• Journal of Digital Convergence
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• v.19 no.6
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• pp.331-341
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• 2021

This paper analyzed the discourse on writing by experts such as writers, novelists, and writing instructors appearing in YouTube videos through narrative analysis methods. According to the analysis, the five key topics comprising writing discourse were: Active reading for writing, Nonstop writing and writing more, Rewriting 10 times more than talent, Writing in spoken language in the era of one-person media, Sharing feedback on social media. The writing discourse of professionals illustrated the change in writing in the age of social media. First, it was confirmed that the writing culture shifted from reading to writing and rewriting. Second, writing in the social media era naturally showed that the spoken language of writing became the dominant code. Third, it has been confirmed that writing in the social media era is social writing of cooperation and sharing that openly share feedback. These findings will have significant implications for future research on media and writing

• Journal of Life Science
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• v.27 no.9
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• pp.1003-1010
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• 2017

An open reading frame coding for mannanase predicted from the partial genomic sequence of Paenibacillus woosongensis was cloned into Escherichia coli by polymerase chain reaction amplification, and completely sequenced. This mannanase gene, designated man26AT, consisted of 3,162 nucleotides encoding a polypeptide of 1,053 amino acid residues. Based on the deduced amino acid sequence, Man26AT was identified as a modular enzyme, which included a catalytic domain belonging to the glycosyl hydrolase family 26 and two carbohydrate-binding modules, CBM27 and CBM11. The amino acid sequence of Man26AT was homologous to that of several putative mannanases, with identity of 81% for P. ihumii and identity of less than 57% for other strains of Paenibacillus. A cell-free extract of recombinant E. coli carrying the man26AT gene showed maximal mannanase activity at $55^{\circ}C$ and pH 5.5. The enzyme retained above 80% of maximal activity after preincubation for 1 h at $50^{\circ}C$. Man26AT was comparably active on locust bean gum (LBG), galactomanan, and kojac glucomannan, whereas it did not exhibit activity on carboxymethylcellulose, xylan, or para-nitrophenyl-${\beta}$-mannopyranoside. The common end products liberated from mannooligosaccharides, including mannotriose, mannotetraose, mannopentaose, and mannohexaose, or LBG by Man26AT were mannose, mannobiose, and mannotriose. Mannooligosacchrides larger than mannotriose were found in enzymatic hydrolyzates of LBG and guar gum, respectively. However, Man26AT was unable to hydrolyze mannobiose. Man26AT was intracellularly degraded into at least three active proteins with different molecular masses by zymogram.

• 한국HCI학회:학술대회논문집
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• 2006.02a
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• pp.945-953
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• 2006

The researchers in the field of cognitive science and learning science suggest that the teaching activity induces the elaborative and meaningful learning. Actually, lots of research findings have shown the beneficial effect of learning by teaching such as peer tutoring. But peer tutoring has some limitations in the practical learning context. To overcome some limitations, the new concept of "learning by teaching" through the agent called Teachable Agent. The teachable agent is a modified version of traditional intelligent tutoring system that assigns a role of tutor to teach the agent. The teachable agent monitors individual difference and provides a student with a chance for deep learning and motivation to learn by allowing them to play an active role in the process of learning. That is, The teaching activity induces the elaborative and meaningful learning. This study compared the effects of our teachable agent, KORI, and peer tutoring on the cognition and motivation. The field experiment was conducted to examine whether learning by teaching the teachable agent would be more effective than peer tutoring and reading condition. In the experiment, all participants took 30 minutes lesson on rock and rock cycle together to acquire the base knowledge in the domain. After the lesson, participants were randomly assigned to one of the three experimental conditions; reading condition, peer tutoring condition, and teachable agent condition. Next, participants of each condition moved into separated place and performed their own learning activity. After finishing all of the learning activities in each condition, all participants were instructed to rate the interestingness using a 5-point scale on their own learning activity and leaning material, and were given the comprehension test. The results indicated that the teachable agent condition and the peer tutoring condition showed more interests in the learning than the reading condition. It is suggested that teachable agent has more advantages in overcoming the several practical limitations of peer tutoring such as restrictions in time and place, tutor's cognitive burden, unnecessary interaction during peer tutoring. The applicability and prospects of the teachable agent as an efficient substitute for peer tutoring and traditional intelligent tutoring system were also discussed.

