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Volumn 35, Issue 1, 2008, Pages 17-25

Purification and biochemical characterization of a thermostable extracellular glucoamylase produced by the thermotolerant fungus Paecilomyces variotii

Author keywords

Glucoamylase; Paecilomyces variotii; Purification; Thermostable

Indexed keywords

4 NITROPHENYL ALPHA DEXTRO MALTOSIDE; ALPHA CYCLODEXTRIN; AMINO ACID; AMYLOPECTIN; AMYLOSE; BETA CYCLODEXTRIN; DIETHYLAMINOETHYL CELLULOSE; FUNGAL ENZYME; GLUCAN 1,4 ALPHA GLUCOSIDASE; GLUCOPYRANOSIDE; GLUCOSE; GLYCOGEN; MANGANESE; METAL ION; METHYL ALPHA DEXTRO GLUCOPYRANOSIDE; OLIGOSACCHARIDE; PULLULAN; SEPHADEX; STARCH; SUCROSE; TREHALOSE; UNCLASSIFIED DRUG;

EID: 36849036808     PISSN: 13675435     EISSN: 14765535     Source Type: Journal    
DOI: 10.1007/s10295-007-0261-1     Document Type: Article
Times cited : (44)

References (40)
  • 1
    • 0040685650 scopus 로고    scopus 로고
    • Glucoamylases: Microbial sources, industrial applications and molecular biology-a review
    • James JA, Lee BH (1997) Glucoamylases: microbial sources, industrial applications and molecular biology-a review. J Food Biochem 21:1-52
    • (1997) J Food Biochem , vol.21 , pp. 1-52
    • James, J.A.1    Lee, B.H.2
  • 2
    • 0032539964 scopus 로고    scopus 로고
    • Enzymatic properties of ceysteinsulfonic acid derivative of the catalytic base mutant Glu400→Cys of glucoamylase from Aspergillus awamori
    • Fierobe HP, Clarke AJ, Tull D, Svensson B (1998) Enzymatic properties of ceysteinsulfonic acid derivative of the catalytic base mutant Glu400→Cys of glucoamylase from Aspergillus awamori. Biochemistry 37:3753-3759
    • (1998) Biochemistry , vol.37 , pp. 3753-3759
    • Fierobe, H.P.1    Clarke, A.J.2    Tull, D.3    Svensson, B.4
  • 3
    • 33646097700 scopus 로고    scopus 로고
    • Identification and characterization of glucoamylase from fungus Thermomyces lanuginosus
    • Thorsen TS, Johnsen AH, Josefsen K, Jensen B (2006) Identification and characterization of glucoamylase from fungus Thermomyces lanuginosus. Biochim Biophys Acta 1764:671-676
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 671-676
    • Thorsen, T.S.1    Johnsen, A.H.2    Josefsen, K.3    Jensen, B.4
  • 5
    • 84989071169 scopus 로고
    • Glucoamylase research and overview
    • 11
    • Pandey A (1995) Glucoamylase research and overview. Starch 47(11):439-445
    • (1995) Starch , vol.47 , pp. 439-445
    • Pandey, A.1
  • 6
    • 0000120116 scopus 로고    scopus 로고
    • Protein engineering of glucoamylase to improve industrial properties: A review
    • Reilly PJ (1999) Protein engineering of glucoamylase to improve industrial properties: a review. Starch 51:269-274
    • (1999) Starch , vol.51 , pp. 269-274
    • Reilly, P.J.1
  • 7
    • 0035051639 scopus 로고    scopus 로고
    • Purification and properties of a thermostable extracellular β-d-xylosidase produced by a thermotolerant Aspergillus phoenicis
    • Rizzatti ACS, Jorge JA, Terenzi HF, Rechia CGV, Polizeli MLTM (2001) Purification and properties of a thermostable extracellular β-d-xylosidase produced by a thermotolerant Aspergillus phoenicis. J Ind Microbiol Biotechnol 26:156-160
    • (2001) J Ind Microbiol Biotechnol , vol.26 , pp. 156-160
    • Rizzatti, A.C.S.1    Jorge, J.A.2    Terenzi, H.F.3    Rechia, C.G.V.4    Mltm, P.5
  • 8
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller GL (1959) Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal Chem 31:426-489
    • (1959) Anal Chem , vol.31 , pp. 426-489
