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Volumn 45, Issue 7, 2010, Pages 1088-1093

Purification and characterization of a thermostable α-galactosidase with transglycosylation activity from Aspergillus parasiticus MTCC-2796

Author keywords

Galactosidase; Aspergillus parasiticus; Characterization; Purification; Thermostable; Transglycosylation

Indexed keywords

2-MERCAPTOETHANOL; ASPERGILLUS PARASITICUS; ENZYMATIC ACTIVITIES; ETHYLENEDIAMINETETRAACETIC ACID; EXTRACELLULAR; GALACTOPYRANOSIDE; GALACTOSIDASES; MONOMERIC PROTEINS; OPTIMUM ACTIVITY; PURIFIED ENZYME; SEPHADEX; SODIUM DODECYL SULFATE-POLYACRYLAMIDE GEL ELECTROPHORESIS; SUBSTRATE SPECIFICITY; TRANS GLYCOSYLATION ACTIVITY; TRANSGLYCOSYLATION; TRANSGLYCOSYLATION REACTION;

EID: 77954815400     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2010.03.027     Document Type: Article
Times cited : (22)

References (39)
  • 1
    • 0015269593 scopus 로고
    • Biochemistry of α-galactosidases
    • Dey P.M., Pridham J.B. Biochemistry of α-galactosidases. Adv Enzymol 1972, 36:91.
    • (1972) Adv Enzymol , vol.36 , pp. 91
    • Dey, P.M.1    Pridham, J.B.2
  • 2
    • 0029617445 scopus 로고
    • Properties of an extracellular glycosidase of Aspergillus niger suitable for removal of oligo-saccharides from cow pea meal
    • Somiari R.I., Balogh E. Properties of an extracellular glycosidase of Aspergillus niger suitable for removal of oligo-saccharides from cow pea meal. Enzyme Microb Technol 1995, 17:311-316.
    • (1995) Enzyme Microb Technol , vol.17 , pp. 311-316
    • Somiari, R.I.1    Balogh, E.2
  • 3
    • 0032033488 scopus 로고    scopus 로고
    • Production of α-galactosidase by thermophilic fungus Humicola sp. in solid-state fermentation and its application in soya milk hydrolysis
    • Kotwal S.M., Gote M.M., Sainkar S.R., Khan M.I., Khire J.M. Production of α-galactosidase by thermophilic fungus Humicola sp. in solid-state fermentation and its application in soya milk hydrolysis. Process Biochem 1998, 33:337-343.
    • (1998) Process Biochem , vol.33 , pp. 337-343
    • Kotwal, S.M.1    Gote, M.M.2    Sainkar, S.R.3    Khan, M.I.4    Khire, J.M.5
  • 4
    • 0000634771 scopus 로고
    • Immobilization of thermostable α-galactosidase from Pycnoporus cinnabarinus on chitosan beads and its application to the hydrolysis of raffinose in beet sugar molasses
    • Ohtakara M., Mitsutomi Immobilization of thermostable α-galactosidase from Pycnoporus cinnabarinus on chitosan beads and its application to the hydrolysis of raffinose in beet sugar molasses. J Ferment Technol 1987, 65:493-498.
    • (1987) J Ferment Technol , vol.65 , pp. 493-498
    • Ohtakara, M.1    Mitsutomi2
  • 5
    • 0024094905 scopus 로고
    • Production of thermostable recombinant α-galactosidase suitable for raffinose elimination from sugar beet syrup
    • Ganter C., Bock A., Buckel P., Mattes R. Production of thermostable recombinant α-galactosidase suitable for raffinose elimination from sugar beet syrup. J Biotechnol 1988, 8:301-310.
    • (1988) J Biotechnol , vol.8 , pp. 301-310
    • Ganter, C.1    Bock, A.2    Buckel, P.3    Mattes, R.4
  • 6
    • 0025208660 scopus 로고
    • Development of a biotechnological process for the modification of galactomannan polymers with plant α-galactosidase
    • Bulpin P.V., Gidley M.J., Jeffcoat R., Underwood D.R. Development of a biotechnological process for the modification of galactomannan polymers with plant α-galactosidase. Carbohydr Polym 1990, 12:155-168.
