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Volumn 121, Issue 3, 2016, Pages 259-264

Purification and enzymatic characterization of a novel β-1,6-glucosidase from Aspergillus oryzae

Author keywords

Aspergillus oryzae; Gentiobiose; Glycoside hydrolase family 3; 1,6 Glucosidase; Glucosidase

Indexed keywords

DIMETHYL SULFOXIDE; ENCODING (SYMBOLS); ENZYMES; ETHYLENEDIAMINETETRAACETIC ACID; GENE ENCODING; GENES; HYDROLASES; PURIFICATION; SUGARS;

EID: 84959074840     PISSN: 13891723     EISSN: 13474421     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2015.07.011     Document Type: Article
Times cited : (34)

References (27)
  • 2
    • 0036448608 scopus 로고    scopus 로고
    • Microbial β-glucosidases: cloning, properties, and applications
    • Bhatia Y., Mishra S., Bisaria V.S. Microbial β-glucosidases: cloning, properties, and applications. Crit. Rev. Biotechnol. 2002, 22:375-407.
    • (2002) Crit. Rev. Biotechnol. , vol.22 , pp. 375-407
    • Bhatia, Y.1    Mishra, S.2    Bisaria, V.S.3
  • 3
    • 21044437345 scopus 로고    scopus 로고
    • Developing promiscuous glycosidases for glycoside synthesis. Residues W433 and E432 in Sulfolobus solfataricus β-glycosidase are important glucoside- and galactoside-specificity determinants
    • Hancock S.M., Corbett K., Fordham-Skelton A.P., Gatehouse J.A., Davis B.G. Developing promiscuous glycosidases for glycoside synthesis. Residues W433 and E432 in Sulfolobus solfataricus β-glycosidase are important glucoside- and galactoside-specificity determinants. Chembiochem 2005, 6:866-875.
    • (2005) Chembiochem , vol.6 , pp. 866-875
    • Hancock, S.M.1    Corbett, K.2    Fordham-Skelton, A.P.3    Gatehouse, J.A.4    Davis, B.G.5
  • 4
    • 0034681333 scopus 로고    scopus 로고
    • Cloning, expression, characterization, and nucleophile identification of family 3, Aspergillus niger β-glucosidase
    • Siegel D., Ira M., Mara D., Ben-Ami B., Shouming H., Stephen G.W., Oded S. Cloning, expression, characterization, and nucleophile identification of family 3, Aspergillus niger β-glucosidase. J. Biol. Chem. 2000, 275:4973-4980.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4973-4980
    • Siegel, D.1    Ira, M.2    Mara, D.3    Ben-Ami, B.4    Shouming, H.5    Stephen, G.W.6    Oded, S.7
  • 5
    • 84880056854 scopus 로고    scopus 로고
    • Characterization of a novel β-glucosidase from a compost microbial metagenome with strong transglycosylation activity
    • Uchiyama T., Miyazaki K., Yaoi K. Characterization of a novel β-glucosidase from a compost microbial metagenome with strong transglycosylation activity. J. Biol. Chem. 2013, 288:18325-18334.
    • (2013) J. Biol. Chem. , vol.288 , pp. 18325-18334
    • Uchiyama, T.1    Miyazaki, K.2    Yaoi, K.3
  • 6
    • 80055003418 scopus 로고    scopus 로고
    • Characterization of novel β-glucosidases with transglycosylation properties from Trichosporon asahii
    • Wang Y., Li J., Xu Y. Characterization of novel β-glucosidases with transglycosylation properties from Trichosporon asahii. J. Agric. Food Chem. 2011, 59:11219-11227.
    • (2011) J. Agric. Food Chem. , vol.59 , pp. 11219-11227
    • Wang, Y.1    Li, J.2    Xu, Y.3
  • 7
    • 84883008814 scopus 로고    scopus 로고
    • Two-step purification of a novel β-glucosidase with high transglycosylation activity and another hypothetical β-glucosidase in Aspergillus oryzae HML366 and enzymatic characterization
    • He H., Qin Y., Chen G., Li N., Liang Z. Two-step purification of a novel β-glucosidase with high transglycosylation activity and another hypothetical β-glucosidase in Aspergillus oryzae HML366 and enzymatic characterization. Appl. Biochem. Biotechnol. 2013, 169:870-884.
    • (2013) Appl. Biochem. Biotechnol. , vol.169 , pp. 870-884
    • He, H.1    Qin, Y.2    Chen, G.3    Li, N.4    Liang, Z.5
  • 8
    • 84946483652 scopus 로고    scopus 로고
    • Purification and enzymatic characterization of secretory glycoside hydrolase family 3 (GH3) aryl β-glucosidases screened from Aspergillus oryzae genome
