메뉴 건너뛰기




Volumn 96, Issue 4, 2009, Pages 569-578

Purification and biochemical characterization of a novel α-glucosidase from Aspergillus niveus

Author keywords

Glucosidase; Aspergillus niveus; Fungus; Purification; Thermostability

Indexed keywords

4 NITROPHENYL ALPHA DEXTRO GLUCOPYRANOSIDE; ALPHA CYCLODEXTRIN; ALPHA GLUCOSIDASE; AMYLOPECTIN; AMYLOSE; BETA CYCLODEXTRIN; GLUCOSE; GLYCOGEN; ISOMALTOSE; MALTOPENTAOSE; MALTOSE; MALTOSE OLIGOSACCHARIDE; MALTOTETROSE; MALTOTRIOSE; OLIGOSACCHARIDE; POLYSACCHARIDE; STARCH; SUCROSE; TREHALOSE; UNCLASSIFIED DRUG;

EID: 72649105849     PISSN: 00036072     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10482-009-9372-1     Document Type: Article
Times cited : (21)

References (27)
  • 1
    • 0027190754 scopus 로고
    • Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network
    • 10.1093/protein/6.4.383 1:CAS:528:DyaK3sXkvFSmsbg%3D 8332596
    • MA Andrade P Chacon JJ Merelo F Moran 1993 Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network Protein Eng 6 383 390 10.1093/protein/6.4.383 1:CAS:528:DyaK3sXkvFSmsbg%3D 8332596
    • (1993) Protein Eng , vol.6 , pp. 383-390
    • Andrade, M.A.1    Chacon, P.2    Merelo, J.J.3    Moran, F.4
  • 2
    • 44349103174 scopus 로고    scopus 로고
    • Three-dimensional structure of an intact glycoside hydrolase family 15 glucoamylase from Hypocrea jecorina
    • DOI 10.1021/bi702413k
    • R Bott M Saldajeno W Cuevas D Ward M Scheffers W Aehle S Karkehabadi M Sandgren H Hansson 2008 Three-dimensional structure of an intact glycoside hydrolase family 15 glucoamylase from Hypocrea jecorina Biochemistry 47 5746 5754 10.1021/bi702413k 1:CAS:528:DC%2BD1cXlsVKlsrY%3D 18457422 (Pubitemid 351747053)
    • (2008) Biochemistry , vol.47 , Issue.21 , pp. 5746-5754
    • Bott, R.1    Saldajeno, M.2    Cuevas, W.3    Ward, D.4    Scheffers, M.5    Aehle, W.6    Karkehabadi, S.7    Sandgren, M.8    Hansson, H.9
  • 3
    • 0034072923 scopus 로고    scopus 로고
    • Glucoamylase activity from the thermophilic fungus Scytalidium thermophilum. Biochemical and regulatory properties
    • DOI 10.1002/(SICI)1521-4028(200005)40:2<83::AID-JOBM83>3.0.CO;2-6
    • M Cereia HF Terenzi JA Jorge LJ Greene JC Rosa MLTM Polizeli 2000 Glucoamylase activity from the thermophilic fungus Scytalidium thermophilum. Biochemical and regulatory properties J Basic Microbiol 40 2 83 92 10.1002/(SICI)1521-4028(200005)40:2<83::AID-JOBM83>3.0.CO;2-6 1:CAS:528:DC%2BD3cXjvVCitLk%3D (Pubitemid 30334273)
    • (2000) Journal of Basic Microbiology , vol.40 , Issue.2 , pp. 83-92
    • Cereia, M.1    Terenzi, H.F.2    Jorge, J.A.3    Greene, L.J.4    Rosa, J.C.5    Polizeli, M.D.L.T.M.6
  • 4
    • 78651153791 scopus 로고
    • Disc electrophoresis. II. Methods and application to human serum proteins
    • 10.1111/j.1749-6632.1964.tb14213.x 1:CAS:528:DyaF2MXltlKltw%3D%3D 14240539
    • BJ Davis 1964 Disc electrophoresis. II. Methods and application to human serum proteins Ann NY Acad Sci 121 404 427 10.1111/j.1749-6632.1964.tb14213.x 1:CAS:528:DyaF2MXltlKltw%3D%3D 14240539
