메뉴 건너뛰기




Volumn 46, Issue 2, 2011, Pages 448-457

Synthesis of a novel prebiotic trisaccharide by a type i α-glucosidase from B. licheniformis strain TH4-2

Author keywords

Glucosidase; B. licheniformis; Melibiose; Oligosaccharide synthesis; Sucrose; Transglucosylation

Indexed keywords

B. LICHENIFORMIS; GLUCOSIDASE; MELIBIOSE; OLIGOSACCHARIDE SYNTHESIS; SUCROSE; TRANSGLUCOSYLATION;

EID: 78650726917     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2010.09.018     Document Type: Article
Times cited : (20)

References (37)
  • 1
    • 35148893576 scopus 로고    scopus 로고
    • Enzymatic synthesis of polyglucosyl-fructosides from sucrose alone by a novel α-glucosidase isolated from the digestive juice of Archachatina ventricosa (Achatinideae)
    • R.Y. Soro, J.K. Diopoh, R.M. Willemot, and D. Combes Enzymatic synthesis of polyglucosyl-fructosides from sucrose alone by a novel α-glucosidase isolated from the digestive juice of Archachatina ventricosa (Achatinideae) Enzyme Microb Technol 42 2007 44 51
    • (2007) Enzyme Microb Technol , vol.42 , pp. 44-51
    • Soro, R.Y.1    Diopoh, J.K.2    Willemot, R.M.3    Combes, D.4
  • 2
    • 0036979741 scopus 로고    scopus 로고
    • New source of the thermostable α-glucosidase suitable for single step starch processing
    • A. Zdzieblo, and J. Synowiecki New source of the thermostable α-glucosidase suitable for single step starch processing Food Chem 79 2002 485 491
    • (2002) Food Chem , vol.79 , pp. 485-491
    • Zdzieblo, A.1    Synowiecki, J.2
  • 3
    • 3242716846 scopus 로고    scopus 로고
    • Purification and characterization of Acremonium implicatum α-glucosidase having regioselectivity for α-1,3-glucosidic linkage
    • T. Yamamoto, T. Unno, Y. Watanabe, M. Yamamoto, M. Okuyama, and H. Mori Purification and characterization of Acremonium implicatum α-glucosidase having regioselectivity for α-1,3-glucosidic linkage Biochim Biophys Acta 1700 2004 189 198
    • (2004) Biochim Biophys Acta , vol.1700 , pp. 189-198
    • Yamamoto, T.1    Unno, T.2    Watanabe, Y.3    Yamamoto, M.4    Okuyama, M.5    Mori, H.6
  • 4
    • 23744447380 scopus 로고    scopus 로고
    • Purification and characterization of the hyper-glycosylated extracellular α-glucosidase from Schizosaccharomyces pombe
    • M. Okuyama, Y. Tanimota, T. Ito, A. Anzai, H. Mori, and A. Kimura Purification and characterization of the hyper-glycosylated extracellular α-glucosidase from Schizosaccharomyces pombe Enzyme Microb Technol 37 2005 472 480
    • (2005) Enzyme Microb Technol , vol.37 , pp. 472-480
    • Okuyama, M.1    Tanimota, Y.2    Ito, T.3    Anzai, A.4    Mori, H.5    Kimura, A.6
  • 5
    • 0031972297 scopus 로고    scopus 로고
    • Plant α-glucosidases of the glycoside hydrolase family 31. Molecular properties, substrate specificity, reaction mechanism, and comparison with family members of different origin
    • T.P. Frandsen, and B. Svensson Plant α-glucosidases of the glycoside hydrolase family 31. Molecular properties, substrate specificity, reaction mechanism, and comparison with family members of different origin Plant Mol Biol 37 1998 1 13
    • (1998) Plant Mol Biol , vol.37 , pp. 1-13
    • Frandsen, T.P.1    Svensson, B.2
  • 6
    • 33646776730 scopus 로고    scopus 로고
    • A novel α-glucosidase from Chaetomium thermophilum var. coprophilum that converts maltose into trehalose: Purification and partial characterization of the enzyme
    • G.C. Giannesi, M.L.T.M. Polizeli, H.F. Terenzi, and J.A. Jorge A novel α-glucosidase from Chaetomium thermophilum var. coprophilum that converts maltose into trehalose: purification and partial characterization of the enzyme Process Biochem 41 2006 1729 1735
    • (2006) Process Biochem , vol.41 , pp. 1729-1735
