• Microbiology and Biotechnology Letters
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• v.23 no.4
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• pp.425-431
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• 1995

A kinetic model of the cyclodextrin formation in a heterogeneous enzyme reaction system using swollen extrusion starch as substrate was derived emphasing the structural features of extrusion starch. The degree of gelatinization, the ratio of accessible and inaccessible portion of extrusion starch, adsorption of CGTase on swollen starch, the structural transformation during reaction, and product inhibition caused by produced CDs were considered in deriving kinetic model. Various kinetic constants were also evaluated. The derived kinetic equation was numerically simulated, which result showed that the derived kinetic equations can be used to predict the experimental data reasonably well under the various experimental conditions. Kinetic model can be utilized for the optimization of enzyme reactor and the process development for CD production from swollen extrusion starch.

• 한국신재생에너지학회:학술대회논문집
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• 2009.06a
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• pp.749-752
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• 2009

Anodized tubular titania ($TiO_2$) electrodes (ATTEs) are prepared and used as both the photoanode and the cathode substrate in a photoelectrochemical system designed to split water into hydrogen with the assistance of an enzyme and an external bias (solar cell). In particular, the ATTE used as the cathode substrate for the immobilization of the enzyme is prepared by two methods; adsorption and crosslinking. Results show that the optimized amount of enzyme is 10.98 units for the slurried enzyme, 3.66 units for the adsorbed one and 7.32 units for the crosslinked one, and the corresponding hydrogen evolution rates are 33.04, 148.58, and 234.88 umol/hr, respectively. The immobilized enzyme, specifically the chemically crosslinked one, seems to be much superior to the slurried enzyme, due to the enhanced charge-transfer process that is caused by the lower electrical resistance between the enzyme and the ATTE. This results in a greater number of accepted electrons and a larger amount of enzymes able to deal with the electrons.

• Journal of Microbiology and Biotechnology
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• v.20 no.2
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• pp.332-339
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• 2010

The lipase from Mucor racemosus NRRL 3631 was partially purified by fractional precipitation using 60% ammonium sulfate, which resulted in a 8.33-fold purification. The partially purified lipase was then immobilized using different immobilization techniques: physical adsorption, ionic binding, and entrapment. Entrapment in a 4% agar proved to be the most suitable technique (82% yield), as the immobilized lipase was more stable at acidic and alkaline pHs than the free enzyme, plus 100% of the original activity was retained owing to the thermal stability of the immobilized enzyme after heat treatment for 60 min at $45^{\circ}C$. The calculated half-lives (472.5, 433.12, and 268.5 min at 50, 55, and $60^{\circ}C$, respectively) and the activation energy (9.85 kcal/mol) for the immobilized enzyme were higher than those for the free enzyme. Under the selected conditions, the immobilized enzyme had a higher $K_m$ (11.11 mM) and lower $V_{max}$ (105.26 U/mg protein) when compared with the free enzyme (8.33 mM and 125.0 U/mg protein, respectively). The operational stability of the biocatalyst was tested for both the hydrolysis of triglycerides and esterification of fatty acids with glycerol. After 4 cycles, the immobilized lipase retained approximately 50% and 80% of its original activity in the hydrolysis and esterification reactions, respectively.

• Journal of the Korean Chemical Society
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• v.40 no.1
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• pp.72-80
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• 1996

A chitinase-producing bacterium, Serratia marcescens JM, was isolated from a seashore muds. A chitinase was purified by ammonium sulfate precipitation, affinity adsorption, hydroxylapatite and sephadex G-200 column chromatography. The chitinase obtained from Serratia marcescens JM was purified 42.2 folds with the overall yield of 7.1%. The purified chitinase showed a single band on sodium dodecyl sulfate polyacrylamide gel electrophoresis. The molecular weight of the enzyme was 59,000 and the apparent kinetic parameters $K_m\;and\;V_{max}$ for the purified chitinase were 5.17 mg/mL and 39.8 unit/mL, respectively. The optimum pH and temperature of the purified chitinase were 7.0 and 50$^{\circ}C$, respectively and the purified enzyme was stable on pH 7.0 up to 50$^{\circ}C$. The enzyme were activated by $Cu^{2+},\;Ca^{2+}\;and\;Mg^{2+}$ and inhibited by $Hg^{2+}$ respectively. In addition, Cysteine increased the chitinase activity and EDTA, MIA, PCMB and SDS inhibited enzyme activities. Major cations, $MG^{2+},\;Ca^{2+},\;K^+\;and\; Na^+$ present in seawater slightly stimulated the chitinase activity.

• KSBB Journal
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• v.16 no.2
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• pp.128-132
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• 2001

Cyclodextrin glucanotransferase (EC 2.4.1.19 : 1,4-$alpha$-glucan 4-$alpha$-D-(1,4-glucano) transferase, cyclizing; CGTase) was recovered by starch adsorption. The adsorption and desorption of CGTase to starch was studied as a function of pH, temperature, and starch type. The optimal pH, temperature, and starch for adsorption were, 8.0, $4^{circ}C$, and 1% (w/v) corn starch, respectively, per 205 U/mL enzyme activity in the presence of 25% (w/v) ammonium sulfate. The maximum adsorption ratio was 95%. On the other hand, the optimal pH, temperature, and starch type for desorption were 8.0 (tris-buffer), $50^{circ}C$, and oxidized starch, respectively. The maximum desorption ratio was 98% by tris-buffer solution at pH 8.0. The efficiency of adsorption and desorption were affected slightly by the removal of cells from the fermentation broth.

