• 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.

• Food Science and Preservation
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• v.24 no.5
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• pp.697-706
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• 2017

The purpose of this study was to investigate the physiochemical properties of Doenjang was fermented by added with fungi and protease. The moisture content and pH of Doenjang added with protease (WP) were lower than those of control w/o protease while the contents of titratable acidity, reducing sugar, and amino-type nitrogen in WP were higher than control. The ${\alpha}$-amylase activities of Doenjang added with single and mixed Protease B were the highest at 4 weeks of fermentation period and protease activity of WP was about 4 times higher than that of control. The 4-9 kinds of free amino acids (proline, isoleucine, leucine, and phenylalanine etc.) in WP was increased in comparison with control. The DPPH radical scavenging activity and total polyphenol content were higher in WP than control. Total aerobic bacterial and fungal numbers were decreased depending on fermentation time regardless of addition of protease. In conclusion, the protease can be used as additives improving the quality and taste of fermented Doenjang.

• Proceedings of the KAIS Fall Conference
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• 2012.05a
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• pp.239-242
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• 2012

효모 (Saccharomyces Cervisiae)는 단일 세포의 형태로 존재하는 진핵 세포로써 동물세포와 유사한 기작으로 분비성 단백질을 생성한다. 따라서 박테리아와 달리 효모를 이용하면 당단백질이나 이황결합을 포함하는 분비성 단백질을 경제적으로 대량 합성할 수 있다. 효모의 필수 단백질 중 하나인 단백질 이황이성질화 효소는 소포체에 위치하며 분비성 단백질에 구조적으로 안정한 이황결합을 제공하는 효소이다. 본 연구는 단백질 이황이성질화 효소 (protein disulfide isomerase)가 지니고 있는 두 개의 활성도메인 중 분비성 단백질들의 합성 효율에 직접적으로 관여하는 부위를 찾는 연구이다. 효모 유전체로부터 단백질 이황이성질화 효소의 유전자 (PDI1)을 제거하고 효소의 변이 유전자를 주입한 후 효모의 성장 속도를 측정하였다. 또한 효모의 대표적 분비성 단백질을 각 변이 효소를 지니는 효모에 과발현시켜 합성 및 이황결합 형성 효율을 측정하였다. 단백질 이황이성질화 효소내 두 개의 활성 부위 중 아미노 말단쪽에 위치한 a 도메인에 있는 활성 부위가 분비성 단백질의 활성에 중요한 역할을 한다는 것을 알 수 있었다. 이 결과는 이황결합이나 당을 포함하는 외래 단백질의 고효율 합성을 위한 새로운 효모종 개발에 중요한 정보를 제공할 것으로 기대 된다.

• The Korean Journal of Mycology
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• v.26 no.4 s.87
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• pp.496-501
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• 1998

The mycelia of Tricholoma matsutake DGUM 26001, 26101, 26210 and FRI 91024 were used to determine the extracellular enzyme activity in mycelia. When the filtrate of culture broth after 30-day cultivation at $24^{\circ}C$ was used as a crude solution of extracellular enzyme, the average specific activity of ${\alpha}-amylase$ was 6142.3 unit/mg protein. The specific activity of xylanase was comparatively high. However, little or no enzyme activities were found for ${\beta}-glucosidase$, ligninase, CMCase, chitinase, protease, and lipase.

• Journal of Periodontal and Implant Science
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• v.24 no.3
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• pp.443-457
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• 1994

