http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
이영우,이병희,이기은,이순열,임완택 한국미생물학회 2020 미생물학회지 Vol.56 No.1
Mucilaginibacter ginsenosidivorax KHI-28 T (KACC 14955 T = LMG 25804 T ) is Gram-stain-negative, strictly aerobic, nonmotile, non-spore-forming, and rod-shaped. M. ginsenosidivorax was isolated from sediment in a river in Gapcheon, Daejeon, South Korea. Strain KHI-28 T had β-glucosidase activity, responsible for transforming ginsenosides Rb1 and Re into Rg2 and C-K, respectively. The complete genome of M. ginsenosidivorax KHI-28 T revealed a single circular chromosome comprising 7,811,413 bp, with a G + C content of 43.1%. Several glycoside hydrolase-encoding genes were found, which might contribute in converting major ginsenosides to minor ginsenosides and they were expected strong pharmacological effects. In addition, genes encoding nucleotide excision repair enzymes and virulence factors were found.
이지은,이병희,이기은,강명석,임완택 한국미생물학회 2019 미생물학회지 Vol.55 No.4
A Gram-stain-negative, rod-shaped, non-spore-forming, aerobic bacterium, designated Anseongella ginsenosidimutans Gsoil 524 T , was isolated from the soil of a field used for cultivating ginseng. Anseongella ginsenosidimutans Gsoil 524 T showed the ability to convert major ginsenosides to minor ginsenosides, and its whole genome was sequenced. The whole genome of Anseongella ginsenosidimutans Gsoil 524 T consists of a single circular chromosome of 4,322,684 bp, with 49.9% G + C content. Based on the complete genome sequence of strain Gsoil 524 T , we found several glycoside hydrolase-encoding genes that may be involved in the conversion of major ginsenosides into minor ginsenosides and some polysaccharide lyases.
금동호,이병희,이기은,이순열,임완택 한국미생물학회 2019 미생물학회지 Vol.55 No.4
A yellow-colored, circular, convex, rod-shaped baterial strain designated Flavisolibacter ginsenosidimutans Gsoil 636 T was isolated from soil of a ginseng cultivation field in Pocheon Province, South Korea. Gsoil 636 T showed the ability to convert Rb1 (one of the dominant active components of ginseng) to F2, and its whole genome was sequenced. The whole genome of Flavisolibacter ginsenosidimutans Gsoil 636 T consist of a single circular chromosome of 5,079,621 bp, with 48.9% G + C content. Of the 4,338 predicted genes, 4,251 were proteincording genes, 46 were RNAs, and 41 were pseudogenes. Using the complete genome sequence of the strain Gsoil 636 T , we identified several glycoside hydrolase-encoding genes that may be involved in the conversion of major ginsenosides into minor ginsenosides and unexpectedly found antibiotic biosynthesis- encoding genes and excinuclease genes.
금동호,이병희,이기은,이순열,임완택 한국미생물학회 2019 미생물학회지 Vol.55 No.4
A yellow-colored, long rod baterial strain of low convexity, designated Panacibacter ginsenosidivorans Gsoil 1550 T was isolated from soil of a ginseng field collected in Pocheon, Republic of Korea. Gsoil 1550 T showed the ability to convert major ginsenosides Rb1, Rc, and Rd to minor ginsenoside F2, and its whole genome was sequenced. The whole genome sequence of Panacibacter ginsenosidivorans Gsoil 1550 T consisted of one circular chromosome of 5,528,026 bp, with 44.6% G + C content. Of the 4,657 predicted genes, 4,572 were proteincording genes, 52 were RNAs, and 33 were pseudogenes. From the complete genome sequence of the strain Gsoil 1550 T , we found several glycoside hydrolase-encoding genes that may be involved in the conversion of major ginsenosides into minor ginsenosides, antibiotic biosynthesis-encoding genes, and cobalamin B12-binding domain-containing genes.
이영우,시디키 무하마드 주베르,류청매,김대철,임완택,Lee, Young-Woo,Siddiqi, Muhammad Zubair,Liu, Qing-Mei,Kim, Dae-Cheol,Im, Wan-Taek The Microbiological Society of Korea 2018 미생물학회지 Vol.54 No.4
퇴비로부터 분리한 Niabella ginsenosidivorans $BS26^T$ 균주의 유전체서열을 분석하였다. 균주 $BS26^T$의 유전체는 G + C 비율이 44.48%이며, 4,800개의 유전자와 4,704개의 단백질 코딩 유전자, 85개의 위유전자 그리고49개의 RNA유전자를 포함한 단일 원형 염색체로 구성되었으면 그 크기는 5,627,734 bp였다. 균주 $BS26^T$는 인삼사포닌의 당 분해에 관여하는 여러 타입의 글라이코시다제 유전자를 가지고 있었다. 이러한 유전체 분석은 주요 진세노사이드 전환에 관여하는 유전자 특징을 이해하는데 큰 기여가 되었다. An orange-colored, rod-shaped strain, designated Niabella ginsenosidivorans $BS26^T$, was isolated from compost. Strain $BS26^T$ showed the ability to convert major ginsenosides to minor ginsenosides, and its whole genome was sequenced. The whole genome of N. ginsenosidivorans $BS26^T$ consists of a single circular chromosome of 5,627,734 bp with 44.48% G + C content. Based on the complete genome sequence of strain $BS26^T$, we found several glycosides hydrolase-encoding genes that might involve in the conversion of major ginsenosides into minor ginsenoside and deliberate its strong pharmacological effects.
