• Microbiology and Biotechnology Letters
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• v.17 no.6
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• pp.593-599
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• 1989

A strain producing extracellular endo-type inulase was selected from Actinomycetes isolated from soil, and identified as Streptomyces sp. The maximum inulase production was obtained with medium containing inulin 1.0%, yeast extract 1.0%, (NH$_4$)$_2$HPO$_4$ 0.4%, NH$_4$H$_2$PO$_4$0.8%, KCl 0.05%, MgSO$_4$ㆍ7$H_2O$ 0.05%, FeSO$_4$ㆍ7$H_2O$ 0.001% at 96 hours culture in jar fermentor. The endo-type inulase was considered to be an inducible enzyme produced by inulin only.

• The Korean Journal of Food And Nutrition
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• v.30 no.6
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• pp.1359-1363
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• 2017

The purpose of this study was that the optimal hydrolysis conditions of endo- and exo-type enzymes were selected to utilize organic cheese byproducts. Optimal substrate concentration and optimum enzyme ratio were measured by using 4 kinds of endo-type enzymes (alcalase, neutrase, protamex, and foodpro alkaline protease) and two exo-type enzymes (flavourzyme and prozyme 2000P) for whey protein hydrolysis were analyzed using liquid chromatography. As a result, the optimal endo-type enzyme through the first enzyme reaction was selected as alcalse, and as a result of the secondary enzyme reaction, flavourzme was selected as the Exo type enzyme. The concentration of whey protein substrate for optimal primary and secondary enzyme reactions was 10%. In addition, the optimum ratio of enzyme was 0.5% of alcalase and 0.2% of flavourzyme, which showed low molecular weight chromatography pattern compared to 2% of alcalase and 1% of flavourzyme hydrolyzate. Therefore, hydrolyzing the endo-type enzyme alcalase at a concentration of 0.5% for 10 hours and then hydrolyzing the exo-type enzyme flavouryme at a concentration of 0.2% for 4 hours was considered to be the optimum condition.

• Journal of Dental Rehabilitation and Applied Science
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• v.38 no.2
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• pp.81-89
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• 2022

Purpose: Wireless endodontic handpieces (WEH) are widely used in dental clinics due to their convenience and portability. This study aimed to compare the vibration magnitudes and patterns generated by five WEH. Materials and Methods: Vibration acceleration of five WEH (X-Smart IQ, E connect S, Endo A Class, ENDOIT, and TRAUS ENDO) in the rotary and reciprocating motion was measured with accelerometer The average vibration acceleration was analyzed using the t-test, Welch's ANOVA test, and Dunnett T3 test at P < 0.05. Results: In all WEH, the average vibration acceleration in reciprocating motion was significantly higher than that in rotary motion (P < 0.001). In rotary motion, repeated vibration graphs of constant amplitude were obtained without sudden changes in the magnitude of vibration, and the average vibration acceleration value was high in the order of X Smart IQ, Endo A Class, ENDOIT, E Connect S, and TRAUS ENDO (P < 0.001), there was no statistically significant difference between X Smart IQ and Endo A Class. In reciprocating motion, a vibration graph was obtained in which large amplitude peaks appear at specific points within one cycle are repeated. The average vibration acceleration value was highest in the order of X Smart IQ, E Connect S, Endo A class, ENDOIT, and TRAUS ENDO (P < 0.001). Conclusion: Regardless of the type of WEH, greater vibration occurred in the reciprocating motion than in the rotary motion (P < 0.001). In the reciprocating motion, there was a difference in vibration for all handpieces (P < 0.001).

• Journal of Microbiology and Biotechnology
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• v.26 no.5
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• pp.946-952
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• 2016

The eglS gene in Bacillus amyloliquefaciens encodes an endo-β-1,4-glucanase that belongs to glycosyl hydrolase family 5. In this study, a disruption mutant of gene eglS was constructed to examine its role in bacterial adaptation in plants. The mutant TB2_k, eglS gene inactivated bacterial strain, was remarkably impaired in extracellular cellulase activity. When inoculated on Brassica campestris, the TB2_k population was reduced by more than 60% compared with the wild-type strain in the root, stem, and leaf tissues. Overexpression of eglS in the wild-type strain increased the bacteria population in the plant tissues. Further studies revealed that the transcription level of eglS was correlated with bacterial population. These data demonstrate that endo-β-1,4-glucanase of B. amyloliquefaciens is required for its optimal endophytic colonization.

• Applied Biological Chemistry
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• v.37 no.4
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• pp.243-247
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• 1994

Endo-polygalacturonase was purified from Jujube. The purification procedures included DEAE-cellulose ion exchange chromatography and gel filtration on Sephdex G-100. Enzyme was purified as a single protein band and purification yield was about 6%. When the purified enzyme was applied to sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the molecular weight was estimated about 19,000. Purified enzyme formed hexagonal board type.

• Applied Chemistry for Engineering
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• v.18 no.1
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• pp.36-40
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• 2007

The study on the isomerization reaction of endo-tetrahydrodicyclopentadiene and endo-tetrahydrodi(methylcyclopentadiene) using heteropolyacid catalyst was carried out. Exo compound was prepared from endo compound through isomerization reaction. To improve the problem of aluminum chloride as an isomerization catalyst, application of heteropolyacid was attempted. In use of Keggin type heteropolyacid, catalytic activity was extremely high at cesium substitution instead of 2.5 hydrogen atoms of $H_3PW_{12}O_{40}$. Using the cesium substituted heteropolyacid, isomerization reaction rate was faster than aluminum chloride and the effect of reaction temperature and times on reactivities were compared in isomerization of tetrahydrodicyclopentadiene and tetrahydrodi(methylcyclopentadiene).