    • (1964) Ann NY Acad Sci , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 5
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugars and related substances
    • 10.1021/ac60111a017 1:CAS:528:DyaG28XjvFynsg%3D%3D
    • M Dubois KA Gilles JK Hamilton PA Rebers F Smith 1956 Colorimetric method for determination of sugars and related substances Anal Chem 28 350 356 10.1021/ac60111a017 1:CAS:528:DyaG28XjvFynsg%3D%3D
    • (1956) Anal Chem , vol.28 , pp. 350-356
    • Dubois, M.1    Gilles, K.A.2    Hamilton, J.K.3    Rebers, P.A.4    Smith, F.5
  • 6
    • 0000137653 scopus 로고
    • α-4-O-methyl-d-glucuronidase component of xylanolytic complexes
    • 10.1016/0076-6879(88)60169-8 1:CAS:528:DyaL1MXhs1yktb8%3D
    • JD Fontana M Gebara M Blumel H Schneider CR Mackenzie KG Johnson 1988 α-4-O-methyl-d-glucuronidase component of xylanolytic complexes Methods Enzymol 160 560 571 10.1016/0076-6879(88)60169-8 1:CAS:528:DyaL1MXhs1yktb8%3D
    • (1988) Methods Enzymol , vol.160 , pp. 560-571
    • Fontana, J.D.1    Gebara, M.2    Blumel, M.3    Schneider, H.4    MacKenzie, C.R.5    Johnson, K.G.6
  • 7
    • 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
    • DOI 10.1023/A:1005925819741
    • TP Frandsen B Svensson 1998 Plant α-glucosidase of the glycoside hydrolase family 31. Molecular properties, substrate specificity, reaction mechanism, and comparison with family members of different origin Plant Mol Biol 27 1 13 10.1023/A:1005925819741 (Pubitemid 28219665)
    • (1998) Plant Molecular Biology , vol.37 , Issue.1 , pp. 1-13
    • Frandsen, T.P.1    Svensson, B.2
  • 8
    • 33646776730 scopus 로고    scopus 로고
    • A novel α-glucosidase from Chaetomium thermophilum var. coprophilum that converts maltose into trehalose: Purification and partial characterisation of the enzyme
    • DOI 10.1016/j.procbio.2006.03.017, PII S1359511306001152
    • GC Giannesi MLTM Polizeli HF Terenzi JA Jorge 2006 A novel α-glucosidase from Chaetomium thermophilum var. coprophilum that converts maltose into trehalose: purification and partial characterization of the enzyme Process Biochem 41 1729 1735 10.1016/j.procbio.2006.03.017 1:CAS:528: DC%2BD28XltFCksb0%3D (Pubitemid 43767158)
    • (2006) Process Biochemistry , vol.41 , Issue.8 , pp. 1729-1735
    • Giannesi, G.C.1    De Lourdes Teixeira De Moraes Polizeli, M.2    Terenzi, H.F.3    Jorge, J.A.4
  • 9
    • 0001465376 scopus 로고
    • The effect of starch concentration upon the velocity of hydrolysis by the amylase of germinated barley
    • 1:CAS:528:DyaA3sXnt1er 16744959
    • CS Hanes 1932 The effect of starch concentration upon the velocity of hydrolysis by the amylase of germinated barley Biochem J 26 1406 1421 1:CAS:528:DyaA3sXnt1er 16744959
    • (1932) Biochem J , vol.26 , pp. 1406-1421
    • Hanes, C.S.1
  • 10
    • 0036196070 scopus 로고    scopus 로고
    • Novel α-glucosidase from Aspergillus nidulans with strong transglycosylation activity
    • DOI 10.1128/AEM.68.3.1250-1256.2002