    • (1990) Carbohydr Polym , vol.12 , pp. 155-168
    • Bulpin, P.V.1    Gidley, M.J.2    Jeffcoat, R.3    Underwood, D.R.4
  • 8
    • 0020041868 scopus 로고
    • Group B erythrocytes enzymatically converted to group O survives normal in AB and O individuals
    • Goldstein J., Siviglia G., Hurst R. Group B erythrocytes enzymatically converted to group O survives normal in AB and O individuals. Science 1982, 215:168-170.
    • (1982) Science , vol.215 , pp. 168-170
    • Goldstein, J.1    Siviglia, G.2    Hurst, R.3
  • 9
    • 34447607076 scopus 로고
    • Ein Beitrag Zur Kenntnis der Purpura haemorrhagica nodularis (Purpura papulosa hemorrhagica Hebrae)
    • Fabry J. Ein Beitrag Zur Kenntnis der Purpura haemorrhagica nodularis (Purpura papulosa hemorrhagica Hebrae). Arch Dermatol Syphilol 1898, 43:187-200.
    • (1898) Arch Dermatol Syphilol , vol.43 , pp. 187-200
    • Fabry, J.1
  • 10
    • 0042833200 scopus 로고    scopus 로고
    • Enzyme replacement therapy in Fabry disease: clinical implication
    • Breunig F., Knoll A., Wanner C. Enzyme replacement therapy in Fabry disease: clinical implication. Curr Opin Nephrol Hypertens 2003, 12:491-495.
    • (2003) Curr Opin Nephrol Hypertens , vol.12 , pp. 491-495
    • Breunig, F.1    Knoll, A.2    Wanner, C.3
  • 11
    • 33745746213 scopus 로고    scopus 로고
    • Glycosyl hydrolases and glycosyltransferases in the synthesis of oligosaccharides
    • Trincone A., Giordano A. Glycosyl hydrolases and glycosyltransferases in the synthesis of oligosaccharides. Curr Org Chem 2006, 10:1163-1193.
    • (2006) Curr Org Chem , vol.10 , pp. 1163-1193
    • Trincone, A.1    Giordano, A.2
  • 12
    • 84961782599 scopus 로고
    • Oligosaccharide formation during enzymatic lactose hydrolysis: a literature review
    • Zarate S., Lopex-Leiva M.H. Oligosaccharide formation during enzymatic lactose hydrolysis: a literature review. J Food Protect 1990, 53:262-268.
    • (1990) J Food Protect , vol.53 , pp. 262-268
    • Zarate, S.1    Lopex-Leiva, M.H.2
  • 13
    • 0001448532 scopus 로고
    • Purification and enzymatic properties of α-galactosidase from Pycnoporus cinnabarinus
    • Ohtakara M., Mitsutomi M., Uchida Y. Purification and enzymatic properties of α-galactosidase from Pycnoporus cinnabarinus. Agr Bio Chem 1984, 48:1319-1327.
    • (1984) Agr Bio Chem , vol.48 , pp. 1319-1327
    • Ohtakara, M.1    Mitsutomi, M.2    Uchida, Y.3
  • 14
    • 0023005968 scopus 로고
    • Production, purification and characterization of α-galactosidase from Monascus pilosus
    • Wong H., Hu C., Yeh H., Su W., Lu H., Lin C. Production, purification and characterization of α-galactosidase from Monascus pilosus. Appl Environ Microbiol 1986, 52:1147-1152.
    • (1986) Appl Environ Microbiol , vol.52 , pp. 1147-1152
    • Wong, H.1    Hu, C.2    Yeh, H.3    Su, W.4    Lu, H.5    Lin, C.6
  • 15
    • 0000049352 scopus 로고
    • Purification and some properties of α-galactosidase from Candida guilliermondii H-404
    • Hashimoto H., Katayama C., Goto M., Kitahata S. Purification and some properties of α-galactosidase from Candida guilliermondii H-404. Biosci Biotechnol Biochem 1993, 57:372-378.
    • (1993) Biosci Biotechnol Biochem , vol.57 , pp. 372-378
    • Hashimoto, H.1    Katayama, C.2    Goto, M.3    Kitahata, S.4
  • 16
    • 0345482589 scopus 로고    scopus 로고