    • Giannesi, G.C.1    Polizeli, M.L.T.M.2    Terenzi, H.F.3    Jorge, J.A.4
  • 7
    • 0036664864 scopus 로고    scopus 로고
    • Present status and future of functional oligosaccharides development in Japan
    • T. Nakakuki Present status and future of functional oligosaccharides development in Japan Pure Appl Chem 74 2002 1245 1251
    • (2002) Pure Appl Chem , vol.74 , pp. 1245-1251
    • Nakakuki, T.1
  • 8
    • 52949087971 scopus 로고    scopus 로고
    • Enhancement of the oligosaccharide synthetic activity of β-galactosidase in organic solvents by cyclodextrin
    • W. Srisimarat, and P. Pongsawasdi Enhancement of the oligosaccharide synthetic activity of β-galactosidase in organic solvents by cyclodextrin Enzyme Microb Technol 43 2008 436 441
    • (2008) Enzyme Microb Technol , vol.43 , pp. 436-441
    • Srisimarat, W.1    Pongsawasdi, P.2
  • 9
    • 17344386610 scopus 로고    scopus 로고
    • Towards regioselective synthesis of oligosaccharides by use of α-glucosidases with different substrate specificity
    • S. Mala, H. Dvorakova, R. Hrabal, and B. Kralova Towards regioselective synthesis of oligosaccharides by use of α-glucosidases with different substrate specificity Carbohydr Res 322 1999 209 218
    • (1999) Carbohydr Res , vol.322 , pp. 209-218
    • Mala, S.1    Dvorakova, H.2    Hrabal, R.3    Kralova, B.4
  • 10
    • 35148887289 scopus 로고    scopus 로고
    • Transformation of maltose into prebiotic isomaltooligosaccharides by a novel α-glucosidase from Xantophyllomyces dendrorhous
    • A. Fernandez-Arrojo, D. Marin, A.G.D. Segura, D. Linde, M. Alcalde, and P. Gutierrez-Alonso Transformation of maltose into prebiotic isomaltooligosaccharides by a novel α-glucosidase from Xantophyllomyces dendrorhous Process Biochem 42 2007 1530 1536
    • (2007) Process Biochem , vol.42 , pp. 1530-1536
    • Fernandez-Arrojo, A.1    Marin, D.2    Segura, A.G.D.3    Linde, D.4    Alcalde, M.5    Gutierrez-Alonso, P.6
  • 11
    • 0037127578 scopus 로고    scopus 로고
    • Site-specific mutagenesis at positions 272 and 273 of the Bacillus sp. SAM1606 α-glucosidase to screen mutants with altered specificity for oligosaccharide production by transglucosylation
    • M. Okada, T. Nakayama, A. Noguchi, M. Yano, H. Hemmi, and T. Nishino Site-specific mutagenesis at positions 272 and 273 of the Bacillus sp. SAM1606 α-glucosidase to screen mutants with altered specificity for oligosaccharide production by transglucosylation J Mol Catal B Enzym 16 2002 265 274
    • (2002) J Mol Catal B Enzym , vol.16 , pp. 265-274
    • Okada, M.1    Nakayama, T.2    Noguchi, A.3    Yano, M.4    Hemmi, H.5    Nishino, T.6
  • 12
    • 9144273061 scopus 로고    scopus 로고
    • Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species
    • M.W. Rey, P. Ramaiya, B.A. Nelson, S.D. Brody-Karpin, E.J. Zaretsky, and M. Tang Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species Genome Biol 5 2004 R77
    • (2004) Genome Biol , vol.5 , pp. 77
    • Rey, M.W.1    Ramaiya, P.2    Nelson, B.A.3    Brody-Karpin, S.D.4    Zaretsky, E.J.5    Tang, M.6
  • 13
    • 0037163865 scopus 로고    scopus 로고
    • Characterization of a thermostable levansucrase from Bacillus sp. TH4-2 capable of producing high molecular weight levan at high temperature
    • Y.B. Ammar, T. Matsubara, K. Ito, M. Iizuka, T. Limpaseni, and P. Pongsawasdi Characterization of a thermostable levansucrase from Bacillus sp. TH4-2 capable of producing high molecular weight levan at high temperature J Biotechnol 99 2002 111 119
    • (2002) J Biotechnol , vol.99 , pp. 111-119
    • Ammar, Y.B.1    Matsubara, T.2    Ito, K.3    Iizuka, M.4    Limpaseni, T.5    Pongsawasdi, P.6
  • 14
    • 33750423631 scopus 로고