    • N Kato S Suyama M Shirokane M Kato T Kobayashi N Tsukagoshi 2002 Novel α-glucosidase from Aspergillus nidulans with strong transglycosylation activity Appl Environ Microbiol 68 1250 1256 10.1128/AEM.68.3.1250-1256.2002 1:CAS:528:DC%2BD38XitFSjsrc%3D 11872475 (Pubitemid 34205364)
    • (2002) Applied and Environmental Microbiology , vol.68 , Issue.3 , pp. 1250-1256
    • Kato, N.1    Suyama, S.2    Shirokane, M.3    Kato, M.4    Kobayashi, T.5    Tsukagoshi, N.6
  • 11
    • 0029141322 scopus 로고
    • Production, isolation and partial purification of xylanase from Aspergillus sp
    • 10.1007/BF00704661 1:CAS:528:DyaK2MXmtFyhu78%3D
    • P Khanna SS Sundari NJ Kumar 1995 Production, isolation and partial purification of xylanase from Aspergillus sp World J Microbiol Biotechnol 11 242 243 10.1007/BF00704661 1:CAS:528:DyaK2MXmtFyhu78%3D
    • (1995) World J Microbiol Biotechnol , vol.11 , pp. 242-243
    • Khanna, P.1    Sundari, S.S.2    Kumar, N.J.3
  • 12
    • 0042352394 scopus 로고    scopus 로고
    • Purification and characterization of a new type of α-glucosidase from Paecilomyces lilacinus that has transglucosylation activity to produce α-1,3- and α-1,2-linked oligosaccharides
    • 10.1271/bbb.67.29 1:CAS:528:DC%2BD3sXhtVWqtrY%3D 12619670
    • I Kobayashi M Tokuda H Hashimoto T Konda H Nakano S Kitahata 2003 Purification and characterization of a new type of α-glucosidase from Paecilomyces lilacinus that has transglucosylation activity to produce α-1,3- and α-1,2-linked oligosaccharides Biosci Biotechnol Biochem 67 29 35 10.1271/bbb.67.29 1:CAS:528:DC%2BD3sXhtVWqtrY%3D 12619670
    • (2003) Biosci Biotechnol Biochem , vol.67 , pp. 29-35
    • Kobayashi, I.1    Tokuda, M.2    Hashimoto, H.3    Konda, T.4    Nakano, H.5    Kitahata, S.6
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of head of bacteriophage T4
    • 10.1038/227680a0 1:CAS:528:DC%2BD3MXlsFags7s%3D 5432063
    • UK Laemmli 1970 Cleavage of structural proteins during the assembly of head of bacteriophage T4 Nature 227 680 685 10.1038/227680a0 1:CAS:528:DC%2BD3MXlsFags7s%3D 5432063
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0034135550 scopus 로고    scopus 로고
    • Molecular basis of glucoamylases overproduction by a mutagenised industrial strain of Aspergillus niger
    • 10.1016/S0141-0229(99)00145-3 1:CAS:528:DC%2BD3cXht1Ohsbw%3D 10689077
    • DA MacKenzie DJ Jeenes X Gou DB Archer 2000 Molecular basis of glucoamylases overproduction by a mutagenised industrial strain of Aspergillus niger Enzyme Microb Technol 26 193 200 10.1016/S0141-0229(99)00145-3 1:CAS:528:DC%2BD3cXht1Ohsbw%3D 10689077
    • (2000) Enzyme Microb Technol , vol.26 , pp. 193-200
    • MacKenzie, D.A.1    Jeenes, D.J.2    Gou, X.3    Archer, D.B.4
  • 16
    • 33644964484 scopus 로고    scopus 로고
    • Purification and biochemical characterization of an α-glucosidase from Xanthophyllomyces dendrorhus
    • 10.1002/yea.1345 16491468