    • Miller, G.L.1
  • 9
    • 34250511548 scopus 로고
    • The bioassay of gibberelins
    • Jones RL, Verner JE (1967) The bioassay of gibberelins. Plant 72:155-161
    • (1967) Plant , vol.72 , pp. 155-161
    • Jones, R.L.1    Verner, J.E.2
  • 11
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugars and related substances
    • Dubois M, Gilles KA, Hamilton JK, Rebers PA, Smith F (1956) Colorimetric method for determination of sugars and related substances. Anal Chem 28:350-356
    • (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
  • 12
    • 0001465376 scopus 로고
    • The effect of starch concentration upon the velocity of hydrolysis by the amylase of germinated barley
    • Hanes CS (1932) The effect of starch concentration upon the velocity of hydrolysis by the amylase of germinated barley. Biochem J 26:1406-1421
    • (1932) Biochem J , vol.26 , pp. 1406-1421
    • Hanes, C.S.1
  • 13
  • 14
    • 78651153791 scopus 로고
    • Disc electrophoresis. II. Methods and application to human serum proteins
    • Davis BJ (1964) Disc electrophoresis. II. Methods and application to human serum proteins. Ann N Y Acad Sci 121:404-427
    • (1964) Ann N Y Acad Sci , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of head of bacteriophage T4. Nature 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels
    • Blum H, Beier H, Gross HJ (1987) Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 8:93-99
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Blum, H.1    Beier, H.2    Gross, H.J.3
  • 17
    • 0035232638 scopus 로고    scopus 로고
    • Thermostable glucose-tolerant glucoamylase produced by the thermophilic fungus Scytalidium thermophilum
    • 1
    • Aquino ACMM, Jorge JA, Terenzi HF, Polizeli MLTM (2001) Thermostable glucose-tolerant glucoamylase produced by the thermophilic fungus Scytalidium thermophilum. Folia Microbiol 46(1):11-16
    • (2001) Folia Microbiol , vol.46 , pp. 11-16
    • Acmm, A.1    Jorge, J.A.2    Terenzi, H.F.3    Mltm, P.4
  • 18
    • 0017696571 scopus 로고
    • High resolution two dimensional electrophoresis of basic as well as acidic proteins
    • O'Farrel PZ, Goodman HM, O'Farrel PH (1977) High resolution two dimensional electrophoresis of basic as well as acidic proteins. Cell 12:1133-1142
    • (1977) Cell , vol.12 , pp. 1133-1142
    • O'Farrel, P.Z.1    Goodman, H.M.2    O'Farrel, P.H.3
  • 21
    • 0015158152 scopus 로고
    • Glucoenzymes: Structure and properties of the two forms of glucoamylase from Aspergillus niger
    • Pazur JH, Knull HR, Cepure A (1971) Glucoenzymes: structure and properties of the two forms of glucoamylase from Aspergillus niger. Carbohyd Res 20:83-96
    • (1971) Carbohyd Res , vol.20 , pp. 83-96
    • Pazur, J.H.1    Knull, H.R.2    Cepure, A.3
  • 22
    • 0017716340 scopus 로고
    • Three forms of α-glucosidase and glucoamylase from Aspergillus awamori
    • Yamasaki Y, Suzuki Y, Ozawa J (1977) Three forms of α-glucosidase and glucoamylase from Aspergillus awamori. Agric Biol Chem 41:2149-2161
    • (1977) Agric Biol Chem , vol.41 , pp. 2149-2161
    • Yamasaki, Y.1    Suzuki, Y.2    Ozawa, J.3
  • 23
    • 0037008421 scopus 로고    scopus 로고
    • Purification and characterisation of amylolytic enzymes from thermophilic fungus Thermomyces lanuginosus strain ATCC 34626
    • Nguyen QD, Rezessy-Szabó JM, Claeyssens M, Stals I, Hoschke A (2002) Purification and characterisation of amylolytic enzymes from thermophilic fungus Thermomyces lanuginosus strain ATCC 34626. Enzyme Microb Technol 31:345-352
