• Journal of Industrial and Engineering Chemistry
• /
• v.68
• /
• pp.364-371
• /
• 2018

Enzyme polymerization is a benign process exploiting the unique activity of enzymes. In this study, a peroxidase-mimetic catalyst is demonstrated as an alternative to horseradish peroxidase (HRP) for the polymerization of aniline. The mimetic catalyst successfully catalyzes the polymerization of aniline monomers to produce polyaniline (PANI) in an aqueous solution. The PANI produced is rich of para-structure that is generally observed when HRP is used as a catalyst. Compared to HRP, the peroxidase-mimetic catalyst shows a considerably higher catalytic activity at neutral and weak basic conditions (pH >6.5) and at temperatures over $45^{\circ}C$, at which HRP is denatured.

• Journal of Microbiology and Biotechnology
• /
• v.23 no.2
• /
• pp.205-210
• /
• 2013

Thiol-ene polymerization is a versatile tool for several applications. Here we report the preparation of epoxide groups containing thiol-ene photocurable polymeric support and the covalent immobilization of ${\alpha}$-amylase onto these polymeric materials. The morphology of the polymeric support was characterized by scanning electron microscopy (SEM), and energy dispersive spectroscopy (EDS) coupled with SEM was used to explore the chemical composition. The polymeric support and the immobilization of the enzyme were characterized by FTIR analysis. SEM-EDS and FTIR results showed that the enzyme was successfully covalently attached to the polymeric support. The immobilization efficiency and enzyme activity of ${\alpha}$-amylase were examined at various pH (5.0-8.0) and temperature ($30-80^{\circ}C$) values. The storage stability and reusability of immobilized ${\alpha}$-amylase were investigated. The immobilization yield was $276{\pm}1.6$ mg per gram of polymeric support. Enzyme assays demonstrated that the immobilized enzyme exhibited better thermostability than the free one. The storage stability and reusability were improved by the immobilization on this enzyme support. Free enzyme lost its activity completely within 15 days. On the other hand, the immobilized enzyme retained 86.7% of its activity after 30 days. These results confirm that ${\alpha}$-amylase was successfully immobilized and gained a more stable character compared with the free one.

• Journal of Sericultural and Entomological Science
• /
• v.42 no.2
• /
• pp.104-108
• /
• 2000

To hydrolyze insolule sericin the enzyme hydrolysis was used, and then obtained the results as given belows. When insoluble sericin was hydrolyzed by enzyme treatment, the solubility was best at pH 7, 60$\^{C}$ and was slightly increased both above 2 hours treatment and above 10% of enzyme concentration. As the results of electrophoresis, the distribution of molecular weight of sericin powder obtained by enzyme hydrolysis was very weak and showed in the wide range having no distinguishable band. Average degree of polymerzations (A.D.P.) of sericin hydrolyzed by enzyme were about 4.1∼6.3, average molecular weight were about 470∼730. The whiteness of the sericin powder obtained by enzyme hydrolysis was high and increased slightly with higher treatment concentration of enzyme. As the results of amino acid analysis, the amino acid analysis, the amino acid composition of the sericin powder from the enzyme treatment were similar to which located at near 230$\^{C}$ and 320$\^{C}$. The peak of near 230$\^{C}$ could not been found in the sericin powder obtained by enzyme hydrolysis.

• Archives of Pharmacal Research
• /
• v.26 no.10
• /
• pp.826-831
• /
• 2003

ADP-ribose pyrophosphatase (ADPRase) hydrolyzes ADP-ribose (ADPR) into AMP and ribose-5'-phosphate. It is classified into two groups, $Mg^{2+}$-dependent and $Mg^{2+}$-independent ADPRase, depending on its $Mg^{2+}$requirement. Here, we purified $Mg^{2+}$-dependent ADPRase from rabbit liver and examined what factors affect $Mg^{2+}$ requirement. The purified enzyme showed a single band with the molecular weight of 34 kDa on SDS-PAGE both in the presence and absence of 2-mercaptoethanol. The molecular weight of the native enzyme calculated by gel filtration was 68 kDa, indicating that ADPRase is a dimer made up of two identical subunits. $Mg^{2+}$-dependent ADPRase with the highest ADPR affinity had a $K_m$ of 160$\pm$10 $\mu$M and a pH optimum of around pH 9.5. Treatment of the purified ADPRase with heated cytosol fractions at 37$^{\circ}C$ for 3 h caused some changes in the chemical properties of the enzyme, including an increase in molecular weight, a decrease in solubility, and a loss of $Mg^{2+}$-dependency. The molecular weight of the cytosol-treated ADPRase measured by gel filtration was over 420 kDa, suggesting, for the first time, that ADPRase could be polymerized by undefined cytoplasmic factors, and that polymerization is accompanied by changes in the solubility and metal ion dependency of the enzyme.

