• Fisheries and Aquatic Sciences
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• v.13 no.1
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• pp.36-48
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• 2010

An agar-degrading Agarivorans sp. AG17 strain was isolated from the red seaweed Grateloupia filicina collected from Jeju Island. A beta-agarase gene from Agarivorans sp. AG17 was cloned and designated as agrA. agrA has a 2,985 bp coding region encoding 995 amino acids and was classified into the glycoside hydrolase family (GHF)-50. Predicted molecular mass of the mature protein was 105 kDa. His-tagged agrA was overexpressed in Escherichia coli and purified as a fusion protein. The enzyme showed 158.8 unit/mg specific activity (optimum temperature at $65^{\circ}C$ and pH 5.5 in acetate buffer) with unique biochemical properties (high thermal and pH stabilities). Enzyme produced neoagarohexaose, neoagarotetraose and neoagarobiose by degrading agar, and hydrolyzed neoagaro-oligosaccharides were biologically active. Hence the purified enzyme has potential for use in industrial applications such as the development of cosmetics and pharmaceuticals.

• Journal of the Korean Society of Food Science and Nutrition
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• v.28 no.2
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• pp.371-377
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• 1999

In order to evaluate the antimicrobial function of natural herb extracts as antimicrobial agent or packaging material for the preservation of foods and greenhouse produce, the water extract of chopi (Zanthoxylum piperitum DC.) was prepared and its antimicobial activity was determined. In the paper disk test its antimicrobial activity was increased in proportion to its concentraion. The growth of microorganisms was completely inhibited above 500ppm of its concentration. It showed wide spectrum of thermal(40 to 180oC) and pH(4 to 10) stabilities. In the electronic microscopic observation(TEM and SEM) of microbial morphological change it showed to decrease the activation of physiological enzymes and to lose the function of cell membranes. Even in the activation test of galactosidase, it seemed to weaken the osmotic function of cell membranes remarkably in comparison with chloroform and its activation corresponded to 40~50% of toluene. Zanthoxylum piperitum DC. extract seemed to be an excellent antimicrobial for the inhibition of food borne microorganisms as well as the pre servation of greenhouse produces.

• Bulletin of the Korean Chemical Society
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• v.6 no.4
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• pp.210-214
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• 1985

Urokinase, a plasminogen activator, was conjugated with dextran by the cyanogen bromide activation-coupling method. The resulting water-soluble conjugate was purified by gel permeation chromatography on Sephadex G-200. The maximal activity was obtained when the ratio of urokinase/dextran was 1/20 for the coupling. The final preparation showed 5 CTA units/mg conjugate, 300 CTA units/mg protein, 8.4 % activity retention, and 47 % protein retention. The urokinase-dextran conjugate had good thermal, pH and storage stabilities. In addition, it showed greater resistance to the inhibitory effect of human plasma than native urokinase. Also in vitro biological half-life of urokinase increased 40 times by this conjugation. In view of activity, excellent stability and increased half-life, the conjugate can be a potential fibrinolytic agent in an injectable form.

• Food Science and Preservation
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• v.16 no.3
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• pp.392-399
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• 2009

Recent studies indicate that green tea may have anticancer, antioxidant, and antihypertensive effects, and aids body weight control and the promotion of various desirable physiological functions. However, few studies have investigated the antimicrobial effects of green tea. We sought to determine the antimicrobial activity of green tea extract against food spoilage microorganisms. The extract showed remarkable antimicrobial effects against a wide spectrum of putrefactive and food spoilage microorganisms when used at concentrations greater than $500{\mu}g/ml$. The extract showed thermal and pH stability in the range of $40{\sim}150^{\circ}C$ and pH 3.11, respectively. Green tea extract seems to be an ideal natural antimicrobial, considering both efficacy and thermal and pH stabilities. Antimicrobial substances in green tea extract were investigated using electron microscopy and a $\beta$-galactosidase assay. The data showed that the extract contains several efficacious materials, and that their activities are not synergistic but are instead independent. Our data indicate that hydrophilic antimicrobial substances in green tea extract might control food spoilage microorganisms owing to perturbation of the microbial cell membrane.

