• 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.

• Textile Coloration and Finishing
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• v.30 no.4
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• pp.264-274
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• 2018

Immobilization of lysozyme on chitosan non-woven using glutaraldehyde(GA) was investigated. For this, 100 % chitosan non-woven was prepared as novel support for the enzyme immobilization. In addition, free lysozyme activity was examined depending on various pH and temperature by measuring time. Moreover, the optimum immobilization conditions depending on various pH, temperature, immobilization time and lysozyme concentration was evaluated. In addition, thermal stability and storage stability of immobilized lysozyme were measured. The characteristics of immobilized lysozyme was examined by FT-IR, surface morphology, and MTT assay. The results are follows: the optimal immobilization of lysozyme were pH 7.0, $25^{\circ}C$, lysozyme concentration 1.5 mg/ml, immobilization time 240 min. The immobilized lysozyme showed higher thermal stability than the free trypsin. The immobilized lysozyme activity was retained 80 % of its initial activity at $4^{\circ}C$ over 30 days of storage. The lysozyme was immobilized effectively on chitosan non-woven by observation of surface morphology.

• Archives of Pharmacal Research
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• v.29 no.12
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• pp.1179-1186
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• 2006

Cross-linked starch microspheres were prepared using different kinds of cross-linking agents. The influence of several parameters on morphology, size, swelling ratio and drug release rate from these microspheres were evaluated. These parameters included cross-linker type, concentration and the duration of cross-linking reaction. Microspheres cross-linked with glutaraldehyde had smooth surface compared with those prepared with epichlorhydrine or formaldehyde. The particle size increased with increasing the cross-linking time and increasing the drug loading. Swelling ratio of the particles was a function of cross-linker type but not the concentration or time of cross-linking. Drug release from starch microspheres was measured in phosphate buffer and also in phosphate buffer containing a-amylase. Results showed that microspheres cross-linked with epichlorhydrine released all their drug content in the first 30 minutes. However, cross-linking of the starch microspheres with glutaraldehyde or formaldehyde decreased drug release rate. SEM and drug release studies showed that cross-linked starch microspheres were susceptible to the enzymatic degradation under the influence of alpha-amylase. Changing the enzyme concentration from 5000 to 10,000 IU/L, increased drug release rate but higher concentration of enzyme (20,000 IU/L) caused no more acceleration.

• KSBB Journal
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• v.5 no.2
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• pp.141-149
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• 1990

$\beta$-glucosidase derived from Aspergillus niger was immobilized by (1) covalent linkage on chitin and chitosan with glutaraldehyde, (2) adsorption on DEAE-cellulose and Amberite IRA93 after succinylation, and (3) entrapment on alginate and polyacrylamide gels with various cross linking agents. The retention yield of $\beta$-glucosidase immobilized on chitosan was 31.5% and operational stability was 69% after continuous operation at column reactor(5$0^{\circ}C$ at pH 4.8) for 15 days. The retention yield and operational stability were 24.7% and 60% respectively, in adsorption on Amberite IRA 93. On the other hand, the entrapment method by alginate and polyacrylamide gel was identified to be not appropriate due to the continuous elution of inlmobilized $\beta$-glucosidase. Optimum conditions for the immobilization on chitosan were also studied with optimum pH of 4.8 and glutaraldehyde concentration of 0.4%(w/v). The properties and stability of immobilized $\beta$-glucosidase are also investigted. The conversion yield of cellobiose to glucose was also analyzed using the column type enzyme reactor to evaluate the effectiveness of immobilized enzyme.

• Journal of Pharmaceutical Investigation
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• v.25 no.1
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• pp.37-46
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• 1995

The experiment was designed to investigate the sustained release dosage form of silymarin (SL) from chitosan (CS) carrier. Solid dispersed system was prepared by mixing the drug with chitosan. This solid dispersed system was cross-linked by glutaraldehyde, formaldehyde, acetaldehyde and butylaldehyde, respectively. The dissolution rates of these preparations were compared with each other in vitro. The silymarin was mired with anionic alginate gel and bead was prepared by dropping this mixture to cationic chitosan solution including calcium chloride. Chitosan encapsulated alginate bead after drying in the oven was investigated for the dissolution rate. The dissolution rate of SL-CS mixture was delayed with increase in the amounts of CS and the concentration of aldehyde. The effect on the delay of dissolution rate was in the increasing order of formaldehyde, glutaraldehyde, acetaldehyde, butylaldehyde. The dissolution rate of chitosan encapsulated alginate bead was parallel with the concentration of chitosan in diluted hydrochloric acid solution and delayed with increase in the concentration of chitosan in phosphate buffer solution.

