• Proceedings of the Korea Technical Association of the Pulp and Paper Industry Conference
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• 2001.11a
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• pp.141-141
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• 2001

사이즈 프레스용 전분은 주로 산화전분이 이용되고 있으며, 전분업체에서 공급되는 것과 제지공장에서 자가변성으로 제조하여 이용하는 것으로 나눌 수 있다. 자가변성의 경우 경제적 측면에서 원가절감이 가능한 장점이 있는 반면 전분 품질이 다소 미흡한 단점이 있다. 자가변성 산화제로는 APSCAmmonium persulfate), 효소 등이 이용된다. 효소는 APS에 비해 전분 분자 내의 1,4결합만을 가수분해 시키고 점도안정성과 전분 용액 색상이 양호한 특성을 보인다. 또한 온도/농도/점도 등의 상관성을 자유롭게 이용하여 요구하는 전분 용액 품질을 얻을 수 있다. 제지용 전분 산화용으로는 주로 알파 -아밀라아제가 이용된다.본 실험은 산화전분을 효소변성을 이용한 생전분으로 가능성을 알아보고자 진행되었다. 일차적으로 실험실에서 하였고, 몇 차례의 mill trial을 통해 효소변성 전분 적용을 최적화하고자 하였다. 실험실적으로 효소변성을 위한 반응조건으로 온도, 시간, pH, 투입량 등을 설정하였 고, 각 조건별로 제조된 전분 용액의 점도를 측정하여 효소 반응성을 평가하였다. 실험 결과 전분 용액의 점도는 낮았고, 점도 안정성 또한 양호한 수준을 보였다. Cooking농 도는 20%로 하였으나 보다 고농도 cooking의 가능성을 확인할 수 있었다. 시트 물성도 전반적으로 산화전분 대비 대등한 수준을 나타내었다. Mill trial은 무림제지에서 실시하였고 사이즈 프레스 조제식을 이용하였다. 전분 농도는 초기에 20%로 시작하여 30%까지 올려서 trial을 실시하 였고, 그 외 작업조건들은 산화전분 적용 시와 동일하게 하였다. 효소 반응시간으로 인해 cooking시간이 다소 많이 걸렸으나 전반적인 조제 작업은 큰 문제 없이 이루어졌고, 효소변성 전분 용액의 점도는 낮은 수준으로 유지되었다. 사이즈 프레스 작업성이나 시 트 물성도 산화전분 적용 시와 대등한 수준을 보였으나, 전분 차이로 인한 색상 차이로 부가적인 염료 조정이 이루어졌다. 한편 폐수부하 증가를 우려하였으나, 이에 따른 문제는 크게 발생되지 않았다.

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

• Journal of Korean Ophthalmic Optics Society
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• v.20 no.2
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• pp.237-246
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• 2015

Purpose: The present study was conducted to reveal the correlation of structural denaturation and decrease of enzyme activity when the antioxidative enzymes, superoxide dismutase (SOD) and catalase (CAT) were repeatedly exposed to UV-B, and further investigate whether the denaturation and inactivation of those enzymes can be effectively blocked by using UV-inhibitory RGP lens. Methods: Each enzyme solution was prepared from the standardized SOD and CAT, and repeatedly exposed to UV-B of 312 nm for 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-B irradiation was confirmed by the electrophoretic analysis, and their enzyme activity was determined by the colorimetric assay using the proper assay kit. At that time, the change in structure and activity of the antioxidant enzymes directly exposed to UV-B was compared to the case that UV-B was blocked by UV-inhibitory RGP lens. Results: SOD exposed repeatedly to UV-B showed the polymerization pattern in the electrophoretic analysis when it repeatedly exposed for 30 min a day, however, the change of its activity was less than 10%. On the other hand, CAT repeatedly exposed to UV-B reduced size and density of the electrophoretic band which indicated a structure denaturation, and its activity was significantly decreased. In the case that the repeat exposure time was longer, CAT activity was completely lost even though some enzyme band occurred in the electrphoretic analysis. In addition, the degeneration of CAT due to UV-B irradiation was inhibited to some extent by using RGP lens with a UV-B blocking of 63.7%, however, it was not completely inhibited. Conclusions: From these results, it was revealed that the structural denaturation of antioxidative enzymes was not perfectly correlated with the reduction in enzyme activity according to the type of enzyme. It is recommended to minimize the exposure time to UV when wearing contact lens, or wear the contact lenses having UV blocking rate of the FDA Class I blocker or the sunglasses having equivalent UV-blocking rate for reducing the damage of antioxidative enzymes induced by UV.