• Applied Chemistry for Engineering
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• v.25 no.6
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• pp.624-631
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• 2014

In this study, a new series of conjugated polymer 3-(5-(5,6-bis(octyloxy)-7-(thiophen-2-yl)benzo[c][1,2,5]thiadiazol-4-yl)thiophen-2-yl)-10-(4-(octyloxy)phenyl)-10H-phenothiazine (P1) and 3-(5-(5,6-bis(octyloxy)-7-(thiophen-2-yl)benzo[c][1,2,5]thiadiazol-4-yl)thiophen-2-yl)-10-(4-((2-ethylhexyl)oxy)phenyl)-10H-phenothiazine (P2) were synthesised and organic photovoltaics (OPVs) properties were characterized. The push-pull structure polymer consisted of phenothiazine derivative as an electron donor and benzothiadiazole derivative as an electron acceptor. The aliphatic chain substituted aromatic ring was substituted at the position of N in phenothiazine for the electron-rich and improved solubility. Excellent thermal stabilities of P1 and P2 were confirmed by measured Td values as 321.9 and $323.7^{\circ}C$, respectively and the degrees of polymerization were 4,911 (P1) and 5,294 (P2). The maximum absorption wavelength of P1 and P2 were 549 and 566 nm, respectively. The device was fabricated and the OPVs property was measured. As a result, the power efficiency of conversion for P1 and P2 were 0.96 and 0.90%, respectively.

• KSBB Journal
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• v.17 no.2
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• pp.189-194
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• 2002

Laccase produced from Trametes sp. was immobilized on CNBr-activated Sepharose-4B (CAS4B) and tested for degradation of azo dyes. Laccase was efficiently immobilized on CAS4B. Immobilization of laccase on CAS4B increased pH, thermal and proteolytic stabilities. Optimum pH and temperature of immobilized laccase were pH 3 and 40$\^{C}$, respectively as same as those of free laccase. The K$\_$m/($\mu$mol/ml) values of free and immobilized laccase for Reactive Blue 19 as the substrate were 0.34 and 2.07, respectively V$\_$max/($\mu$mol/mL$.$min) values of them were 0.12 and 0.1, respectively. In repeated batch reactions, conditions retained high stability and degradation of dye for immobilized laccase were pH 5 and 30$\^{C}$. HBT didn\\`t decrease highly activity of immobilized laccase. Immobilized laccase was very stable for degrading dyes continuously in a packed-bed reactor containing laccase immobilized on CAS4B. For continuous degradation of 100 $\mu$M Reactive Blue 19 and 50 $\mu$M Acid Red 57 in the presence of 0.1 mM HBT under optimum conditions, immobilized laccase retained 70% of degradation ability even after 30 hours.

• Journal of Life Science
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• v.20 no.11
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• pp.1589-1594
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• 2010

Glutaraldehyde was used to cross-link chitosan beads to immobilize the crude enzyme $\beta$-glucosidase from Exiguobacterium sp. DAU5. The conditions for preparing cross-linking chitosan beads and immobilization such as concentration of glutaradehyde, cross-linking time, immobilization pH and time were optimized. The chitosan beads were cross-linked with 1.5% glutaraldehyde for 1.5 hr. The immobilized $\beta$-glucosidase had an overall yield of 20% and specific activity of 5.22 U/g. The optimized pH and temperature were 9.0 and $55^{\circ}C$, respectively. More than 80% of its activity at pH 7.0-10.0, 80% at $40^{\circ}C$ for 2 hr and 48% at $50^{\circ}C$ for 1 hr, were retained. However, the immobilization product showed higher pH and thermal stabilities than free enzymes. It also showed high hydrolyzing activity on soybean isoflavone glycoside linkage. These results suggest the broad application prospects of immobilization enzymes.