( Wei Li ),( Han Fan ),( Chao He ),( Xuecheng Zhang ),( Xiaotang Wang ),( Jing Yuan ),( Zemin Fang ),( Wei Fang ),( Yazhong Xiao ) 한국미생물 · 생명공학회 2016 Journal of microbiology and biotechnology Vol.26 No.11
A novel α-glucoside hydrolase (named PspAG97A) from glycoside hydrolase family 97 (GH97) was cloned from the deep-sea bacterium Pseudoalteromonas sp. K8, which was screened from the sediment of Kongsfjorden. Sequence analysis showed that PspAG97A belonged to GH97, and shared 41% sequence identity with the characterized α-glucosidase BtGH97a. PspAG97A possessed three key catalytically related glutamate residues. Mutation of the glutamate residues indicated that PspAG97A belonged to the inverting subfamily of GH97. PspAG97A showed significant reversibility against changes in salt concentration. It exhibited halophilic ability and improved thermostability in NaCl solution, with maximal activity at 1.0 M NaCl/KCl, and retained more than 80% activity at NaCl concentrations ranging from 0.8 to 2.0 M for over 50 h. Furthermore, PspAG97A hydrolyzed not only α-1,4-glucosidic linkage, but also α-1,6- and α-1,2-glucosidic linkages. Interestingly, PspAG97A possessed high catalytic efficiency for long-chain substrates with α-1,6-linkage. These characteristics are clearly different from other known α-glucoside hydrolases in GH97, implying that PspAG97A is a unique α-glucoside hydrolase of GH97.
( Christiane Liers ),( Rene Ullrich ),( Harald Kellner ),( Do Huu Chi ),( Dang Thu Quynh ),( Nguyen Dinh Luyen ),( Le Mai Huong ),( Martin Hofrichter ),( Do Huu Nghi ) 한국미생물 · 생명공학회 2021 Journal of microbiology and biotechnology Vol.31 No.10
A bifunctional glycoside hydrolase GH78 from the ascomycete Xylaria polymorpha (XpoGH78) possesses catalytic versatility towards both glycosides and esters, which may be advantageous for the efficient degradation of the plant cell-wall complex that contains both diverse sugar residues and esterified structures. The contribution of XpoGH78 to the conversion of lignocellulosic materials without any chemical pretreatment to release the water-soluble aromatic fragments, carbohydrates, and methanol was studied. The disintegrating effect of enzymatic lignocellulose treatment can be significantly improved by using different kinds of hydrolases and phenoloxidases. The considerable changes in low (3 kDa), medium (30 kDa), and high (> 200 kDa) aromatic fragments were observed after the treatment with XpoGH78 alone or with this potent cocktail. Synergistic conversion of rape straw also resulted in a release of 17.3 mg of total carbohydrates (e.g., arabinose, galactose, glucose, mannose, xylose) per gram of substrate after incubating for 72 h. Moreover, the treatment of rape straw with XpoGH78 led to a marginal methanol release of approximately 17 μg/g and improved to 270 μg/g by cooperation with the above accessory enzymes. In the case of beech wood conversion, the combined catalysis by XpoGH78 and laccase caused an effect comparable with that of fungal strain X. polymorpha in woody cultures concerning the liberation of aromatic lignocellulose fragments.
Jeon, E.J.,Jung, J.H.,Seo, D.H.,Jung, D.H.,Holden, J.F.,Park, C.S. IPC Science and Technology Press ; Elsevier Scienc 2014 Enzyme and microbial technology Vol.60 No.-
Maltose-forming α-amylase is a glycoside hydrolase family 57 (GH57) member that is unique because it displays dual hydrolysis activity toward α-1,4- and α-1,6-glycosidic linkages and only recognizes maltose. This enzyme was previously identified only in Pyrococcus sp. ST04 (PSMA); however, we recently found two homologs subgroups in Thermococcus species. One subgroup (subgroup A) showed relatively high amino acid sequence similarity to PSMA (>71%), while the other subgroup (subgroup B) showed lower homology with PSMA (<59%). To characterize the subgroup B maltose-forming α-amylase from Thermococcus species (TCMA), we cloned the CL1_0868 gene from Thermococcus sp. CL1 and then successfully expressed the gene in Escherichia coli. Although TCMA has a different oligomeric state relative to PSMA, TCMA showed similar substrate specificity. However, TCMA was shown to hydrolyze maltooligosaccharides more easily than PSMA. Also, TCMA displayed different optimum conditions depending on the glycosidic linkage of the substrate. TCMA had the highest activity at 85<SUP>o</SUP>C and at pH 5.0 for α-1,4-glycosidic linkage hydrolysis whereas it showed its maximal activity to cleave α-1,6-glycosidic linkages at 98<SUP>o</SUP>C and pH 6.0.