    • Notes on sugar determination
    • M. Somogyi Notes on sugar determination J Biol Chem 195 1952 19 23
    • (1952) J Biol Chem , vol.195 , pp. 19-23
    • Somogyi, M.1
  • 15
    • 0017184389 scopus 로고
    • A rapid and sensititive method for the quantification of microgram quantities of protein using the principle of protein-dye binding
    • M. Bradford A rapid and sensititive method for the quantification of microgram quantities of protein using the principle of protein-dye binding Anal Biochem 72 1976 248 254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.1
  • 16
    • 0014478917 scopus 로고
    • Determination of enzymatic activity in polyacrylamide gels
    • O. Gabriel, and S.F. Wang Determination of enzymatic activity in polyacrylamide gels Anal Biochem 27 1969 545 554
    • (1969) Anal Biochem , vol.27 , pp. 545-554
    • Gabriel, O.1    Wang, S.F.2
  • 17
    • 0026514916 scopus 로고
    • Improving accuracy of glucose oxidase procedure for glucose determinations on discrete analyzers
    • N.O. Leary, A. Pembroke, and P.F. Duggan Improving accuracy of glucose oxidase procedure for glucose determinations on discrete analyzers Clin Chem 38 2 1992 298 302
    • (1992) Clin Chem , vol.38 , Issue.2 , pp. 298-302
    • Leary, N.O.1    Pembroke, A.2    Duggan, P.F.3
  • 18
    • 33845602014 scopus 로고    scopus 로고
    • Multiple form of α-glucosidase in rice seeds (Oryza sativa L., var Nipponbare)
    • H. Nakai, T. Ito, M. Hayashi, K. Kamiya, T. Yamamoto, and K. Matsubara Multiple form of α-glucosidase in rice seeds (Oryza sativa L., var Nipponbare) Biochim 89 2007 49 62
    • (2007) Biochim , vol.89 , pp. 49-62
    • Nakai, H.1    Ito, T.2    Hayashi, M.3    Kamiya, K.4    Yamamoto, T.5    Matsubara, K.6
  • 19
    • 17444370100 scopus 로고    scopus 로고
    • Purification of an α-glucosidase from germinating millet seeds
    • Y. Yamasaki, M. Fujimoto, J. Kariya, and H. Konno Purification of an α-glucosidase from germinating millet seeds Phytochemistry 66 2005 851 857
    • (2005) Phytochemistry , vol.66 , pp. 851-857
    • Yamasaki, Y.1    Fujimoto, M.2    Kariya, J.3    Konno, H.4
  • 20
    • 0037272612 scopus 로고    scopus 로고
    • Purification and characterization of rice α-glucosidase, a key enzyme for alcohol fermentation of rice polish
    • H. Iwata, T. Suzuki, and I. Aramaki Purification and characterization of rice α-glucosidase, a key enzyme for alcohol fermentation of rice polish J Biosci Bioeng 95 1 2003 106 108
    • (2003) J Biosci Bioeng , vol.95 , Issue.1 , pp. 106-108
    • Iwata, H.1    Suzuki, T.2    Aramaki, I.3
  • 21
    • 27644570786 scopus 로고    scopus 로고
    • α-Glucosidase from a strain of deep-sea Geobacillus: A potential enzyme for the synthesis of complex carbohydrates
    • V.S. Hung, Y. Hatada, S. Goda, J. Lu, Y. Hidaka, and Z. Li α-Glucosidase from a strain of deep-sea Geobacillus: a potential enzyme for the synthesis of complex carbohydrates Appl Microbiol Biotechnol 68 2005 757 765
    • (2005) Appl Microbiol Biotechnol , vol.68 , pp. 757-765
    • Hung, V.S.1    Hatada, Y.2    Goda, S.3    Lu, J.4    Hidaka, Y.5    Li, Z.6
  • 22
    • 0030570989 scopus 로고    scopus 로고
    • Purification and characterization of α-glucosidase complex from the intestine of the frog, Rana japonica
    • Y. Takesue, and S. Takesue Purification and characterization of α-glucosidase complex from the intestine of the frog, Rana japonica Biochim Biophys Acta 1296 1996 152 158
    • (1996) Biochim Biophys Acta , vol.1296 , pp. 152-158
    • Takesue, Y.1    Takesue, S.2
  • 23
    • 0033113677 scopus 로고    scopus 로고
    • Properties of maltose-inducible α-glucosidase MalL (sucrase-isomaltase-maltase) in Bacillus subtilis: Evidence for its contribution to maltodextrin utilization