• Journal of Applied Biological Chemistry
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• v.53 no.4
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• pp.195-201
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• 2010

A gene encoding an alanine racemase in B. pseudomycoides was cloned and one (Cys316) or both of two cysteines (Cys316 and Cys365) was (were) substituted with alanine. The cysteine (-) alanine racemases were expressed in E. coli BL21 (DE3) using a pET-21 vector. The expressed enzymes were purified through affinity chromatography using 6xHis ligand. The purified enzymes all showed major one bands by SDS-PAGE analysis, corresponding to 46 kDa. The cysteine (-) alanine racemases as well as the wild type enzyme showed alanine racemase activities, indicating that the enzyme is an alanine racemase and the cysteines in the enzyme may not be involved in the catalysis and/or substrate binding. Thermal stabilities of Cys (-) alanine racemases decreased considerably and half-lives were 26 (wild type), 21 (C316A) and 18 min (C316-365A), respectively at $60^{\circ}C$ pH 8.0, suggesting that cysteine is considerably contributive to the thermal stability of the alanine racemase.

• Journal of the Korean Society of Food Science and Nutrition
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• v.30 no.6
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• pp.1147-1151
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• 2001

We investigated stabilities of blue pigment extracted from Gardenia jasminoides at various conditions to check its applicability for beverages. Gardenia blue pigment with maximum absorption at 587 nm was obtained from the reaction of glycine and genipin (aglycone of geniposide). The blue pigment was found to be relatively unstable at acidic pH but very stable at alkaline conditions with half-life values of 102 days and 126 days at PH 9.0 and PH 11.0, respectively. The pigment also showed high thermal stability with half-life value of 55, 18, and 2 days at 50, 70, and 9$0^{\circ}C$, respectively. The addition of inorganic ions, sugars, and amino acids to model beverage containing this blue pigment increased retention rate at room temperature while addition of vitamin C decreased the stability. The sensory evaluation of the model beverage showed that inorganic ions and amino acids increased overall acceptability, indicating that the blue pigments of Gardenia jasminoides can be used as a natural colorant for leverage.

• Archives of Pharmacal Research
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• v.3 no.1
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• pp.7-12
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• 1980

Ampliciline was synthesized from 6-amino-pencillanic acid (6-APA) and D-.alpha. phenylglycine methyl ester by using amplicilin synthesizing enzyme from Peudomonas melanogenum (IAM 1655). The whole cell enzyme was immobilized by entrapping it in the polyacrylamide gel lattices. The polymer used in the enzyme entrapment was made from 150 mg per ml of acrylamide monomer and 8 mg per ml of N, N'-methylenebisacrylamide. About 200 mg/whole cell enzyme was mixed in the polymer for entrapment. The maximal activity retention after immobilization was 56%. The optimal pH values for the whole cell enzyme and the immobilized whole cell enzyme were 6.0 and 5.9, respectively. The optimal temperature for the enzyme activity were the same for both type of preparations. The enzyme stabilities against pH and heat increased for immobilized whole cell enzyme. Immobilized cell was more stable especially in the acidic condition while both type were found to be very suceptible to thermal inactivation at a temperature above 4.deg.C. The kinetic constants obtained from Lineweaver-Burk plot based on two substate reaction mechanism showed somewhat higher value for immobilized whole cell enzyme as compared to the whole cell enzyme : the Km value for 6-APA were 7.0 mM and 12.5 mM while Km values for phenylglycine methyl ester were 4.5 mM and 8.2 mM, respectively. Using the immobilized whole cell enzyme packed in a column reactor, the productivity of ampiciline was studied by varying the flow rate of substrate solution. At the space velocity, SV, 0.14 hr$^{-1}$ the conversion was 45%. Operational stability found in terms of half life was 30 hr at SV = 0.2 hr.