• Journal of Korean Ophthalmic Optics Society
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• v.12 no.3
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• pp.97-103
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• 2007

This study was investigated to find the proper UV-A blocking percentage that could protect the denaturation of catalase and superoxide dismutase (SOD), antioxidative enzymes in eye, induced by UV-A. Catalase or SOD were irradiated at 365 nm for 1, 3, 6, 24, 96 hr and the extent of denaturation was evalutated by polyacrylamide gel electrophoresis. Furthermore, it was investigated whether blocking of UV-A by 20, 50, 80 and 99% eyeglass lens could protect the denaturation of catalase and SOD or not. Catalase became to denature when catalase were irradiated by UV-A for more than 3 hours. However, the denaturation of SOD was induced by more than 6 hours irradiation. The denaturation of catalase induced by irradiation for 3 hr could be perfectly protected by 99% UV-A blocking lens. But, when the irradiation time became longer than 3 hr or the blocking percentage of lens were lower than 99%, the denaturation of catalase was not perfectly protected but partially protected. Although 50% UV-A blocking lens had partial protecting effects, lenses having 80 or 99% UV-A blocking effect could perfectly prevent the denaturation of SOD induced by 96 hr irradiation.

• Biomedical Science Letters
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• v.2 no.2
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• pp.241-247
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• 1996

Poor yields of amplified DNAs could be resulted in polymerase chain reaction(PCR) processes with G+C-rich DNA primers because of their high $T_m$ values. To maximize the yields of amplification in PCR processes with G+C-rich primers, we compared the yields of amplified DNA fragments according to the concentrations of specific denaturants added to the reaction mixture of PCR system. With addition of the mixture of 2.5% glycerol and 1.25% formamide, or 2.5% dimethyl sulfoxide to the reaction cocktail, respectively, remarkable increases in the yields of amplified DNA fragments were not observed in the PCR systems with G+C-low primers of Lyl chromosomal gene from Borrelia burgdorferi but observed in the PCR system with G+C- ich primers of Is900 gene from Mycobacterium parahberculosis. Although we were not practically able to discriminate the yields of PCR DNAs according to the concentrations used in this study, addition of the mixture of 5% glycerol and 2.5% formamide, or 5% DMSO tended to increase the production of extra bands.

• Proceedings of the Korean Society of Applied Pharmacology
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• 1993.04a
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• pp.57-57
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• 1993

단백질 분해효소는 염증주변에 축적된 파괴조직이나 변성단백질등을 분해하여 염증, 특히 만성염증의 순환을 정상화함으로써 소염제로서 사용되어 왔으며 현재, Chymotrypsin, Trypsin, Promelain, Papain, Serrathiopeptidase, Pronase 등이 소염효소제로써 사용되고 있다. 이들은 주로 미생물 배양액에서 통상적인 방법으로 정제하여 사용하며, 유전자 재조합기술을 사용하여 재조합 균주에서 생산할 경우 그 생산성을 증대시킬수 있을 것이라 기대된다.

• The Korean Journal of Food And Nutrition
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• v.18 no.1
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• pp.4-10
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• 2005

Periodate-oxidized soluble starch increased pH stability of Aspergillus awamori a-glucosidase. After incubation for two hours, the enzyme in the absence of oxidized soluble starch was stable in the range of pH 3-7 at 40℃, pH 3-6 at 50℃ and the enzyme in the presence of oxidized soluble starch was stable in the range of pH 3-9 at 40℃, pH 3-8 at 50℃. At 60℃, the enzyme was stable in pH 3-6 regardless of the presence or absence of IO₄-oxidized soluble starch, but when IO₄-oxidized soluble starch existed in pH 5-6, remained activity of the enzyme increased 20% more than when it didn't exist. The enzyme modified with IO₄-oxidized soluble starch remained 70% of activity in pH 9, but native enzyme didn't remain, showing the increase of stability due to modification. In thermal stability, modified enzyme remained 12% at 50℃ and 7% at 80℃. But native enzyme remained 8% at 50℃ and didn't remain at more than 70℃. The result of HPLC analysis revealed the subunit of the enzyme at under pH 2 or over pH 9 was separated or the enzyme was denatured and conjugated. Protein structure of native enzyme was denatured by acidic and basic pH but was stable in the presence of IO₄-oxidized soluble starch.