본 연구의 목적은 비외과적 치주치료시에 부가적으로 사용하기 위해 개발한 테트라싸이클린 젤의 효과를 임상지수, 치은 열구액양 및 치은열구액내 효소활성도 측정을 통해 평가함에 있다. 치주낭 깊이가 4mm 이상 6mm이하인 구치가 편악당 적어도 2개 이상 존재하는 중등도 치주염에 이환된 환자 23명을 선택하여, 한 편악에서는 치근활택술 만을 시행하였고, 다른 한 편악에는 치근활택술 후 테트라싸이클린 젤을 치은연하로 주입한 뒤 치근면 처리하였다. 사용된 임상검사 지수는 치태지수, 치은지수, 치주낭 깊이, 치은부착 상실도 및 탐침시 출혈로, 각각 치료시작 전과 치료 후 4, 12주에 검사하였으며, 치은열구액내 효소활성도 검사를 위해 치은열구액을 치료시작 전과 치료 후 1, 2, 4, 12주에 각각 채취하고 치은열구액 양을 조사한 뒤 Lactate dehydrogenase(LDH)와 Beta-glucuronidase(BG)의 활성도를 측정하였고, 효소활성도는 LDH는 340nm에서, BG는 550nm에서 각각 흡광도를 조사 분석하여 다음과 같은 결과를 얻었다. 1. 임상지수를 측정 비교한 결과 치근활택술 만으로 치료한 군과 치근활택술 후 테트라싸이클린 젤을 병용한 군 모두에서 임상적으로 치은건강의 현저한 향상을 관찰할 수 있었으나, 통계상 두 군간의 유의성있는 차이는 발견되지 않았다. 2. 치은열구액 양은 치근활택술 후 테트라싸이클린 젤을 병용한 군이 치근활택술만 시행한 군보다 치료 후 2주와 4주에 유의성 있게 감소하였다. 3. LDH와 BG 효소 활성도는 두 군 모두 현저히 감소하였고, 비록 통계학적인 유의성은 관찰할 수 없었으나 치근활택술 후 테트라싸이클린 젤을 병용한 군에서 감소량이 더 크게 나타났다.

• Korean Journal of Soil Science and Fertilizer
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• v.18 no.1
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• pp.105-110
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• 1985

A incubation study was conducted to find out the effects of rice straw and gypsum as soil ameriolite on urease, nitrate and nitrite reductase activities in newly reclaimed saline sandy soil. The results obtained were summarized as follows: 1. Very low urease activities were observed in saline soil if contrast to high productive paddy soil. Urease activities were lower at 5 days than that of 25 and 50 days after incubation. Remarkably high urease activities were obtained by the application of rice straw and gypsum. 2. Comparing with NPK treatment, application of rice straw and gypsum were enhanced the activities of nitrate and nitraite reductase. 3. Positive correlation (r=0.5501 p=0.05) was obtained between urease activities and ammonium nitrogen concentration in soil. 4. Cyclic oxidation and reduction of nitrate and nitrite in soil were obtained in terms of first order microbial kinetics reaction in case of application of rice straw and gypsum, respectively. 5. Positive correlation (r=0.6296 p=0.05) was obtained between the activitie of nitrite reductase and nitrate reductase in soil.

• Journal of Chitin and Chitosan
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• v.23 no.4
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• pp.228-233
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• 2018

We isolated microorganisms from soil, which is sampled at forest, Kyeonbuk, Korea, as cellulolytic microorganisms. The isolated strains were identified by analysis of 16S rRNA gene from the starins. The result, four kinds of Bacillus subtilis, one kind of Bacillus amyloliquefaciens, and one kind of Bacillus cereus were identified. Among these strains, Bacillus subtilis was selected due to its high cellulase activity and this strain was named as Bacillus subtilis CNS. The optimum pH and temperature of the cellulase from Bacillus subtilis CNS was pH 5.0 and $40^{\circ}C$, respectively. In the investigation of pH and temperature stability, the cellulase from Bacillus subtilis NSC stabled pH 4.0~6.0 range and until $40^{\circ}C$ for 30 min perfectly. In the enzyme activity for various cellulosic substrate, cellulase from Bacillus subtilis CNS showed the highest activity for CM-cellulose. And, the enzyme activities for alkali swollen cellulose, Alpha-cellulose, Sigmacell-cellulose, and Avicel were approximately 31%, 8%, 8% and 4% of activity for CM-cellulose, respectively. In the degradation of CM-cellulose, the 0.26 U/ml and 0.52 U/ml of cellulase showed 0.43 and 0.76 U/ml activity for CM-cellulose after the reaction of 120 min, respectively.