• Bulletin of the Korean Chemical Society
• /
• v.33 no.12
• /
• pp.4122-4126
• /
• 2012

Cellulose-graft-poly (L-lactide) (cellulose-g-PLLA) was successfully prepared via ring-opening polymerization (ROP) by using 4-dimethylaminopyridine (DMAP) as an organic catalyst in an ionic liquid 1-allyl-3-methylimidazolium chloride (AmimCl). The structure and morphology of the polymer was characterized by nuclear magnetic resonance (NMR) and transmission electron microscope (TEM). From wide-angle X-ray powder diffraction (WAXD) and degradation test (by acid, alkaline, PBS and enzyme solution), changes in the crystalline structure as a result of degradation was also investigated. The results indicated that materials which have low degree of crystallinity showing higher degradability, however, in acid liquor, enzyme solution, alkaline liquor and PBS system, the degradation rate of the polymer decreased by the above sequence. Moreover, with the further increase of graft degree of this material, its degradation degree decreased.

• Proceedings of the Korea Technical Association of the Pulp and Paper Industry Conference
• /
• 2008.04a
• /
• pp.177-177
• /
• 2008

• Korean Journal of Food Science and Technology
• /
• v.28 no.1
• /
• pp.146-151
• /
• 1996

For the purpose of production of oligosaccharides from alginates, a bacterium was isolated from seaweed, and then an enzyme which degraded alginates was obtained from the bacterium. A specific activity of the enzyme was shown in G-rich block and Na-alginate (Wako Co.) as a result of reaction between the enzyme and six types of alginates (G-rich block, M-rich block and 4 commercial Na-alginate). Degradation products were prepared from the Na-alginate (Wako Co.) by the enzyme. The oligosaccharides were fractioned by Sephadex G-25 and Bio-gel P-2 and identified on a thin layer chromatography (TLC). Degree of polymerization (DP) of the oligosaccharides was shown from 2.6 to 7.5.

• Proceedings of the Korean Institute of Electrical and Electronic Material Engineers Conference
• /
• 2000.07a
• /
• pp.909-912
• /
• 2000

We synthesized polypyrrole (PPy) nanotubules by oxidative polymerization of the pyrrole monomer within the pores of a polycarbonate template. The electrochemical behavior was investigated using cyclic voltammetry. The redox potential was about -0.5 V vs. Ag/AgCl reference electrode, while the potential was about 0 V for PPy film. It is considered as the backbone grows according to the pore wall. Therefore, it is possible to be arranged regularly. That leads to improvement in the electron hopping. By electrochemical doping of glucose oxidase (GOx) on PPy nanotubules, an enzyme electrode has been fabricated. The kinetic parameter of biochemical reaction with glucose was evaluated. The formal Michaelis constant and maximum current calculated by computer were about 11.4 mmol $dm^3$ and 170.85 A respectively. Obviously, an affinity for the substrate and current response of the PPy nanotubules enzyme electrode are rather good, comparing with that of PPy film.

• Elastomers and Composites
• /
• v.43 no.4
• /
• pp.221-229
• /
• 2008

Starch as matrix polymer was used to do graft copolymerization with 2-ethylhexylacrylate, methyl methacrylate and acrylic acid. The polymerization was carried out by radical emulsion polymerization with increasing contents of starch. When 0.174% of $\alpha$-amylase as enzyme for starch was added, it was found that it made the best stable emulsion. The glass transion temperature of the polymerized material was increased with starch contents. The particle size and viscosity of the emulsion increased with starch contents due to the increased hydroxy group. Peel strength also increased with contents of starch because the enhanced hydroxy group caused to increase affinity between substrate surface and polymer materials. However, the initial tackiness decreased with starch contents owing to film hardness by higher glass transion temperature.

• Journal of Korean Ophthalmic Optics Society
• /
• v.20 no.1
• /
• pp.75-81
• /
• 2015

Purpose: The present study was conducted to investigate whether the changes in structure and activity of antioxidative enzymes, superoxide dismutase(SOD) and catalase(CAT) present in the eyes appeared when they were repeatedly exposed to UV-A, and reveal the correlation of these changes. Methods: Each enzyme solution was prepared from the standardized SOD and CAT, and repeatedly exposed to UV-A of 365 min under the condition of 30 minutes, 1 hour and 2 hours a day over 1, 2, 3, 4 and 5 days. Structural denaturation of SOD and CAT induced by repeat UV-A irradiation was confirmed by the electrophoretic analysis, and their enzyme activity was determined by the colorimetric assay using the proper assay kit. Results: SOD exposed repeatedly to UV-A showed the polymerization pattern through the electrophoretic analysis when it was repeatedly exposed under the condition of at least 1 hour a day however, the change of its activity was found to be less than 12%. On the other hand, CAT repeatedly exposed to UV-A showed reduced size of the electrophoretic band which indicated a structure denaturation and its activity was significantly decreased. In the case of that the repeat exposure time was longer, CAT activity was completely lost even though some enzyme band was shown in the electrphoretic analysis. Conclusions: From these results, it was revealed that the degree and pattern in structural denaturation of antioxidative enzymes differently appeared according to the type of enzyme, and the degree of structural denaturation was not always consistent with the reduction in enzyme activity.