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INFLUENCE OF BASALT FIBRES ON THE PROPERTIES OF FLY ASH BASED GEOPOLYMER BINDER
Temuujin, J.,Minjigmaa, A.,Davaabal, B.,Darkhijav, B.,Ruescher, C.H. Korean Association for Particle and Aerosol Resear 2016 Particle and Aerosol Research Vol.12 No.2
The influence of basalt fibres on the compressive strength of the geopolymer type binders has been studied. For the experiments 2 types of the basalt fibres were used, namely chopped and spooled fibres. Both types of basalt fibres were 7-10 micron thick in diameter and cut into pieces of 6 mm length. The fibres were mixed with 1% weight to the fly ash powder, followed by the addition of the activator solution (8M NaOH). The pastes obtained were cured at $70^{\circ}C$ for 20 h revealing compact bodies. Compressive strength was measured after 7 days and microstructure observation performed with SEM. The cube bodies ($2{\times}2{\times}2cm$) reveal compressive strength of 47.25(4.03) MPa, while it decreased to 34.0(9.05) MPa in spooled basalt fibres and to 17.33(5.86) MPa in the chopped basalt fibres containing binder, i.e 76% and 36% of the strength without fibres, respectively. The much weaker compressive strength of the chopped fibres containing binder is related to the absence of significant adhesion between the geopolymer binder and the basalt fibres, forming voids instead. Alkali leaching effect of basalt fibres could probably explain the drop in the compressive strength with spooled and chopped fibres, respectively.
Temuujin, Ulambayar,Kim, Jae-Won,Kim, Jong-Kun,Lee, Byoung-Moo,Kang, Hee-Wan Elsevier 2011 Physiological and molecular plant pathology Vol.76 No.2
<P><B>Abstract</B></P><P>Twelve genes encoding cellulases, including endo- and exoglucanases, were identified from the genomic database of <I>Xanthomonas oryzae</I> pv. <I>oryzae</I> KACC10331. The genes were amplified by polymerase chain reaction (PCR) from <I>X. oryzae</I> pv. <I>oryzae</I> KACC10859 and mutated by transposon insertion; further, marker exchange was performed with the target genes of the wild type strain. Homologous recombination events were confirmed by PCR and Southern hybridization analysis. We found that the mutant strains <I>eglXoA::Tn5</I>, <I>eglXoB</I>::<I>Tn5</I>, and <I>celXoB</I>::<I>Tn5</I> were completely virulence-deficient. In addition, mutants <I>celbXoA</I>::<I>Tn5</I>, <I>bglXoC</I>::<I>Tn5</I>, and <I>bglXoF</I>::<I>Tn5</I> showed attenuated virulence, while the virulence of other mutants was not affected.</P> <P><B>Graphical abstract</B></P><P><ce:figure id='dfig1'></ce:figure></P><P><B>Highlights</B></P><P>► Twelve cellulase genes in <I>X. oryzae</I> pv. <I>oryzae</I> genome were mutated by transposon insertion. ► Pathogenicity and complementation of the mutants were assayed on rice leaves. ► <I>eglXoA, celXoB</I>, <I>celbXoA, bglXoC</I> and <I>bglXoF</I> were identified as novel pathogenicity-related genes.</P>
( Uyangaa Temuujin ),( Jae Seon Park ),( Soon Kwang Hong ) 한국미생물 · 생명공학회 2016 Journal of microbiology and biotechnology Vol.26 No.9
The SCO0284 gene of Streptomyces coelicolor A3(2) is predicted to encode an α-galactosidase (680 amino acids) belonging to glycoside hydrolase family 27. In this study, the SCO0284 coding region was cloned and overexpressed in Streptomyces lividans TK24. The mature form of SCO0284 (641 amino acids, 68 kDa) was purified from culture broth by gel filtration chromatography, with 83.3-fold purification and a yield of 11.2%. Purified SCO0284 showed strong activity against p-nitrophenyl-α-D-galactopyranoside, melibiose, raffinose, and stachyose, and no activity toward lactose, agar (galactan), and neoagarooligosaccharides, indicating that it is an α-galactosidase. Optimal enzyme activity was observed at 40°C and pH 7.0. The addition of metal ions or EDTA did not affect the enzyme activity, indicating that no metal cofactor is required. The kinetic parameters Vmax and Km for p-nitrophenyl α Dgalactopyranoside were 1.6 mg/ml (0.0053 M) and 71.4 U/mg, respectively. Thin-layer chromatography and mass spectrometry analysis of the hydrolyzed products of melibiose, raffinose, and stachyose showed perfect matches with the masses of the sodium adducts of the hydrolyzed products, galactose (M+Na, 203), melibiose (M+Na, 365), and raffinose (M+Na, 527), respectively, indicating that it specifically cleaves the α-1,6-glycosidic bond of the substrate, releasing the terminal D-galactose.
Jadambaa Temuujin 한양대학교 세라믹연구소 2017 Journal of Ceramic Processing Research Vol.18 No.2
Influence of Cerium oxide (CeO2) addition in crystallization behavior and mechanical properties of glass ceramics in the Na2OCaO-Al2O3-SiO2system have been studied. Thermal behavior and hardness were studied by DTA-TG and indentationtechniques respectively. Glass ceramic precursors were prepared by fusing fly ash, window glass and fluorite either with(0.5 wt.%) or without cerium oxide at 1500 oC for 4 hrs followed by quenching in cold water. Crystallization of the amorphousprecursor occurred after 30 min at 800 oC forming plagioclase-type minerals. Hardness of the glass ceramics sintered at1000 oC was 5.66 GPa, while in the sample with cerium oxide was 7.45 GPa.
Uyangaa Temuujin,지원재,박재선,장용근,송재양,홍순광 한국미생물학회 2012 The journal of microbiology Vol.50 No.6
Victivallis vadensis ATCC BAA-548 is a Gram-negative, anaerobic bacterium that was isolated from a human fecal sample. From the genomic sequence of V. vadensis, one gene was found to encode agarase; however, its enzymatic properties have never been characterized. The gene encoding the putative agarase (NCBI reference number ZP_01923925) was cloned by PCR and expressed in E. coli Rosetta-gami by using the inducible T7 promoter of pET28a(+). The expressed protein with a 6×His tag at the N-terminus was named His6-VadG925 and purified as a soluble protein by Ni2+-NTA agarose affinity column chromatography. The purification of the enzyme was 26.8-fold, with a yield of 73.2% and a specific activity of 1.02 U/mg of protein. The purified His6-VadG925 produced a single band with an approximate MW of 155 kDa, which is consistent with the calculated value (154,660 Da) including the 6×His tag. Although VadG925 and many of its homologs were annotated as agarases, it did not hydrolyze agarose. Instead, purified His6-VadG925 hydrolyzed an artificial chromogenic substrate, p-nitrophenyl-β-D-galactopyranoside, but not p-nitrophenyl-α-D-galactopyranoside. The optimum pH and temperature for this β-galactosidase activity were pH 7.0 and 40°C, respectively. The Km and Vmax of His6-VadG925 towards p-nitrophenyl-β-D-galactopyranoside were 1.69 mg/ml (0.0056 M) and 30.3 U/mg, respectively. His6-VadG925 efficiently hydrolyzed lactose into glucose and galactose, which was demonstrated by TLC and mass spectroscopy. These results clearly demonstrated that VadG925 is a novel β-galactosidase that can hydrolyze lactose, which is unusual because of its low homology to validated β-galactosidases.