enzymatic digestion and thermal hydrolysis, but was readily hydrolyzed under acidic conditions by releasing its corresponding toluenediamine (TDA), suggesting that TDI caused the crosslinking of DNA. Reaction of TDI with albumin and globin resulted in the formation of several adducts, and some adducts were formed in blood of TDI-treated rats in a dose-dependent fashion. Administration of TDI to rats resulted also in a dose-dependent binding of TDI to hepatic tissue. Levels of TDI-albumin adducts were 10 times higher than those of TDI-globin adducts; the biological half lives of TDI-albumin and TDI-globin adducts were 1.2 and 12.5 days, respectively. Globin adducts were detected up to 28 days after the treatment. Hepatic TDI protein adducts were persistent for a substantial period whereas the levels of hepatic TDI-DNA adduct were decreased rapidly. These results indicate that the isocyanato group of TDI is not readily hydrolyzed under physiological conditions, is transported to other organs, and is bound to DNA and/or proteins without further metabolic activation. As the adducted products degrade in the body, TDA is released and introduced to the liver. TDA may additionally bind to hepatic tissue after metabolic activation. Thus, the toxic effect of TDI exposure is considered to persist during the lifetime of the adducted biological macromolecules.

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Oxidative modification of ferritin induced by methylglyoxal

  • An, Sung-Ho;Lee, Myeong-Seon;Kang, Jung-Hoon
    • BMB Reports
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    • v.45 no.3
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    • pp.147-152
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    • 2012
  • Methylglyoxal (MG) was identified as an intermediate in non-enzymatic glycation and increased levels were reported in patients with diabetes. In this study, we evaluated the effects of MG on the modification of ferritin. When ferritin was incubated with MG, covalent crosslinking of the protein increased in a time- and MG dose-dependent manner. Reactive oxygen species (ROS) scavengers, $N-acetyl-_L-cysteine$ and thiourea suppressed the MG-mediated ferritin modification. The formation of dityrosine was observed in MG-mediated ferritin aggregates and ROS scavengers inhibited the formation of dityrosine. During the reaction between ferritin and MG, the generation of ROS was increased as a function of incubation time. These results suggest that ROS may play a role in the modification of ferritin by MG. The reaction between ferritin and MG led to the release of iron ions from the protein. Ferritin exposure to MG resulted in a loss of arginine, histidine and lysine residues. It was assumed that oxidative damage to ferritin caused by MG may induce an increase in the iron content in cells, which is deleterious to cells. This mechanism, in part, may provide an explanation or the deterioration of organs under diabetic conditions.