• Journal of Microbiology and Biotechnology
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• v.19 no.10
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• pp.1085-1091
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• 2009

A phytase with high activity at low temperatures has great potential for feed applications, especially in aquaculture. Therefore, this study used a degenerate PCR and TAIL PCR to clone a phytase gene from Erwinia carotovora var. carotovota, the cause of soft rot of vegetables in the ground or during cold storage. The full-length 2.5-kb fragment included an open reading frame of 1,302 bp and encoded a putative phytase of 45.3 kDa with a 50% amino acid identity to the Klebsiella pneumoniae phytase. The phytase contained the active site RHGXRXP and HD sequence motifs that are typical of histidine acid phosphatases. The enzyme was expressed in Escherichia coli, purified, and displayed the following characteristics: a high catalytic activity at low temperatures (retaining over 24% activity at $5^{\circ}C$) and remarkably thermal lability (losing >96% activity after incubation at $60^{\circ}C$ for 2 min). The optimal phytase activity occurred at pH 5.5 and ${\sim}49^{\circ}C$, and the enzyme activity rapidly decreased above $40^{\circ}C$. When compared with mesophilic counterparts, the phytase not only exhibited a high activity at a low temperature, but also had a low $K_m$ and high $k_{cat}$. These temperature characteristics and kinetic parameters are consistent with low-temperature-active enzymes. To our knowledge, this would appear to be the first report of a low-temperature-active phytase and its heterogeneous expression.

• Proceedings of the Korean Vacuum Society Conference
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• 2016.02a
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• pp.278-278
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• 2016

Solution-processed metal-oxide semiconductors have been considered as the next generation semiconducting materials for transparent and flexible electronics due to their high electrical performance. Moreover, since the oxide semiconductors show high sensitivity to light illumination and possess persistent photoconductivity (PPC), these properties can be utilized in realizing optical memory devices, which can transport information much faster than the electrons. In previous works, metal-oxide semiconductors are utilized as a memory device by using the light (i.e. illumination does the "writing", no-gate bias recovery the "reading" operations) [1]. The key issues for realizing the optical memory devices is to have high photoconductivity and a long life time of free electrons in the oxide semiconductors. However, mono-layered indium-zinc-oxide (IZO) and mono-layered indium-gallium-zinc-oxide (IGZO) have limited photoconductivity and relaxation time of 570 nA, 122 sec, 190 nA and 53 sec, respectively. Here, we boosted up the photoconductivity and relaxation time using a double-layered IZO/IGZO active layer structure. Solution-processed IZO (top) and IGZO (bottom) layers are prepared on a Si/SiO2 wafer and we utilized the conventional thermal annealing method. To investigate the photoconductivity and relaxation time, we exposed 9 mW/cm2 intensity light for 30 sec and the decaying behaviors were evaluated. It was found that the double-layered IZO/IGZO showed high photoconductivity and relaxation time of 28 uA and 1048 sec.

• Journal of Korean Library and Information Science Society
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• v.42 no.1
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• pp.125-144
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• 2011

In order to investigate school libraries' educational impact, two different surveys were conducted. One examined students' school library use in general, including the frequency, purpose, and effect of their library use, and the relative importance of the library in their campus life. The other examined and analyzed their perception of the benefit of the school library to determine if any differences exist among the following three levels: 1) libraries staffed with a dedicated teacher librarian, 2) libraries without a dedicated teacher librarian but active, and 3) libraries without a dedicated teacher librarian and inactive. The questionnaire to survey student's perception had 38 statements, The surveys on student's library use and their perceptions indicated that school libraries benefit the students' reading activities the most. The overall mean of the perception was 3.24(in 5 scales), There were distinct differences among the three levels of school library conditions: the mean for libraries with a teacher librarian scored highest at 3.37, libraries without a teacher librarian but active scored second highest at 3.20, and libraries without a teacher librarian and inactive scored lowest at 3.16. The levels of school library condition suggested direct links to the educational effect on students' achievements.

• Journal of Microbiology and Biotechnology
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• v.20 no.4
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• pp.670-677
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• 2010

An alkaline pectate lyase, Bsp165PelA, was purified to homogeneity from the culture broth of alkaliphilic Bacillus sp. N16-5. The enzyme showed a specific activity as high as 1,000 U/mg and had optimum activity at pH 11.5 and $50^{\circ}C$. It was composed of a single polypeptide chain with a molecular mass of 42 kDa deduced from SDS-PAGE, and its isoelectric point was around pH 6.0. It could efficiently depolymerize polygalacturonate and pectin. Characterization of product formation revealed unsaturated digalacturonate and trigalacturonate as the main products. The pectate lyase gene (pelA) contained an open reading frame (ORF) of 1,089 bp, encoding a 36-amino acids signal peptide and a mature protein of 326 amino acids with a calculated molecular mass of 35.943 Da. The deduced amino acid sequence from the pelA ORF exhibited significant homology to those of known pectate lyases in polysaccharide lyase family 1. Some conserved active-site amino acids were found in the deduced amino acid sequence of Bsp165PelA. $Ca^{2+}$ was not required for activity on pectic substrates.