    • Kudo K., Watanabe A., Ujiie S., Shintani T., Gomi K. Purification and enzymatic characterization of secretory glycoside hydrolase family 3 (GH3) aryl β-glucosidases screened from Aspergillus oryzae genome. J. Biosci. Bioeng. 2015, 120:614-623.
    • (2015) J. Biosci. Bioeng. , vol.120 , pp. 614-623
    • Kudo, K.1    Watanabe, A.2    Ujiie, S.3    Shintani, T.4    Gomi, K.5
  • 10
    • 33749545443 scopus 로고    scopus 로고
    • Development of high expression system with the improved promoter using the cis-acting element in Aspergilus species
    • Minetoki T., Tsuboi H., Koda A., Ozeki K. Development of high expression system with the improved promoter using the cis-acting element in Aspergilus species. J. Biol. Macromol. 2003, 3:89-96.
    • (2003) J. Biol. Macromol. , vol.3 , pp. 89-96
    • Minetoki, T.1    Tsuboi, H.2    Koda, A.3    Ozeki, K.4
  • 11
    • 85004562322 scopus 로고
    • Integrative transformation of Aspergillus oryzae with a plasmid containing the Aspergillus nidulans argB gene
    • Gomi K., Iimura Y., Hara S. Integrative transformation of Aspergillus oryzae with a plasmid containing the Aspergillus nidulans argB gene. Agric. Biol. Chem. 1987, 51:2549-2555.
    • (1987) Agric. Biol. Chem. , vol.51 , pp. 2549-2555
    • Gomi, K.1    Iimura, Y.2    Hara, S.3
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 0031685554 scopus 로고    scopus 로고
    • Purification, characterization, and substrate specificity of a novel highly glucose-tolerant β-glucosidase from Aspergillus oryzae
    • Riou C., Salmon J.M., Vallier M.J., Gunata Z., Barre P. Purification, characterization, and substrate specificity of a novel highly glucose-tolerant β-glucosidase from Aspergillus oryzae. Appl. Environ. Microbiol. 1998, 64:3607-3614.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 3607-3614
    • Riou, C.1    Salmon, J.M.2    Vallier, M.J.3    Gunata, Z.4    Barre, P.5
  • 14
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • Lineweaver H., Burk D. The determination of enzyme dissociation constants. J. Am. Chem. Soc. 1934, 56:658-666.
    • (1934) J. Am. Chem. Soc. , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 15
    • 0013770017 scopus 로고
    • Inhibition of glycosidases by aldonolactones of corresponding configuration
    • Lewy G.A., Hay A.J., Conchie J. Inhibition of glycosidases by aldonolactones of corresponding configuration. Biochem. J. 1964, 91:378-384.
    • (1964) Biochem. J. , vol.91 , pp. 378-384
    • Lewy, G.A.1    Hay, A.J.2    Conchie, J.3
  • 16
    • 0035091719 scopus 로고    scopus 로고
    • β-Glucosidase multiplicity from Aspergillus tubingensis CBS 643.92: purification and characterization of four β-glucosidases and their differentiation with respect to substrate specificity, glucose inhibition and acid tolerance
    • Decker C.H., Visser J., Schreier P. β-Glucosidase multiplicity from Aspergillus tubingensis CBS 643.92: purification and characterization of four β-glucosidases and their differentiation with respect to substrate specificity, glucose inhibition and acid tolerance. Appl. Microbiol. Biotechnol. 2001, 55:157-163.
    • (2001) Appl. Microbiol. Biotechnol. , vol.55 , pp. 157-163
    • Decker, C.H.1    Visser, J.2    Schreier, P.3
  • 17
    • 0016856650 scopus 로고
    • Purification and properties of a β-1,6-glucosidase from Flavobacterium
    • Sano K., Amemura A., Harada T. Purification and properties of a β-1,6-glucosidase from Flavobacterium. Biochim. Biophys. Acta 1975, 377:410-420.
    • (1975) Biochim. Biophys. Acta , vol.377 , pp. 410-420
    • Sano, K.1    Amemura, A.2    Harada, T.3
  • 18
    • 0003126327 scopus 로고
    • Cyanide and cyanogenic glycosides
    • Academic Press, New York, G.A. Rosenthal, D.H. Janzen (Eds.)
    • Conn E.E. Cyanide and cyanogenic glycosides. Herbivores, their interactions with secondary plant metabolites 1979, 387-412. Academic Press, New York. G.A. Rosenthal, D.H. Janzen (Eds.).