    • S. Schonert, T. Buder, and M.K. Dahl Properties of maltose-inducible α-glucosidase MalL (sucrase-isomaltase-maltase) in Bacillus subtilis: evidence for its contribution to maltodextrin utilization Res Microbiol 150 1999 167 177
    • (1999) Res Microbiol , vol.150 , pp. 167-177
    • Schonert, S.1    Buder, T.2    Dahl, M.K.3
  • 24
    • 0022480506 scopus 로고
    • Resolution, purification and characterization of two extracelluar glucohydrolases, α-glucosidase and maltase, of Bacillus licheniformis
    • C. Kelly, M. Giblin, and W.M. Fogarty Resolution, purification and characterization of two extracelluar glucohydrolases, α-glucosidase and maltase, of Bacillus licheniformis Can J Microbiol 32 1986 342 347
    • (1986) Can J Microbiol , vol.32 , pp. 342-347
    • Kelly, C.1    Giblin, M.2    Fogarty, W.M.3
  • 25
    • 0023614198 scopus 로고
    • Synthesis of two distinct α-glucosidase activities in Bacillus licheniformis
    • J. Moore, and F.G. Priest Synthesis of two distinct α-glucosidase activities in Bacillus licheniformis Lett Appl Microb 4 1987 1 3
    • (1987) Lett Appl Microb , vol.4 , pp. 1-3
    • Moore, J.1    Priest, F.G.2
  • 26
    • 71749096642 scopus 로고    scopus 로고
    • Purification and partial characterization of midgut membrane-bound α-glucosidase from Quesada gigas (Hemiptera: Cicadidae)
    • F.V. Fonseca, J.R. Silva, R.I. Samuels, R.A. Damatta, W.R. Terra, and C.P. Silva Purification and partial characterization of midgut membrane-bound α-glucosidase from Quesada gigas (Hemiptera: Cicadidae) Comp Biochem Physiol 155B 2010 20 25
    • (2010) Comp Biochem Physiol , vol.155 , pp. 20-25
    • Fonseca, F.V.1    Silva, J.R.2    Samuels, R.I.3    Damatta, R.A.4    Terra, W.R.5    Silva, C.P.6
  • 27
    • 33746164361 scopus 로고    scopus 로고
    • Purification, characterization, and synergistic action of phytate-resistant α-amylase and α-glucosidase from Geobacillus thermodenitrificans HRO10
    • T.C. Ezeji, and H. Bahl Purification, characterization, and synergistic action of phytate-resistant α-amylase and α-glucosidase from Geobacillus thermodenitrificans HRO10 J Biotechnol 125 2006 27 38
    • (2006) J Biotechnol , vol.125 , pp. 27-38
    • Ezeji, T.C.1    Bahl, H.2
  • 28
    • 1542376212 scopus 로고    scopus 로고
    • Purification and biochemical characterization of a membrane-bound α-glucosidase from the parasite Entamoeba histolytica
    • J.C. Bravo-Torres, J.C. Villagomez-Castro, C. Calvo-Mendez, A. Flores-Carreon, and E. Lopez-Romero Purification and biochemical characterization of a membrane-bound α-glucosidase from the parasite Entamoeba histolytica J Parasitol 34 2004 455 462
    • (2004) J Parasitol , vol.34 , pp. 455-462
    • Bravo-Torres, J.C.1    Villagomez-Castro, J.C.2    Calvo-Mendez, C.3    Flores-Carreon, A.4    Lopez-Romero, E.5
  • 29
    • 0034220797 scopus 로고    scopus 로고
    • The primary structure of the subunit in Bacillus thermoamyloliquefaciens KP1071 molecular weight 540,000 homohexameric alpha-glucosidase II belonging to the glycosyl hydrolase family 31
    • S. Kashiwabara, S. Azuma, M. Tsuduki, and Y. Suzuki The primary structure of the subunit in Bacillus thermoamyloliquefaciens KP1071 molecular weight 540,000 homohexameric alpha-glucosidase II belonging to the glycosyl hydrolase family 31 Biosci Biotechnol Biochem 64 7 2000 1379 1393
    • (2000) Biosci Biotechnol Biochem , vol.64 , Issue.7 , pp. 1379-1393
    • Kashiwabara, S.1    Azuma, S.2    Tsuduki, M.3    Suzuki, Y.4
  • 30
    • 15144341062 scopus 로고    scopus 로고
    • Alpha-glucosidase from the hepatopancreas of the shrimp, Penaeus vannamei (Crustacea-Decapoda)