• Journal of the Korean Society of Food Science and Nutrition
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• v.25 no.1
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• pp.150-156
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• 1996

유산균의 균주개량방법의 일환으로 photoplast fu-sion 기법과 electrofusion법을 이용하여 protease 활성, lipase 활성, 내열성, 내산성 등이 우수한 L. bulgaricus와 bacteriocin을 생산하는 L. acidophilus 간의 융합시켜 얻은 융합주들의 생리학적 성질을 검토하였다. 산 생성능, 내열성, 내산성 protease, lipase 활성 등 L. bulgaricus가 L. acidophilus보다 우수하였다. L. bulgaricus는 lactose와 sorbos를 이용하였으나. mal-tose 와 dorbitol을 이용하지 못하는 반면 , L. acidophilus는 matose를 이용하고 lactose 와 sorbose를 이용하지 못하였다. 융합주 가운데서는 367810번이 모균주의 발효능 특성을 함께 지님으로서 재조합체임을 확인 할 수 있었으며, sorbitol의 경우 모균주에서는 발효능이 전혀 나타나지 않았음에도 불구하고 융합주 4, 7번이 발효능을 나타내어 융합과정에서 새로운 형질을 획득하기도 한다는 사실을 알 수 있었다. Lactase 활성은 모균주 모두 높은 $\beta-galactosidase$ 활성을 보였으나, $phospho-\beta-galactosidase$ 활성은 거의 없었으며 융합주들도 다소 차이는 있었지만 모균주와 유사한 효소활성을 나타내었다. 발효에 있어서 key enzyme으로 작용하는 protease. lipase 등의 효소활성도 모균주의 활성보다 우수한 융합주도 존재하였다.

• Microbiology and Biotechnology Letters
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• v.26 no.1
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• pp.15-22
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• 1998

The dnrF gene, responsible for conversion of aklavinone to $\varepsilon$-rhodomycinone via C-11 hydroxylation, was mapped in the daunorubicin gene cluster of Streptomyces peucetius subsp. caesius ATCC 27952, close to drrAB, one of the anthracycline resistance genes. To characterize the enzymatic properties of the aklavinone 11-hydroxylase, the dnrF gene was overexpressed in Escherchia coli. The pET-22(+) plasmid which has the T7 promoter under the control of lacUV5 gene was used for the overexpression of the dnrF gene, and the recombinant plasmid pET213 that contains the dnrF gene linked to the T7 promoter of pET-22b(+) was introduced into the E. coli BL2l. When the expression of the dnrF gene was induced by IPTG at the final concentration of 1 mM, the induced protein could be detected in SDS-PAGE only in insoluble precipitate. The insoluble protein was electroeluted from the gel and used for the preparation of antiserum in mice. Various culture conditions were tested to maximize the expression of the aklavinone 11-hydroxylase in soluble form. The enzymatic activity was checked by the bioconversion experiment, and the protein was confirmed by the SDS-PAGE and the Western blot analysis. From the analysis of the data, it was concluded that the culture induced with IPTG at the final concentration of 0.02 mM at 37$^{\circ}C$ yielded the best productivity of active form of enzyme.

• Applied Biological Chemistry
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• v.49 no.4
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• pp.287-292
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• 2006

The effects of cadmium on the catalase activity and isozyme patterns under light and dark conditions of rice(Oryza sativa L. cv. Dongjin) seedlings were examined. Cadmium treatment resulted in the notable enhancement of $H_2O_2$ contents in the seedling roots and leaves under light and dark conditions. The catalase isozyme patterns in the roots were different from those in the leaves, showing tissue-specific expression of the enzyme. Moreover, the expression patterns of catalase isozymes in the green seedling roots were different from those in the etiolated seedling roots following cadmium treatment. The increase of total catalase activity was about 16 times at 1 mM cadmium and marked inductions of the isozyme CAT1 and CAT2 contributed to this increase in the green seedling roots. On the other hand, in the etiolated seedling roots, total catalase activity was lower than that of control at 0.5 and 1 mM cadmium, even though catalase activity increased about 3 times at 0.1 mM cadmium. The 3 fold increase of total catalase activity was mainly due to the increase of CAT1, CAT3 and CAT4 at 0.1 mM cadmium. However, treatment with higher concentrations of cadmium decreased the activity of CAT2 and CAT4 in the etiolated roots. In the leaves, the catalase existed as three isozymes; one cationic isozyme CATc, one neutral isozyme CATn and one anionic isozyme CAT1 in the control. The isozyme patterns and total activities remained unaffected by cadmium under light and dark conditions in the seedling leaves. Taken together, it seems that cadmium-induced changes of catalase might be regulated by light in the roots, but not in the leaves.