    • Purification and some properties of α-galactosidase from Mortierella vinacea IBT-3
    • Galas E., Miszkiewicz H. Purification and some properties of α-galactosidase from Mortierella vinacea IBT-3. Acta Microbiologica Polonica 1996, 45:143-154.
    • (1996) Acta Microbiologica Polonica , vol.45 , pp. 143-154
    • Galas, E.1    Miszkiewicz, H.2
  • 17
    • 27944510722 scopus 로고    scopus 로고
    • Purification and characterization of an α-galactosidase from Aspergillus fumigatus
    • Rezende S.T., Guimarǎes V.M., Rodrigues M.C., Felix C.R. Purification and characterization of an α-galactosidase from Aspergillus fumigatus. Braz Arch Biol Technol 2005, 48:195-202.
    • (2005) Braz Arch Biol Technol , vol.48 , pp. 195-202
    • Rezende, S.T.1    Guimarǎes, V.M.2    Rodrigues, M.C.3    Felix, C.R.4
  • 19
    • 0034669843 scopus 로고    scopus 로고
    • Purification and characterization of α-galactosidase from a thermophilic fungus Thermomyces lanuginosus
    • Puchart V., Vrsanska M., Bhat M.K., Biely P. Purification and characterization of α-galactosidase from a thermophilic fungus Thermomyces lanuginosus. Biochim Biophys Acta 2000, 1524:27-37.
    • (2000) Biochim Biophys Acta , vol.1524 , pp. 27-37
    • Puchart, V.1    Vrsanska, M.2    Bhat, M.K.3    Biely, P.4
  • 21
    • 2342598391 scopus 로고    scopus 로고
    • Temperature effect on the biological activity of Bifidobacterium longum CRL 849 and Lactobacillus fermentum CRL 251 in pure and mixed cultures grown in soymilk
    • Garro M.S., Valdez G.F., Giorigs Temperature effect on the biological activity of Bifidobacterium longum CRL 849 and Lactobacillus fermentum CRL 251 in pure and mixed cultures grown in soymilk. Food Microbiol 2004, 21:511-518.
    • (2004) Food Microbiol , vol.21 , pp. 511-518
    • Garro, M.S.1    Valdez, G.F.2    Giorigs3
  • 22
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller G.L. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal Chem 1956, 31:426-428.
    • (1956) Anal Chem , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 25
    • 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
  • 27
    • 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
  • 28
    • 0040068057 scopus 로고
    • A spectrophotometric study of the behavior of carbohydrates in seventy-nine per cent sulfuric acid
    • Ikawa M., Niemann C. A spectrophotometric study of the behavior of carbohydrates in seventy-nine per cent sulfuric acid. J Biol Chem 1949, 180:923-931.
    • (1949) J Biol Chem , vol.180 , pp. 923-931
    • Ikawa, M.1    Niemann, C.2
  • 29
    • 0017578718 scopus 로고
    • Glycoprotein enzymes secreted by Aspergillus niger: purification and properties of α-galactosidase
    • Adya S., Elbein A.D. Glycoprotein enzymes secreted by Aspergillus niger: purification and properties of α-galactosidase. J Bacteriol 1977, 129:850-856.
    • (1977) J Bacteriol , vol.129 , pp. 850-856
    • Adya, S.1    Elbein, A.D.2
  • 30
    • 0021426952 scopus 로고
    • Glycosidases induced in Aspergillus tamarii (mycelial α-d-galactosidases)
    • Civas A., Eberhard R., Dizet P.L., Petek F. Glycosidases induced in Aspergillus tamarii (mycelial α-d-galactosidases). Biochem J 1984, 219:849-855.
    • (1984) Biochem J , vol.219 , pp. 849-855
    • Civas, A.1    Eberhard, R.2    Dizet, P.L.3    Petek, F.4
  • 31
    • 34548456824 scopus 로고    scopus 로고