    • D Marín D Linde MF Lobato 2006 Purification and biochemical characterization of an α-glucosidase from Xanthophyllomyces dendrorhus Yeast 23 117 125 10.1002/yea.1345 16491468
    • (2006) Yeast , vol.23 , pp. 117-125
    • Marín, D.1    Linde, D.2    Lobato, M.F.3
  • 18
    • 36849036808 scopus 로고    scopus 로고
    • Purification and biochemical characterization of a thermostable extracellular glucoamylase produced by the thermotolerant fungus Paecilomyces variotii
    • DOI 10.1007/s10295-007-0261-1
    • M Michelin R Ruller RJ Ward LAB Moraes JA Jorge HF Terenzi MLTM Polizeli 2008 Purification and biochemical characterization of a thermostable extracellular glucoamylase produced by the thermotolerant fungus Paecilomyces variotii J Ind Microbiol Biotechnol 35 17 25 10.1007/s10295-007-0261-1 1:CAS:528:DC%2BD2sXhsVSmurfI 17938981 (Pubitemid 350234126)
    • (2008) Journal of Industrial Microbiology and Biotechnology , vol.35 , Issue.1 , pp. 17-25
    • Michelin, M.1    Ruller, R.2    Ward, R.J.3    Moraes, L.A.B.4    Jorge, J.A.5    Terenzi, H.F.6    Polizeli, M.D.L.T.M.7
  • 19
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • 10.1021/ac60147a030 1:CAS:528:DyaG1MXmtFKiuw%3D%3D
    • GL Miller 1959 Use of dinitrosalicylic acid reagent for determination of reducing sugar Anal Chem 31 426 489 10.1021/ac60147a030 1:CAS:528: DyaG1MXmtFKiuw%3D%3D
    • (1959) Anal Chem , vol.31 , pp. 426-489
    • Miller, G.L.1
  • 20
    • 0001642923 scopus 로고
    • Existence of a novel enzyme converting maltose into trehalose
    • 10.1271/bbb.59.2189 1:CAS:528:DyaK2MXpslyht7s%3D
    • T Nishimoto M Nakano S Ikegami H Chaen S Fukuda T Sugimoto 1995 Existence of a novel enzyme converting maltose into trehalose Biosci Biotechnol Biochem 59 2189 2190 10.1271/bbb.59.2189 1:CAS:528:DyaK2MXpslyht7s%3D
    • (1995) Biosci Biotechnol Biochem , vol.59 , pp. 2189-2190
    • Nishimoto, T.1    Nakano, M.2    Ikegami, S.3    Chaen, H.4    Fukuda, S.5    Sugimoto, T.6
  • 21
    • 0017696571 scopus 로고
    • High resolution two dimensional electrophoresis of basic as well as acidic proteins
    • 10.1016/0092-8674(77)90176-3
    • PZ O'Farrel HM Goodman PH O'Farrel 1977 High resolution two dimensional electrophoresis of basic as well as acidic proteins Cell 12 1133 1142 10.1016/0092-8674(77)90176-3
    • (1977) Cell , vol.12 , pp. 1133-1142
    • O'Farrel, P.Z.1    Goodman, H.M.2    O'Farrel, P.H.3
  • 22
    • 4544240287 scopus 로고
    • Purification and substrate specificity of a α-glucosidase from Paecilomyces variotii AHU
    • 10.1271/bbb.56.1906 1:CAS:528:DyaK3sXps1ygsg%3D%3D
    • T Oguma H Matsui M Tanida S Takao M Honma S Chiba 1992 Purification and substrate specificity of a α-glucosidase from Paecilomyces variotii AHU Biosci Biotechnol Biochem 56 1906 1910 10.1271/bbb.56.1906 1:CAS:528: DyaK3sXps1ygsg%3D%3D
    • (1992) Biosci Biotechnol Biochem , vol.56 , pp. 1906-1910
    • Oguma, T.1    Matsui, H.2    Tanida, M.3    Takao, S.4    Honma, M.5    Chiba, S.6
  • 23
    • 23744447380 scopus 로고    scopus 로고