• Journal of Microbiology and Biotechnology
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• v.17 no.1
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• pp.37-43
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• 2007

A gene encoding inulin fructotransferase (di-D-fructofuranose 1,2': 2,3' dianhydride [DFA III]-producing IFTase, EC 4.2.2.18) from Bacillus sp. snu-7 was cloned. This gene was composed of a single, 1,353-bp open reading frame encoding a protein composed of a 40-amino acid signal peptide and a 410-amino acid mature protein. The deduced amino acid sequence was 98% identical to Arthrobacter globiformis C11-1 IFTase (DFA III-producing). The enzyme was successfully expressed in E. coli as a functionally active, His-tagged protein, and it was purified in a single step using immobilized metal affinity chromatography. The purified enzyme showed much higher specific activity (1,276 units/mg protein) than other DFA III-producing IFTases. The recombinant and native enzymes were optimally active in very similar pH and temperature conditions. With a 103-min half-life at $60^{\circ}C$, the recombinant enzyme was as stable as the native enzyme. Acidic residues and cysteines potentially involved in the catalytic mechanism are proposed based on an alignment with other IFTases and a DFA IIIase.

• Journal of Microbiology and Biotechnology
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• v.16 no.11
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• pp.1753-1759
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• 2006

Paenibacillus sp. HY-8 isolated from the digestive tracts of the longicorn beetle, Moechotypa diphysis, produced an extracellular endoxylanase with a molecular weight of 20 kDa estimated by SDS-PAGE. The xylanase was purified to near electrophoretic homogeneity from the culture supernatant after ammonium sulfate precipitation, gel filtration, and ionexchange chromatography. The purified xylanase exhibited the highest activities at pH 6.0 and $50^{\circ}C$. The $K_m\;and\;V_{max}$ values were 7.2 mg/ml and 16.3 U/mg, respectively, for birchwood xylan as the substrate. Nucleotide sequence of the PCR-cloned gene was determined to have the open reading frame encoding a polypeptide of 212 amino acids. The N-terminal amino acid sequence and the nucleotide sequence analyses predicted that the precursor xylanase contained a signal peptide composed of 28 amino acids and a catalytically active 19.9-kDa peptide fragment. The deduced amino acid sequence shared extensive similarity with those of the glycoside hydrolase family 11 of xylanases from other bacteria. The predicted amino acid sequence contained two glutamate residues, previously identified as essential and conserved for active sites in other xylanases of the glycoside hydrolase family 11.

• Journal of Microbiology and Biotechnology
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• v.24 no.9
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• pp.1260-1268
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• 2014

Screening of a gene library from Paenibacillus sp. PBS-2 generated in Escherichia coli led to the identification of a clone with lipolytic activity. Sequence analysis showed an open reading frame encoding a polypeptide of 378 amino acid residues with a predicted molecular mass of 42 kDa. The esterase displayed 69% and 42% identity with the putative ${\beta}$-lactamases from Paenibacillus sp. JDR-2 and Clostridium sp. BNL1100, respectively. The esterase contained a Ser-x-x-Lys motif that is conserved among all ${\beta}$-lactamases found to date. The protein PBS-2 was produced in both soluble and insoluble forms when E. coli cells harboring the gene were cultured at $18^{\circ}C$. The enzyme is a serine protein and was active against p-nitrophenyl esters of $C_2$, $C_4$, $C_8$, and $C_{10}$. The optimum pH and temperature for enzyme activity were pH 9.0 and $30^{\circ}C$, respectively. Relative activity of 55% remained at up to $5^{\circ}C$ with an activation energy of 5.84 kcal/mol, which indicates that the enzyme is cold-adapted. Enzyme activity was inhibited by $Cd^{2+}$, $Cu^{2+}$, and $Hg^{2+}$ ions. As expected for a serine esterase, activity was inhibited by phenylmethylsulfonyl fluoride. The enzyme was remarkably active and stable in the presence of commercial detergents and organic solvents. This cold-adapted esterase has potential as a biocatalyst and detergent additive for use at low temperatures.