    • P. Chevalier, and A. van Worhmoudt Alpha-glucosidase from the hepatopancreas of the shrimp, Penaeus vannamei (Crustacea-Decapoda) J Exp Zool 280 1998 384 394
    • (1998) J Exp Zool , vol.280 , pp. 384-394
    • Chevalier, P.1    Van Worhmoudt, A.2
  • 31
    • 0031026328 scopus 로고    scopus 로고
    • Altering substrate specificity of Bacillus sp. SAM1606 α-glucosidase by comparative site-specific mutagenesis
    • M. Inohara-Ochiai, T. Nakayama, R. Goto, M. Nakao, T. Ueda, and Y. Shibanoi Altering substrate specificity of Bacillus sp. SAM1606 α-glucosidase by comparative site-specific mutagenesis J Biol Chem 272 1996 1601 1607
    • (1996) J Biol Chem , vol.272 , pp. 1601-1607
    • Inohara-Ochiai, M.1    Nakayama, T.2    Goto, R.3    Nakao, M.4    Ueda, T.5    Shibanoi, Y.6
  • 32
    • 0033945034 scopus 로고    scopus 로고
    • An active-site mutation causes enhanced reactivity and altered regiospecificity of transglucosylation catalyzed by the Bacillus sp. SAM1606 α-glucosidase
    • M. Inohara-Ochiai, M. Okada, T. Nakayama, H. Hemmi, T. Ueda, and T. Iwashita An active-site mutation causes enhanced reactivity and altered regiospecificity of transglucosylation catalyzed by the Bacillus sp. SAM1606 α-glucosidase J Biosci Bioeng 89 5 2000 431 437
    • (2000) J Biosci Bioeng , vol.89 , Issue.5 , pp. 431-437
    • Inohara-Ochiai, M.1    Okada, M.2    Nakayama, T.3    Hemmi, H.4    Ueda, T.5    Iwashita, T.6
  • 34
    • 0242610362 scopus 로고    scopus 로고
    • Purification and biochemical characterization of a soluble α-glucosidase from the parasite Entamoeba histolytica
    • J.C. Bravo-Torres, C. Calvo-Mendez, A. Flores-Carreon, and E. Lopez-Romero Purification and biochemical characterization of a soluble α-glucosidase from the parasite Entamoeba histolytica Antonie Van Leeuwenhoek 84 2003 169 178
    • (2003) Antonie Van Leeuwenhoek , vol.84 , pp. 169-178
    • Bravo-Torres, J.C.1    Calvo-Mendez, C.2    Flores-Carreon, A.3    Lopez-Romero, E.4
  • 35
    • 0032805959 scopus 로고    scopus 로고
    • Immobilization of native and dextran-free dextransucrase from Leuconostoc mesenteroides NRRL B-512F for the synthesis of glucooligosaccharides
    • M. Alcalde, F.J. Plou, G.D. Segura, M. Remaud-Simeon, R.M. Willemot, and P. Monsan Immobilization of native and dextran-free dextransucrase from Leuconostoc mesenteroides NRRL B-512F for the synthesis of glucooligosaccharides Biotechnol Tech 13 1999 749 755
    • (1999) Biotechnol Tech , vol.13 , pp. 749-755
    • Alcalde, M.1    Plou, F.J.2    Segura, G.D.3    Remaud-Simeon, M.4    Willemot, R.M.5    Monsan, P.6
  • 36
    • 0142130952 scopus 로고    scopus 로고
    • Novel oligosaccharides synthesized from sucrose donor and cellobiose acceptor by alternansucrase
    • M.A.A. Morales, M. Remaud-Simeon, R.M. Willemot, M.R. Vignon, and P. Monsan Novel oligosaccharides synthesized from sucrose donor and cellobiose acceptor by alternansucrase Carbohydr Res 331 2001 403 411
    • (2001) Carbohydr Res , vol.331 , pp. 403-411
    • Morales, M.A.A.1    Remaud-Simeon, M.2    Willemot, R.M.3    Vignon, M.R.4    Monsan, P.5
  • 37
    • 67650944994 scopus 로고    scopus 로고
    • Monitoring the hydrolysis and transglycosylation activity of α-glucosidase from Aspergillus niger by nuclear magnetic resonance spectroscopy and mass spectrometry
    • N. Shimba, M. Shinagawa, W. Hoshino, H. Yamaguchi, N. Yamada, and E.I. Suzuki Monitoring the hydrolysis and transglycosylation activity of α-glucosidase from Aspergillus niger by nuclear magnetic resonance spectroscopy and mass spectrometry Anal Biochem 393 2009 23 28
    • (2009) Anal Biochem , vol.393 , pp. 23-28
    • Shimba, N.1    Shinagawa, M.2    Hoshino, W.3    Yamaguchi, H.4    Yamada, N.5    Suzuki, E.I.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.