    • Purification and characterization of a novel protease-resistant α-galactosidase from Rhizopus sp. ACCC 30795
    • Cao Y., Yang P., Shi P., Wang Y., Luo H., Meng K., et al. Purification and characterization of a novel protease-resistant α-galactosidase from Rhizopus sp. ACCC 30795. Enz Microb Technol 2007, 41:835-841.
    • (2007) Enz Microb Technol , vol.41 , pp. 835-841
    • Cao, Y.1    Yang, P.2    Shi, P.3    Wang, Y.4    Luo, H.5    Meng, K.6
  • 33
    • 0031023550 scopus 로고    scopus 로고
    • Purification and characterization of extremely thermostable β-mannanase, β-mannosidase, and α-galactosidase from the hyperthermophilic eubacterium T. neapolitana 5068
    • Duffaud G.D., McCutchen C.M., Leduc P., Parker K.N., Kelly R.M. Purification and characterization of extremely thermostable β-mannanase, β-mannosidase, and α-galactosidase from the hyperthermophilic eubacterium T. neapolitana 5068. Appl Environ Microbiol 1997, 63:169-177.
    • (1997) Appl Environ Microbiol , vol.63 , pp. 169-177
    • Duffaud, G.D.1    McCutchen, C.M.2    Leduc, P.3    Parker, K.N.4    Kelly, R.M.5
  • 34
    • 0034051323 scopus 로고    scopus 로고
    • High yield production and characterization of α-galactosidase from Bifidobacterium breve grown on raffinose
    • Xiao M., Tanaka K., Qian X.M., Yamamoto K., Kumagai H. High yield production and characterization of α-galactosidase from Bifidobacterium breve grown on raffinose. Biotechnol Lett 2000, 22:747-751.
    • (2000) Biotechnol Lett , vol.22 , pp. 747-751
    • Xiao, M.1    Tanaka, K.2    Qian, X.M.3    Yamamoto, K.4    Kumagai, H.5
  • 35
    • 0028979685 scopus 로고
    • Production of thermostable α-galactosidase from thermophilic fungus Humicola sp
    • Kotwal S.M., Khan M.I., Khire J.M. Production of thermostable α-galactosidase from thermophilic fungus Humicola sp. J Ind Microbiol Biotechnol 1995, 15:116-120.
    • (1995) J Ind Microbiol Biotechnol , vol.15 , pp. 116-120
    • Kotwal, S.M.1    Khan, M.I.2    Khire, J.M.3
  • 36
    • 0035314051 scopus 로고    scopus 로고
    • Penicillium sp. 23 α-galactosidase: purification and substrate specificity
    • Varbanets D.L., Malanchuk V.M., Buglova T.T., Kuhlmann R.A. Penicillium sp. 23 α-galactosidase: purification and substrate specificity. Carbohydr Polym 2001, 44:357-363.
    • (2001) Carbohydr Polym , vol.44 , pp. 357-363
    • Varbanets, D.L.1    Malanchuk, V.M.2    Buglova, T.T.3    Kuhlmann, R.A.4
  • 37
    • 0026060417 scopus 로고
    • Substrate specificity of α-galactosidase from Aspergillus niger 5-16
    • Kaneko R., Kusakabe I., Ida E., Murakami K. Substrate specificity of α-galactosidase from Aspergillus niger 5-16. Agric Biol Chem 1991, 55:109-115.
    • (1991) Agric Biol Chem , vol.55 , pp. 109-115
    • Kaneko, R.1    Kusakabe, I.2    Ida, E.3    Murakami, K.4
  • 38
    • 0002204599 scopus 로고
    • Transgalactosylation activity of sweet almond α-galactosidase: synthesis of saccharides
    • Dey P.M. Transgalactosylation activity of sweet almond α-galactosidase: synthesis of saccharides. Phytochemistry 1979, 18:35.
    • (1979) Phytochemistry , vol.18 , pp. 35
    • Dey, P.M.1
  • 39
    • 0001618467 scopus 로고
    • The formation of oligosaccharides by enzymic transglycosylation
    • Edelman J. The formation of oligosaccharides by enzymic transglycosylation. Adv Enzymol 1956, 17:189-232.
    • (1956) Adv Enzymol , vol.17 , pp. 189-232
    • Edelman, J.1


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