    • (2002) Enzyme Microb Technol , vol.31 , pp. 345-352
    • Nguyen, Q.D.1    Rezessy-Szabó, J.M.2    Claeyssens, M.3    Stals, I.4    Hoschke, A.5
  • 24
    • 0034072923 scopus 로고    scopus 로고
    • Glucoamylase activity from the thermophilic fungus Scytalidium thermophilum. Biochemical and regulatory properties
    • 2
    • Cereia M, Terenzi HF, Jorge JA, Greene LJ, Rosa JC, Polizeli MLTM (2000) Glucoamylase activity from the thermophilic fungus Scytalidium thermophilum. Biochemical and regulatory properties. J Basic Microbiol 40(2):83-92
    • (2000) J Basic Microbiol , vol.40 , pp. 83-92
    • Cereia, M.1    Terenzi, H.F.2    Jorge, J.A.3    Greene, L.J.4    Rosa, J.C.5    Mltm, P.6
  • 25
    • 0345912536 scopus 로고    scopus 로고
    • Purification and characterization of a thermostable glucoamylase from Aspergillus fumigatus
    • Silva WB, Peralta RM (1998) Purification and characterization of a thermostable glucoamylase from Aspergillus fumigatus. Can J Microbiol 44:493-497
    • (1998) Can J Microbiol , vol.44 , pp. 493-497
    • Silva, W.B.1    Peralta, R.M.2
  • 26
    • 0034135550 scopus 로고    scopus 로고
    • Molecular basis of glucoamylases overproduction by a mutagenised industrial strain of Aspergillus niger
    • MacKenzie DA, Jeenes DJ, Xinghua G, Archer DB (2000) Molecular basis of glucoamylases overproduction by a mutagenised industrial strain of Aspergillus niger. Enz Microbial Technol 26:193-200
    • (2000) Enz Microbial Technol , vol.26 , pp. 193-200
    • MacKenzie, D.A.1    Jeenes, D.J.2    Xinghua, G.3    Archer, D.B.4
  • 27
    • 0027448702 scopus 로고
    • Purification and characterization of an extracellular glucoamylase from the thermophilic fungus Humicola grisea var. thermoidea
    • Tosi LRO, Terenzi HF, Jorge JA (1993) Purification and characterization of an extracellular glucoamylase from the thermophilic fungus Humicola grisea var. thermoidea. Can J Microbiol 39:846-852
    • (1993) Can J Microbiol , vol.39 , pp. 846-852
    • Tosi, L.R.O.1    Terenzi, H.F.2    Jorge J.A.́3
  • 28
    • 1542526994 scopus 로고
    • Characteristics of raw-starch-digesting glucoamylase from thermophilic Rhizomucor pusillus
    • Kanlayakrit W, Ishimatsu K, Nakao M, Hayashida S (1987) Characteristics of raw-starch-digesting glucoamylase from thermophilic Rhizomucor pusillus. J Ferment Technol 65:379-385
    • (1987) J Ferment Technol , vol.65 , pp. 379-385
    • Kanlayakrit, W.1    Ishimatsu, K.2    Nakao, M.3    Hayashida, S.4
  • 29
    • 0019988075 scopus 로고
    • Isolation and characterization of Schwanniomyces alluvius amylolytic enzymes
    • 2
    • Wilson JJ, Ingledew WM (1982) Isolation and characterization of Schwanniomyces alluvius amylolytic enzymes. Appl Environ Microbiol 44(2):301-307
    • (1982) Appl Environ Microbiol , vol.44 , pp. 301-307
    • Wilson, J.J.1    Ingledew, W.M.2
  • 31
    • 0038053449 scopus 로고
    • Production of amyloglucosidase by submerged culture
    • Bhumibhamon O (1983) Production of amyloglucosidase by submerged culture. Thai J Agric Sci 16:173
    • (1983) Thai J Agric Sci , vol.16 , pp. 173
    • Bhumibhamon, O.1
  • 32
    • 0020629462 scopus 로고
    • Enzyme preparation glucoamylase from culture liquid of strain Aspergillus niger B77. I. Isolation of crude enzyme preparation and study of some of its properties
    • Tsekova K, Georgieva M, Ganchev I (1983) Enzyme preparation glucoamylase from culture liquid of strain Aspergillus niger B77. I. Isolation of crude enzyme preparation and study of some of its properties. Acta Microbiol Bulgaria 13:83