    • (1979) Herbivores, their interactions with secondary plant metabolites , pp. 387-412
    • Conn, E.E.1
  • 19
    • 0029240490 scopus 로고
    • A β-glucosidase from lodgepole pine specific for the lignin precursor coniferin
    • Dharmawardhana D.P., Ellis B.E., Carlson J.E. A β-glucosidase from lodgepole pine specific for the lignin precursor coniferin. Plant Physiol. 1995, 107:331-339.
    • (1995) Plant Physiol. , vol.107 , pp. 331-339
    • Dharmawardhana, D.P.1    Ellis, B.E.2    Carlson, J.E.3
  • 20
    • 0029346981 scopus 로고
    • Expression of a zeatin-O-glucoside-degrading β-glucosidase in Brassica napus
    • Falk A., Rask L. Expression of a zeatin-O-glucoside-degrading β-glucosidase in Brassica napus. Plant Physiol. 1995, 108:1369-1377.
    • (1995) Plant Physiol. , vol.108 , pp. 1369-1377
    • Falk, A.1    Rask, L.2
  • 21
    • 56149109469 scopus 로고    scopus 로고
    • Genomics of Aspergillus oryzae: learning from the history of koji mold and exploration of its future
    • Machida M., Yamada O., Gomi K. Genomics of Aspergillus oryzae: learning from the history of koji mold and exploration of its future. DNA Res. 2008, 15:173-183.
    • (2008) DNA Res. , vol.15 , pp. 173-183
    • Machida, M.1    Yamada, O.2    Gomi, K.3
  • 22
  • 23
    • 4544335713 scopus 로고    scopus 로고
    • Isolation and characterization of a novel gene encoding α-l-arabinofuranosidase from Aspergillus oryzae
    • Matsumura K., Obata H., Hata Y., Kawato A., Abe Y., Akita O. Isolation and characterization of a novel gene encoding α-l-arabinofuranosidase from Aspergillus oryzae. J. Biosci. Bioeng. 2004, 98:77-84.
    • (2004) J. Biosci. Bioeng. , vol.98 , pp. 77-84
    • Matsumura, K.1    Obata, H.2    Hata, Y.3    Kawato, A.4    Abe, Y.5    Akita, O.6
  • 24
    • 33751538146 scopus 로고    scopus 로고
    • Molecular cloning and characterization of two intracellular β-glucosidases belonging to glycoside hydrolase family 1 from the basidiomycete Phanerochaete chrysosporium
    • Tsukada T., Igarashi K., Yoshida M., Samejima M. Molecular cloning and characterization of two intracellular β-glucosidases belonging to glycoside hydrolase family 1 from the basidiomycete Phanerochaete chrysosporium. Appl. Microbiol. Biotechnol. 2006, 73:807-814.
    • (2006) Appl. Microbiol. Biotechnol. , vol.73 , pp. 807-814
    • Tsukada, T.1    Igarashi, K.2    Yoshida, M.3    Samejima, M.4
  • 25
    • 33646506148 scopus 로고    scopus 로고
    • Substrate specificity of Aspergillus oryzae family 3 beta- glucosidase
    • Langston J., Sheehy N., Xu F. Substrate specificity of Aspergillus oryzae family 3 beta- glucosidase. Biochim. Biophys. Acta 2006, 1764:972-978.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 972-978
    • Langston, J.1    Sheehy, N.2    Xu, F.3
  • 26
    • 79960500791 scopus 로고    scopus 로고
    • Industrial production and higher application of functional β-glucooligosaccharides having a bitter taste
    • Unno T., Nakakuki T., Fujimoto Y., Okada G., Kainuma S., Goda T. Industrial production and higher application of functional β-glucooligosaccharides having a bitter taste. J. Appl. Glycosci. 2005, 52:59-64.
    • (2005) J. Appl. Glycosci. , vol.52 , pp. 59-64
    • Unno, T.1    Nakakuki, T.2    Fujimoto, Y.3    Okada, G.4    Kainuma, S.5    Goda, T.6
  • 27
    • 85008068324 scopus 로고
    • Fungal enzymes active in degrading gentiobiose, part I. Purification and some properties of β-glucosidase of Aspergillus japonicus SAITO
    • (in Japanese)
    • Igaue I., Kito S., Yamazaki H., Kurasawa F. Fungal enzymes active in degrading gentiobiose, part I. Purification and some properties of β-glucosidase of Aspergillus japonicus SAITO. Nihon Nougeikagakukaisi 1969, 43:224-231. (in Japanese).
    • (1969) Nihon Nougeikagakukaisi , vol.43 , pp. 224-231
    • Igaue, I.1    Kito, S.2    Yamazaki, H.3    Kurasawa, F.4


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