• BMB Reports
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• v.40 no.6
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• pp.1095-1099
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• 2007

Endonuclease G (EndoG) is a mitochondrial non-specific nuclease that is highly conserved among the eukaryotes. Although the precise role of EndoG in mitochondria is not yet known, the enzyme is released from the mitochondria and digests nuclear DNA during apoptosis in mammalian cells. Schizosaccharomyces pombe has an EndoG homolog Pnu1p (previously named SpNuc1) that is produced as a precursor protein with a mitochondrial targeting sequence. During the sorting into mitochondria the signal sequence is cleaved to yield the functionally active endonuclease. From the analogy to EndoG, active extramitochondrial Pnu1p may trigger cell killing by degrading nuclear DNA. Here, we tested this possibility by expressing a truncated Pnu1p lacking the signal sequence in the extramitochondrial region of pnu1-deleted cells. The truncated Pnu1p was localized in the cytosol and nuclei of yeast cells. And ectopic expression of active Pnu1p led to cell death with fragmentation of nuclear DNA. This suggests that the Pnu1p is possibly involved in a certain type of yeast cell death via DNA fragmentation. Although expression of human Bak in S. pombe was lethal, Pnu1p nuclease is not necessary for hBak-induced cell death.

• The Korean Journal of Mycology
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• v.25 no.4 s.83
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• pp.330-339
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• 1997

Botrytis cinerea T91-1 has shown to produce at least four different polygalacturonases in a liquid medium containing citrus pectin as a carbon source. One of the enzymes, its molecular weight was estimated as 37 kDa by denatured polyacrylamide gel electrophoresis, was purified by a series of procedures including acetone precipitation, ion exchange, heparin affinity, and reverse phase column chromatographies. By viscometric analysis, the enzyme was revealed as an endo-polygalacturonase. The enzyme activity was inhibited by divalent cations such as $Ca^{2+}$, $Co^{2+}$, and $Cu^{2+}$. Km and Vmax for polygalacturonic acid hydrolysis were 0.33 mg/ml and 28.6 nM/min, respectively. The optimum temperature for enzymatic activity was $55^{\circ}C$ and the enzyme showed optimal pH values between 4.0 and 4.5. The enzyme was stable up to 12 hours in the range of pH 4 to 7 and at the temperature below $30^{\circ}C$. Amino acid sequence from N-terminal up to 6 amino acids determined by Edman degradation showed little homology with polygalacturonases from fungi and plants.

• Restorative Dentistry and Endodontics
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• v.28 no.4
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• pp.295-302
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• 2003

본 연구에서는 인산 칼슘 근관 봉함재 [Apatite Root Sealer (ARS) Type I, II, III]의 세포독성을 혼합후의 시간 경과에 따라서 다른 4계열의 근관 봉함재 (Pulp Canal Sealer EWT, AH Plus, Sealapex, Ketac Endo)와 비교하여 평가하였다. 근관 봉함재를 혼합한 후 1시간, 8시간, 24시간, 48시간, 1주, 2주,4주의 기간동안 배양액을 이용하여 추출액을 얻었다. L929 쥐섬유아세포를 24시간동안 각 시간군에서 얻은 추출액과 함께 배양한 후 dimethylthiazol diphenyltetrazolium (MTT) assay와 neutral red (NR) assay를 이용하여 세포독성(%)을 평가하였다. 실험 결과 ARS Type I, II, III는 전 시간군에 걸쳐 낮은 세포독성을 보였고 (23.65-0.55%) 특히 경화 초기에 다른 계열의 근관 봉함재보다 유의성 있게 낮은 세포독성을 나타내었다. ARS Type I, II, III간의 세포독성은 각 시간군에서 유의성 있는 차이를 보이지 않았다. AH Plus와 Ketac Endo는 초기에 높은 세포독성을 보였으나 AH Plus는 8시간 이후에, Ketac Endo는 24시간 이후에 독성이 급격히 감소하여 ARS와 유의성 있는 차이를 보이지 않았다. Pulp Canal Sealer EWT와 Sealapex는 4주까지 지속적인 세포독성을 나타내었다. 그리고 MTT assay와 NR assay를 이용하여 얻은 각 근관봉함재의 세포독성은 시간 경과에 따라서 비슷한 변화 양상을 나타내었다. 인산 칼슘 근관 봉함재는 생체적합성이 우수한 재료로써 앞으로 지속적인 개발과 평가가 필요할 것으로 사료된다.

• Microbiology and Biotechnology Letters
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• v.49 no.3
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• pp.329-336
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• 2021

Cellulophga sp. J9-3, is a gram-negative, aerobic marine bacterium belonging to the family Flavobacteriaceae. In addition to cellulose degradability, the J9-3 strain is also capable of hydrolyzing agar in the solid and liquid medium, and the production of agarase in the presence of agarose can be remarkably induced by the bacterium. From the cell culture broth of Cellulophga sp. J9-3, ammonium sulfate precipitation and three kinds of column chromatography were successively performed to purify a specific agarase protein, the AgaJ93. Purified AgaJ93 showed the strongest hydrolyzing activity towards agarose (approximately 22%), and even displayed activity towards starch. AgaJ93 hydrolyzed agarose into neoagarotetraose and neoagarohexaose via various oligosaccharide intermediates, indicating that AgaJ93 is an endo-type β-agarase. AgaJ93 showed maximum activity at a pH of 7.0 and temperature of 35 ℃. Its activity increased by more than six times in the presence of Co²⁺ ions. The N-terminal sequence of AgaJ93 showed 82% homology with the heat-resistant endo-type β-agarase Aga2 of Cellulophaga sp. W5C. However, the biochemical properties of the two enzymes were different. Therefore, AgaJ93 is expected to be a novel agarose, different from the previously reported β-agarases.