• 한국생물공학회:학술대회논문집
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• 2003.04a
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• pp.513-516
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• 2003

고체상 풀림과 재접힘 공정을 통해서 EK의 활성이 회복되어지는 것을 확인할 수 있었다. 이는 고정화 효소를 사용함으로써 기존의 액상반응에서 불가능한 효소의 재사용 문제를 해결할 수 있다. 친화도보다는 다중 공유결합을 통한 효소의 고정화가 효소의 활성 회복에 높은 안정성을 가질 수 있다고 예상한다.

• Journal of Life Science
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• v.21 no.1
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• pp.127-133
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• 2011

${\beta}$-Galactosidase was immobilized on chitosan bead by covalent bonding using glutaraldehyde. The characteristics of the immobilized enzyme were investigated. Maximum immobilization yield of 75% was obtained on chitosan bead. Optimum pH and temperature for the immobilized enzyme was 7.0 and $50^{\circ}C$, respectively. The immobilized enzyme showed a broader range of pH and temperature compared to a free one. A mathematical model for the operation of the immobilized enzyme in a packed-bed reactor was established and solved numerically. Under different inlet lactose concentrations and feed flow rate conditions, lactose conversion was measured in a packed-bed reactor. The experimental results of continuous operation in a packed-bed reactor were compared to theoretic results using Michaelis-Menten kinetics with competitive product inhibition and external mass transfer resistance. The model predicted the experimental data with errors less than 5%. Process optimization of continuous operation in a packed-bed reactor was also conducted. In a recirculation packed-bed operation, conversion of lactose was 97% in 3 hours. In a continuous packed-bed operation, the effect of flow rate and initial lactose concentration was investigated. Increasing flow rates and initial lactose concentration decreased the conversion of substrate.

• Journal of Life Science
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• v.8 no.6
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• pp.627-637
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• 1998

In order to utilize tuna pyloric caeca among fish intestines wasted when treated raw fish in fish processing manufactory, a crude enzyme with high proteolytic activity was extracted and its optimum condition were investigated. An immobilized enzymes also were prepared by adsorption method to enhance thermostability of the crude proteinase. The yield of the crude proteinase was approximately 2.7% on dry basis. The proteolytic activity for casein was 0.54 U/mg protein, for BTEE 1.10 U/mg protein, and for BAEE 2.69 U/mg protein. It was almost similar to that of the commercial trypsin purified. Optimum hydrolysis activity of the crude proteinase was about 80%, as the degree of hydrolysis for casein, at pH 10.0 and 45$^{\circ}C$ for 12 hrs. Also, when the crude proteinase was immobilized on DEAE-Cellulose and chitin, the residual activities remained after 7 days of pre-incubation time were maintained about 90% or more and their thermostabilities were enhanced by about 50%, compared with the native enzyme.

• 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.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1978.10a
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• pp.210.1-210
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• 1978

Aspergillus nidulans가 생산하는 naringinase를 ionic binding method 로써 DEAE-Sephadex A-25 를 사용하여 고정화시키는 조건과 그 고정화 효소의 성질에 대하여 검토하였다. 먼저 담체에 흡착되는 효소의 최적 pH는 6.0이었고 조제효소 110units 당 이상적인 담체량은 건조된 담체 1g이었다. 고정화 naringinase의 반응 최적 pH와 온도는 7.0과 5$0^{\circ}C$로서 native enzyme 보다 각각 높았다. 다음은 고정화 효소의 안정성에 미치는 pH와 온도의 영향으로서, pH 5에서 중성의 pH까지는 안정하였고 온도는 5$0^{\circ}C$까지는 안정하였으나 6$0^{\circ}C$ 이상에서는 뚜렷한 activity의 감소를 보였다.

• KSBB Journal
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• v.23 no.4
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• pp.350-354
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• 2008

Magnetically separable immobilized trypsin was developed and their biocatalytic activity was evaluated for the different immobilization media. The activity, recyclability, pH effect, and stability of immobilized enzymes were evaluated for the different supporting media. The biocatalytic activity of immobilized trypsin was highest with magnetically separable polyaniline (PAMP), and Vm and Km of PAMP were 0.169 mM/min and 0.263 mM respectively. With increasedpH, the biocatalytic activity increased for all supporting materials used. Immobilized enzymes were recycled and recycle activities were over 90% of their original activity after ten times reuse. The operational stabilities of enzymes were greatly improved with enzyme immobilization.

• Korean Journal of Food Science and Technology
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• v.29 no.6
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• pp.1075-1081
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• 1997

The objective of this research was to develop a glutamate enzyme sensor for rapid determinations of glutamate in samples. Glutamate oxidase was immobilized onto activated nylon, chitosan and other membranes. The enzymic and nonactin membranes were attached to an ammonia electrode to detect ammonia generated by the reaction between glutamate oxidase and glutamate. The enzyme immobilized on activated nylon membrane was stable for 2 months, and was able to perform about 250 glutamate determinations without losing activities. The enzyme immobilized on chitosan membrane had higher enzyme activity, but was not as much stable as that immobilized on nylon. The glutamate biosensor was able to accurately determine $0.1{\sim}5\;mM$ of glutamate in samples.

• Korean Journal of Food Science and Technology
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• v.11 no.4
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• pp.249-257
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• 1979

Using the whole cell immobilized glucose isomerase which was prepared in the previous work (Korean J. Food Sci. & Technol., 11(3), 192 (1979), the specific activity of the immobilized enzyme was 48.1 units in the batch reaction system and 114 units in the continuous reaction system per g of matrix, respectively. In the continuous reactor the voidity was 0.36, which was suitable for the packed bed reactor. This immobilized enzyme showed a good operational stability of 115 days of half life which was sufficient for the continuous operation. The experimental result showed that 55 % of the substrate was converted to the product in the packed bed reactor. The productivity was dependent on the flow rate, column geometry, enzyme loading, and substrate concentration. An intrapaticle diffusion was observed by the effectiveness factor of 0.75 and interparticle diffusion by the decrease of Km' with increasing the superficial velocity.

• Korean Journal of Food Science and Technology
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• v.11 no.4
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• pp.283-290
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• 1979

Partially purified ${\beta}-fructosidase$ (inulase) from Kluyveromyces fragilis was immobilized on Tygon tube and aminoethyl-cellulose, respectively and both preparations were characterized. Silanization of Tygon tube in chloroform at $65^{\circ}C$ and treatment with 10 % glutaraldehyde were critical for the immobilization of inulase on Tygon tube, while 2 % glutaraldehyde was effective for the immobilization on aminoethyl-cellulose. The derivative of Tygon tube showed 11.5 units of inulase activity per g of dried matrix with retention of 22.5 % of original activity against inulin, whereas one of aminoethyl-cellulose showed 39.3 units per g of dired matrix with 53.4 % of retention. Studies of enzyme stability, pH and temperature dependences, and $K_m$ values are presented for inulase and invertase activities of both immobilized enzymes.

• Korean Journal of Microbiology
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• v.48 no.3
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• pp.225-227
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• 2012

Lignin degrading enzymes from white rot fungi show broad substrate specificities, and therefore they can degrade variety of recalcitrant compounds. We have used three different protocols for the generation of immobilized laccase and manganese peroxidase crude enzymes from the genetically transformed strains of Merulius tremellosus Fr. These immobilized enzymes were used in the decolorization of Remazol Brilliant Blue R (RBBR), and they showed about 75% decolorization rates during the 48 h reactions. Although the decolorization efficiency decreased by 10-15% after a repeated use of the immobilized enzymes, these can be reused in various degrading reactions.