    • Purification and characterization of the hyper-glycosylated extracellular α-glucosidase from Schizosaccharomyces pombe
    • DOI 10.1016/j.enzmictec.2004.06.018, PII S0141022905001286
    • M Okuyama Y Tanimoto T Ito A Anzai H Mori A Kimura 2005 Purification and characterization of the hyper-glycosylated extracellular α-glucosidase from Schizosaccharomyces pombe Enzyme Microb Technol 37 472 480 10.1016/j.enzmictec.2004.06.018 1:CAS:528:DC%2BD2MXns1Wgs7w%3D (Pubitemid 41138177)
    • (2005) Enzyme and Microbial Technology , vol.37 , Issue.5 , pp. 472-480
    • Okuyama, M.1    Tanimoto, Y.2    Ito, T.3    Anzai, A.4    Mori, H.5    Kimura, A.6    Matsui, H.7    Chiba, S.8
  • 24
    • 0006703688 scopus 로고    scopus 로고
    • Advances in microbial amylases. Review
    • 10.1042/BA19990073 1:CAS:528:DC%2BD3cXislWitr4%3D 10744959
    • A Pandey P Nigam CR Soccol VT Soccol DRM Singh 2000 Advances in microbial amylases. Review Biotechnol Appl Biochem 31 135 152 10.1042/BA19990073 1:CAS:528:DC%2BD3cXislWitr4%3D 10744959
    • (2000) Biotechnol Appl Biochem , vol.31 , pp. 135-152
    • Pandey, A.1    Nigam, P.2    Soccol, C.R.3    Soccol, V.T.4    Singh, D.R.M.5
  • 25
    • 0042075003 scopus 로고    scopus 로고
    • Purification and characterization of a novel fungal α-glucosidase from Mortirella alliacea with high starch-hydrolytic activity
    • 10.1271/bbb.66.2415 1:CAS:528:DC%2BD38XpsVOitro%3D 12506981
    • Y Tanaka T Aki Y Hidaka Y Furuya S Kawamoto S Shigeta K Ono O Suzuki 2002 Purification and characterization of a novel fungal α-glucosidase from Mortirella alliacea with high starch-hydrolytic activity Biosci Biotechnol Biochem 66 2415 2423 10.1271/bbb.66.2415 1:CAS:528:DC%2BD38XpsVOitro%3D 12506981
    • (2002) Biosci Biotechnol Biochem , vol.66 , pp. 2415-2423
    • Tanaka, Y.1    Aki, T.2    Hidaka, Y.3    Furuya, Y.4    Kawamoto, S.5    Shigeta, S.6    Ono, K.7    Suzuki, O.8
  • 26
    • 3242716846 scopus 로고    scopus 로고
    • Purification and characterization of Acremonium implicatum α-glucosidase having regioselectivity for α-1,3-glucosidic linkage
    • 1:CAS:528:DC%2BD2cXlvVWgsLw%3D 15262228
    • T Yamamoto T Unno Y Watanabe M Yamamoto M Okuyama H Mori S Chiba A Kimura 2004 Purification and characterization of Acremonium implicatum α-glucosidase having regioselectivity for α-1,3-glucosidic linkage Biochim Biophys Acta 1700 2 189 198 1:CAS:528:DC%2BD2cXlvVWgsLw%3D 15262228
    • (2004) Biochim Biophys Acta , vol.1700 , Issue.2 , pp. 189-198
    • Yamamoto, T.1    Unno, T.2    Watanabe, Y.3    Yamamoto, M.4    Okuyama, M.5    Mori, H.6    Chiba, S.7    Kimura, A.8
  • 27
    • 0015802212 scopus 로고
    • Properties of crystalline α-glucosidase from Mucor javanicus
    • 1:CAS:528:DyaE3sXktFCrtrY%3D
    • Y Yamasaki T Miyake Y Suzuki 1973 Properties of crystalline α-glucosidase from Mucor javanicus Agric Biol Chem 37 251 259 1:CAS:528:DyaE3sXktFCrtrY%3D
    • (1973) Agric Biol Chem , vol.37 , pp. 251-259
    • Yamasaki, Y.1    Miyake, T.2    Suzuki, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.