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Park, Ah-Reum,Kim, Hye-Jung,Lee, Jung-Kul,Oh, Deok-Kun Springer-Verlag 2010 Applied biochemistry and biotechnology Vol.160 No.8
<P>We expressed a putative beta-galactosidase from Sulfolobus acidocaldarius in Escherichia coli and purified the recombinant enzyme using heat treatment and Hi-Trap ion-exchange chromatography. The resultant protein gave a single 57-kDa band by SDS-PAGE and had a specific activity of 58 U/mg. The native enzyme existed as a dimer with a molecular mass of 114 kDa by gel filtration. The maximum activity of this enzyme was observed at pH 5.5 and 90 degrees C. The half-lives of the enzyme at 70, 80, and 90 degrees C were 494, 60, and 0.2 h, respectively. The hydrolytic activity with p-nitrophenyl(pNP) substrates followed the order p-nitrophenyl-beta-D-fucopyranoside>pNP-beta-D-glucopyranoside>pNP-beta-D- galactopyranoside>pNP-beta-D-mannopyranoside>pNP-beta-D-xylopyranoside, but not toward aryl-alpha-glycosides or pNP-beta-L-arabinofuranoside. Thus, the enzyme was actually a beta-glycosidase. The beta-glycosidase exhibited transglycosylation activity with pNP-beta-D-galactopyranoside, pNP-beta-D-glucopyranoside, and pNP-beta-D-fucopyranoside in decreasing order of activity, in the reverse order of its hydrolytic activity. The hydrolytic activity was higher toward cellobiose than toward lactose, but the transglycosylation activity was lower with cellobiose than with lactose.</P>
Biosynthesis of Glycosylated Derivatives of Tylosin in Streptomyces venezuelae
( Ah Reum Han ),( Sung Ryeol Park ),( Je Won Park ),( Eun Yeol Lee ),( Dong Myung Kim ),( Byung Gee Kim ),( Yeo Joon Yoon ) 한국미생물 · 생명공학회 2011 Journal of microbiology and biotechnology Vol.21 No.6
Streptomyces venezuelae YJ028, bearing a deletion of the entire biosynthetic gene cluster encoding the pikromycin polyketide synthases and desosamine biosynthetic enzymes, was used as a bioconversion system for combinatorial biosynthesis of glycosylated derivatives of tylosin. Two engineered deoxysugar biosynthetic pathways for the biosynthesis of TDP-3-O-demethyl-D-chalcose or TDP-Lrhamnose in conjunction with the glycosyltransferaseauxiliary protein pair DesVII/DesVIII were expressed in a S. venezuelae YJ028 mutant strain. Supplementation of each mutant strain capable of producing TDP-3-O-demethyl- D-chalcose or TDP-L-rhamnose with tylosin aglycone tylactone resulted in the production of the 3-O-demethyl- D-chalcose, D-quinovose, or L-rhamnose-glycosylated tylactone.
Park, Ah Reum,Park, Jeong-Hoon,Ahn, Hye-Jin,Jang, Ji Yeon,Yu, Byung Jo,Um, Byung-Hwan,Yoon, Jeong-Jun The Korean Society of Mycology 2015 Mycobiology Vol.43 No.1
${\beta}$-Glucosidase, which hydrolyzes cellobiose into two glucoses, plays an important role in the process of saccharification of the lignocellulosic biomass. In this study, we optimized the activity of ${\beta}$-glucosidase of brown-rot fungus Fomitopsis pinicola KCTC 6208 using the response surface methodology (RSM) with various concentrations of glucose, yeast extract and ascorbic acid, which are the most significant nutrients for activity of ${\beta}$-glucosidase. The highest activity of ${\beta}$-glucosidase was achieved 3.02% of glucose, 4.35% of yeast extract, and 7.41% ascorbic acid where ascorbic acid was most effective. The maximum activity of ${\beta}$-glucosidase predicted by the RSM was 15.34 U/mg, which was similar to the experimental value 14.90 U/mg at the 16th day of incubation. This optimized activity of ${\beta}$-glucosidase was 23.6 times higher than the preliminary activity value, 0.63 U/mg, and was also much higher than previous values reported in other fungi strains. Therefore, a simplified medium supplemented with a cheap vitamin source, such as ascorbic acid, could be a cost effective mean of increasing ${\beta}$-glucosidase activity.