    • (1983) Acta Microbiol Bulgaria , vol.13 , pp. 83
    • Tsekova, K.1    Georgieva, M.2    Ganchev, I.3
  • 33
    • 0027157228 scopus 로고
    • Production, purification and characterization of the catalytic domain of glucoamylase from Aspergillus niger
    • Stoffer B, Frandsen TP, Busk PK, Schneider P, Svendsen I, Svensson B (1993) Production, purification and characterization of the catalytic domain of glucoamylase from Aspergillus niger. Biochem J 292:197-202
    • (1993) Biochem J , vol.292 , pp. 197-202
    • Stoffer, B.1    Frandsen, T.P.2    Busk, P.K.3    Schneider, P.4    Svendsen, I.5    Svensson, B.6
  • 34
    • 0343724851 scopus 로고    scopus 로고
    • Biochemical characterization of glucoamylase from the hyperproducer exo-1 mutant strain of Neurospora crassa
    • Spinelli LBB, Polizeli MLTM, Terenzi HF, Jorge JA (1996) Biochemical characterization of glucoamylase from the hyperproducer exo-1 mutant strain of Neurospora crassa. FEMS Microbiol Lett 138:173-177
    • (1996) FEMS Microbiol Lett , vol.138 , pp. 173-177
    • Spinelli, L.B.B.1    Mltm, P.2    Terenzi, H.F.3    Jorge, J.A.4
  • 36
    • 13844298116 scopus 로고    scopus 로고
    • Purification and biochemical characterization of two xylanases produced by Aspergillus caespitosus and their potential for kraft pulp bleaching
    • Sandrim VC, Rizzatti ACS, Terenzi HF, Jorge JA, Milagres AMF, Polizeli MLTM (2005) Purification and biochemical characterization of two xylanases produced by Aspergillus caespitosus and their potential for kraft pulp bleaching. Process Biochem 40:1823-1828
    • (2005) Process Biochem , vol.40 , pp. 1823-1828
    • Sandrim, V.C.1    Rizzatti, A.C.S.2    Terenzi, H.F.3    Jorge, J.A.4    Milagres, A.M.F.5    Mltm, P.6
  • 37
    • 84987245530 scopus 로고
    • Glucoamylase produced by submerged culture of Aspergillus oryzae
    • Saha BC, Mitsue T, Ueda S (1979) Glucoamylase produced by submerged culture of Aspergillus oryzae. Starch/Särke 31:307-312
    • (1979) Starch/Särke , vol.31 , pp. 307-312
    • Saha, B.C.1    Mitsue, T.2    Ueda, S.3
  • 38
    • 0028357194 scopus 로고
    • Refined structure for the complex of acarbose with glucoamylase from Aspergillus awamori var. X100 to 2.4-A resolution
    • 22
    • Aleshin AE, Firsov LM, Honzatko RB (1994) Refined structure for the complex of acarbose with glucoamylase from Aspergillus awamori var. X100 to 2.4-A resolution. J Biol Chem 269(22):15631-15639
    • (1994) J Biol Chem , vol.269 , pp. 15631-15639
    • Aleshin, A.E.1    Firsov, L.M.2    Honzatko, R.B.3
  • 39
    • 0036422274 scopus 로고    scopus 로고
    • Cloning, heterologous expression, and enzymatic characterization of a thermostable glucoamylase from Talaromyces emersonii
    • Nielsen BR, Lehmbeck J, Frandsen TP (2002) Cloning, heterologous expression, and enzymatic characterization of a thermostable glucoamylase from Talaromyces emersonii. Protein Expr Purif 26:1-8
    • (2002) Protein Expr Purif , vol.26 , pp. 1-8
    • Nielsen, B.R.1    Lehmbeck, J.2    Frandsen, T.P.3
  • 40
    • 0030729996 scopus 로고    scopus 로고
    • Glucoamylase structural, functional, and evolutionary relationships
    • Coutinho PM, Reilly PJ (1997) Glucoamylase structural, functional, and evolutionary relationships. Proteins Struct Funct Gen 29:334-347
    • (1997) Proteins Struct Funct Gen , vol.29 , pp. 334-347
    • Coutinho, P.M.1    Reilly, P.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.