• 한국생물공학회:학술대회논문집
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• 2005.04a
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• pp.566-569
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• 2005

The extracellular polysaccharide...(EPS) has been used in a wide variety of industrial applications because of gel formation, emulsion stability, control of the surface tension, water absorption and film formation etc. In this study, inhibitory activity on tyrosinase and inhibitory activity on angiotensin converting enzyme...(ACE) are determined. UV adsorption wavelength, beads formation of EPS were investigated. In the result, in 1%(w/v) EPS concentration, EPS had inhibitory activity of 71.8% on tyrosinase and inhibitory activity of 61.5% on angiotensin converting enzyme in 1.5% EPS concentration. Adsorption wavelength of EPS was UV-B,C . Beads based on EPS were prepared by w/o emulsion method and the shape of EPS beads observed by SEM was spherical and uniform.

• Textile Coloration and Finishing
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• v.14 no.1
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• pp.18-26
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• 2002

Chitosan has reactive amino and hydroxyl groups which can be used to chemically alter its properties under the mild reaction conditions. Thus the cationization of Tencel with Chitosan is effective to modify the fabric. To investigate the modified properties of Tencel fabric, the tests were performed under the several finishing process with enzyme/glutaraldehyde/softener. The internal structure of Tencel which has the structure of cellulose II wasn't changed by enzyme, chitosan and crosslinking agent treatment and the thermal stability was improved by chitosan and crosslinking agent treatment. Wrinkle recovery angle under the dry condition increased highly until $0.1\textrm{mol}/\ell$ of glutaraldehyde concentration, and then decreased. Tensile strength of modified Tencel fabric decreased with increasing of weight loss, but it was improved more or less by chitosan, crosslinking agent and softener. Moisture regain was improved by enzyme and chitosan treatment. And antibacterial activity showed nearly 100% on Tencel fabric treated with 0.5% chitosan and adsorption of metal ion increased with increasing of chitosan concentration.

• Microbiology and Biotechnology Letters
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• v.23 no.4
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• pp.416-424
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• 1995

Mechanism of the cyclodextrin (CD) production reaction by cyclodextrin glucanotransferase (CGTase) using swollen extrusion starch as substrate was investigated emphasizing the structural features of starch granule. The degree of gelatinization was identified to be the most representative structural characteristic of swollen starch. The most suitable degree of gelatinization of swollen starch for CD production was around 63.52%. The structural transformation of starch granule during enzyme reaction was also followed by measuring the changes of the degree of gelatinization, microcrystallinity, and accessible and inaccessible portion to CGTase action of residual swollen starch. The adsorption phenomenon of CGTase to swollen starch was also examined under various conditions. The inhibition mechanism of CGTase by various CDs was identified to be competitive, most severely by a-CD. The mechanism elucidated will be used for development of a kinetic model describes CD production reaction in heterogeneous enzyme reaction system utilizing swollen extrusion starch.

• Journal of Pharmaceutical Investigation
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• v.19 no.4
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• pp.203-212
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• 1989

A proteolytic enzyme was extracted from Sarcodon aspratus (Berk) S. Ito by percolation method. Proteolytic activity of the extracted proteolytic enzyme (SAP) was compared with several digestives containing proteolytic enzymes. Potency of SAP was higher than that of the other digestives except for protease. The optimum pH ranse of SAP was similar to that of pancveatin and protease. SAP was more stable than pancreatin and protease under various temperature, alkaline pH, and metal ions. Bovine serum albumin hydrolysing activity of SAP was equivalent to that of pancreatin and protease in small intestine of rats. SAP demonstrated lower adsorption to antacids than pancreatin and protease. Among the mixtures of SAP and several antacids, magnesium oxide-SAP showed the highest proteolytic activity.

• Microbiology and Biotechnology Letters
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• v.23 no.2
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• pp.187-196
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• 1995

In order to produce fuctional chitooligosaccharides, a strain excreting mainly endo-type chitinase suitable for chitooligosaccharides production was newly screened and identified as Aspergillus fumigatus JC-19. The chitinase excretion was repressed in nutrient rich medium but stimulated by colloidal chitin indicating that the chitinase is inducible type enzyme. Maximum secretion of the enzyme was observed at pH 7.0 and 37$\circ$C . The growth and chitinase production patterns of Aspergillus fumigatus JC-19 showed that the cell growth reached maximum after 4-5 days with final chitinase concentration of 0.46 unit per ml. Excreted chitinase was purified by ammonium sulfate precipitation, colloidal chitin adsorption, anion exchange chromatography, and gel filtration, respectively, and measured M.W of 50 KDa. The enzyme reaction carried out both by crude and purified chitinase showed that the purified chitinase accumulated more chitooligosaccharides of 1-6 degree of polymerization than that of crude chitinase.