• Journal of Korean Ophthalmic Optics Society
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• v.13 no.4
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• pp.43-49
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• 2008

Purpose: The current study was conducted to evaluate the compatibility of UV-A blocking contact lens on eye protection with regular contact lens. Methods: The protective activity of regular contact lens (UV-A blocking: 20%) and UV-A blocking contact lens (UV-A blocking: 85%) on the denaturation of RNase A, catalase, and superoxide dismutase (SOD) induced UV-A irradiation were compared by acrylamide gel electrophoresis. The enzyme solutions were irradiated with UV-A for 1, 3, 6, 24 and 96 hours at the wavelength of 365 nm. Covering area with contact lenses were varied as 50%, 70% and 100% according to the calculation of blocking areas of anterior eye that could be covered with RGP lens, soft contact lens, and eye glasses, respectively. Results: Denaturations of RNase, catalase and SOD were exaggerated when they were exposed to UV-A for a longer period. The denaturation was effectively prevented by UV-A blocking contact lens compared to regular contact lens. The capability of UV-A blocking contact lens was considerably reduced when the covering area with contact lens decreased and exposure time to UV-A extended. Conclusion: Therefore, it would be suggested that wearing contact lens for a long time under sunlight is carefully considered since the activity of UV-A blocking contact lens against UV-A irradiation may not be enough to protect enzymes presented in eyes when exposure time to UV-A increased.

• KSBB Journal
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• v.6 no.1
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• pp.105-109
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• 1991

In separating alkaline protease from the bacteria (Bacillus licheniformis) fermentation broth using reverse micelle, effects of various factors;ionic strength, pH and surfactant concentration, on separation efficiency were studied. KCl controls the ionic strength. The lower KCl concentration was in the feed solution, the more protein and activity was recovered. The higher KCl concentration was in the stripping solution, the more protein and activity was recovered. Using sodium-di-2-ethylhexyl sulfosuccinate(Aerosol-OT or AOT) as a surfactant, the higher AOT concentration in the solvent, the more activity and protein were recovered. 0.1N NaOH and IN HCl were used to adjust pH. Maximum recovery of protein mass and activity were obtained at feed solution of pH 5.3. Maximum activity was recovered at stripping solution of pH 7.5

• Journal of Korean Ophthalmic Optics Society
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• v.18 no.3
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• pp.253-260
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• 2013

Purpose: To investigate the UV-B blocking rate of eyeglasses lens which can prevent enzymes denaturation in cornea. Methods: The denaturation degree of RNase A and catalase, superoxide dismutase (SOD) was determined by using Acrylamide gel electrophoresis after UV-B irradiation of 312 nm for 1, 3, 6, 24 and 96 hours. Also, the inhibitory effect of eyeglasses lens having UV-B blocking rate of 50%, 80%, 95% and 99% on the enzymes denatration was measured. Results: The denaturation of RNase A was induced by 1 hour-irradiation of UV-B. To inhibit RNase A denaturation after UV-B irradiation between 1 hour and 6 hours, UV-B blocking lens of 95% were effective. UV-B blocking lens of 99% suppressed the inhibition of RNase A denaturation after the UV-B exposure between 24 hours and 96 hours. The denaturation of catalase was not induced by 1 hourirradiation of UV-B. To inhibit enzyme denaturation after UV-B irradiation between 1 hour and 6 hours, UV-B blocking lens of 50% were effective. UV-B blocking lens of 95% suppressed the inhibition of enzyme denaturation induced by UV-B irradiation between 24 hours and 96 hours. The SOD denaturation was not induced by UV-B irradiation shorter than 6 hours exposure. The UV-B blocking lens of 50% could inhibit SOD denaturation after the UV-B irradiation for 24 hours. When SOD was exposed to UV-B for 96 hrs, SOD denaturation was inhibited by eyeglasses lens with UV blocking rate higher than 95%. Conclusions: The results demonstrated that the proper UV-B blocking rates of eyeglasses lens to inhibit the enzymes denaturatioin was different according to the types of enzymes and its inhibitory effect was effective only when eyeglasses lens had higher than certain UV-B blocking rate.