Effect of genetic background differences between FVB and C57BL/6 mice in SARS-CoV-2 infection
Ah-Reum Kang,Hyun Ah Noh,Jae Hyung Son,Sun-Min Seo,Ji-Hun Lee,Na-Won Kim,Eun-Seon Yoo,Han-Bi Jeong,Da In On,Ji Yun Jang,Jun-Won Yun,Jun Won Park,Kang-Seuk Choi,Ho-Young Lee,Jun-Young Seo,Ki Taek Nam,J 한국실험동물학회 2022 한국실험동물학회 학술발표대회 논문집 Vol.2022 No.7
( Ah Reum Park ),( Jeong Hoon Park ),( Hye Jin Ahn ),( Ji Yeon Jang ),( Byung Jo Yu ),( Byung Hwan Um ),( Jeong Jun Yoon ) 한국균학회 2015 韓國菌學會誌 Vol.43 No.1
β-Glucosidase, which hydrolyzes cellobiose into two glucoses, plays an important role in the process of saccharification of the lignocellulosic biomass. In this study, we optimized the activity of β-glucosidase of brown-rot fungus Fomitopsis pinicola KCTC 6208 using the response surface methodology (RSM) with various concentrations of glucose, yeast extract and ascorbic acid, which are the most significant nutrients for activity of β-glucosidase. The highest activity of β-glucosidase was achieved 3.02% of glucose, 4.35% of yeast extract, and 7.41% ascorbic acid where ascorbic acid was most effective. The maximum activity of β-glucosidase predicted by the RSM was 15.34 U/mg, which was similar to the experimental value 14.90 U/mg at the 16th day of incubation. This optimized activity of β-glucosidase was 23.6 times higher than the preliminary activity value, 0.63 U/mg, and was also much higher than previous values reported in other fungi strains. Therefore, a simplified medium supplemented with a cheap vitamin source, such as ascorbic acid, could be a cost effective mean of increasing β-glucosidase activity.
( Ah Reum Park ),( Joo Hee Hong ),( Jae Jin Kim ),( Jeong Jun Yoon ) 한국균학회 2012 Mycobiology Vol.40 No.3
A β-glucosidase from Penicillium italicum was purified with a specific activity of 61.8 U/mg, using a chromatography system. The native form of the enzyme was an 88.5-kDa tetramer with a molecular mass of 354 kDa. Optimum activity was observed at pH 4.5 and 60oC, and the half-lives were 1,737, 330, 34, and 1 hr at 50, 55, 60, and 65oC, respectively. Its activity was inhibited by 47% by 5 mM Ni2+. The enzyme exhibited hydrolytic activity for p-nitrophenyl-β-D-glucopyranoside (pNP-Glu), p-nitrophenyl-β-D-cellobioside, p-nitrophenyl-β-D-xyloside, and cellobiose, however, no activity was observed for p-nitrophenyl- β-D-lactopyranoside, p-nitrophenyl-β-D-galactopyranoside, carboxymetyl cellulose, xylan, and cellulose, indicating that the enzyme was a β-glucosidase. The kcat/Km (s-1 mM-1) values for pNP-Glu and cellobiose were 15,770.4 mM and 6,361.4 mM, respectively. These values were the highest reported for β-glucosidases. Non-competitive inhibition of the enzyme by both glucose (Ki = 8.9 mM) and glucono-δ-lactone (Ki = 11.3 mM) was observed when pNP-Glu was used as the substrate. This is the first report of non-competitive inhibition of β-glucosidase by glucose and glucono-δ-lactone.