• Journal of Sericultural and Entomological Science
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• v.37 no.2
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• pp.137-141
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• 1995

The sericin fixation of raw silk by glutaraldehyde solutions with catalyst(serifix B) was done and the effect of sericin fixation by catalyst on reaction mechanism, whiteness and physical properties were investigated and discussed. The obtained results were summarized as follows; 1) The complete sericin fixation were obtained by glutaraldyhyde solution regardless the concentration of catalyst. 2) The tenacities of sericin fixed silk increased in comparison with that of nontreated silk. 3) There were not constant tendency in elongation of sericin fixed silk in comparison with nontreated silk. 4) The whiteness of sericin fixed silk treated glutaral-silk in comparison with nontreated silk. 5) FT-IR spectra were quite different from sericin fixed reagent and catalyst.

• Membrane Journal
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• v.23 no.2
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• pp.170-175
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• 2013

Poly (vinyl alcohol) (PVA) solution containing the glutaraldehyde (GA) as a crosslinking agent was coated onto the polyacrylonitrile (PAN) hollow fiber membrane as the supporter. Pervaporation experiments were carried out to characterize the prepared PVA/PAN composite membrane for water-isopropyl alcohol mixture. The flux and separation factor were measured at 30, 50, $90^{\circ}C$ for the feed mixture of aqueous 85 wt% IPA solution with varying the reaction temperature and composition of coating solutions. Typically the flux showed 1,870 $g/m^2{\cdot}hr$ at $90^{\circ}C$ feed mixture and the coating concentration of 3.5 wt% and the highest separation factor of 804 was obtained at $30^{\circ}C$ feed mixture and the coating concentration of 7 wt% as well.

• Advances in Traditional Medicine
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• v.5 no.1
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• pp.43-47
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• 2005

Jack bean urease was immobilized on gelatin beads with the help of glutaraldehyde. The optimum immobilization (67.6%) was obtained at 30mg/ml gelatin concentration, 0.5 mg/bead enzyme protein concentration, 1 % glutaraldehyde and at $4^{\circ}C$ incubation temperature. The $t_{1/2}$ of immobilized urease was approximately 90 days at $4^{\circ}C$ compared with $t_{1/2}$ of 20 days for the soluble urease, under identical condition. The apparent optimum pH shifted from 7.3 to 8.0 when the urease was immobilized. The optimum stability temperature of immobilized urease was found to be $60^{\circ}C$ while that of soluble urease was $45^{\circ}C$. Time-dependent thermal inactivation studies showed monophasic kinetics for soluble urease and immobilized urease at $70^{\circ}C$, respectively. The immobilized urease beads stored at $4^{\circ}C$ showed practically no leaching over a period of 30 days. Here we are presenting an easy and economical way of immobilizing urease on the gelatin beads making it suitable for various applications.

• Polymer(Korea)
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• v.28 no.4
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• pp.352-359
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• 2004

Membrane technology was used for the optical resolution of the various racemic compounds such as tryptophan, tyrosine and phenylalanine, using enantioselective membranes prepared from sodium alginate (SA) and glutaraldehyde as a membrane material and crosslinking agent, respectively, The chemical structure of the membranes was characterized with FT-IR spectrophotometry and 3D molecular structure modeling study was done to figure out the optical resolution mechanism through the membrane. Effects of degree of crosslinking, feed concentration, operating pressure and different kinds of feed solution on the membrane performances were studied. As results, it was found that with increasing degree of crosslinking and membrane thickness, and decrease in the concentration of the feed solution and smaller size of solutes, the enantinselectivity of the membrane was improved. When the sodium alginate membranes with 80% of swelling index and 79${\mu}{\textrm}{m}$ of thickness were used, 77% of enantiomeric excess was obtained.

• Korean Journal of Food Science and Technology
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• v.20 no.4
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• pp.541-546
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• 1988

Optimum conditions for immobilization of aminoacylase on chitosan were investigated, and the results are summerized as follows: Optimum conditions for activation of chitosan were pH 6.0, 0.2% of glutaraldehyde, and 120 minutes of reaction time. Enzyme concentration and reaction time for immobilization of aminoacylase on the activated chitosan were 80mg/20ml, and 90 minutes, respectively, and the yield of activity of the immobilized enzyme was 42.6%.