메뉴 건너뛰기




Volumn 39, Issue 4, 2006, Pages 596-600

Catalytic characterization of phytase (myo-inositolhexakisphosphate phosphohydrolase) from Aspergillus niger van Teighem: Glycosylation pattern, kinetics and molecular properties

Author keywords

Acid phosphatases; Aspergillus niger; Catalytic properties; Inositolhexaphosphate phosphohydrolases; Myo inositolhexasulphate; Phytases

Indexed keywords

CATALYST ACTIVITY; ELECTROPHORESIS; ENZYME KINETICS; FUNGI; GELS; PROTEINS;

EID: 33745476036     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2005.11.009     Document Type: Article
Times cited : (21)

References (42)
  • 1
    • 0031034203 scopus 로고    scopus 로고
    • The phytase subfamily of histidine acid phosphatase: isolation of genes for two novel phytases from fungi Aspergillus terreus and Myceliophthora thermophila
    • Mitchell D.B., Vogel K., Weimann B.J., Pasamontes L., and van Loon A.P.G.M. The phytase subfamily of histidine acid phosphatase: isolation of genes for two novel phytases from fungi Aspergillus terreus and Myceliophthora thermophila. Microbiology 143 (1997) 245-252
    • (1997) Microbiology , vol.143 , pp. 245-252
    • Mitchell, D.B.1    Vogel, K.2    Weimann, B.J.3    Pasamontes, L.4    van Loon, A.P.G.M.5
  • 2
    • 0030592120 scopus 로고    scopus 로고
    • Construction of a bioreactor to produce special breakdown products of phytate
    • Greiner R., and Konietzny U. Construction of a bioreactor to produce special breakdown products of phytate. J Biotechnol 48 (1996) 153-159
    • (1996) J Biotechnol , vol.48 , pp. 153-159
    • Greiner, R.1    Konietzny, U.2
  • 3
    • 1642578253 scopus 로고    scopus 로고
    • Biochemical properties and substrate specificities of alkaline and histidine acid phytases
    • Oh B.-C., Choi W.-C., Park S., Kim Y.O., and Oh T.K. Biochemical properties and substrate specificities of alkaline and histidine acid phytases. Appl Microbiol Biotechnol 63 (2004) 362-372
    • (2004) Appl Microbiol Biotechnol , vol.63 , pp. 362-372
    • Oh, B.-C.1    Choi, W.-C.2    Park, S.3    Kim, Y.O.4    Oh, T.K.5
  • 4
    • 0030898612 scopus 로고    scopus 로고
    • Gene cloning, purification and characterization of a heat stable phytase from the fungus Aspergillus fumigatus
    • Pasamontes L., Haiker M., Wyss M., Tessier M., and van Loon A.P.G.M. Gene cloning, purification and characterization of a heat stable phytase from the fungus Aspergillus fumigatus. Appl Environ Microbiol 63 (1997) 1696-1700
    • (1997) Appl Environ Microbiol , vol.63 , pp. 1696-1700
    • Pasamontes, L.1    Haiker, M.2    Wyss, M.3    Tessier, M.4    van Loon, A.P.G.M.5
  • 5
    • 0030775099 scopus 로고    scopus 로고
    • Cloning of phytases from the fungus Emericella nidulans and the thermophilic fungus Talaromyces thermophilus
    • Pasamontes L., Haiker M., Henriquez-Huecas M., Mitchell D.B., and van Loon A.P.G.M. Cloning of phytases from the fungus Emericella nidulans and the thermophilic fungus Talaromyces thermophilus. Biochem Biophys Acta 1353 (1997) 217-223
    • (1997) Biochem Biophys Acta , vol.1353 , pp. 217-223
    • Pasamontes, L.1    Haiker, M.2    Henriquez-Huecas, M.3    Mitchell, D.B.4    van Loon, A.P.G.M.5
  • 6
    • 0000464339 scopus 로고
    • Substrate selectivity in Aspergillus ficuum phytase and acid phosphatases using myo-inositol phosphates
    • Ullah A.H.J., and Phillippy B.Q. Substrate selectivity in Aspergillus ficuum phytase and acid phosphatases using myo-inositol phosphates. J Agric Food Chem 42 (1994) 423-425
    • (1994) J Agric Food Chem , vol.42 , pp. 423-425
    • Ullah, A.H.J.1    Phillippy, B.Q.2
  • 7
    • 0027374538 scopus 로고
    • The cloning and sequencing of the genes encoding phytase (phy) and pH 2.5 optimum acid phosphatase (aph) from Aspergillus niger var. awamori
    • Piddington C.S., Houston C.S., Paloheimo M., Cantrell M., Miettinen-Oinonen A., Nevalanien H., et al. The cloning and sequencing of the genes encoding phytase (phy) and pH 2.5 optimum acid phosphatase (aph) from Aspergillus niger var. awamori. Gene 133 (1993) 55-62
    • (1993) Gene , vol.133 , pp. 55-62
    • Piddington, C.S.1    Houston, C.S.2    Paloheimo, M.3    Cantrell, M.4    Miettinen-Oinonen, A.5    Nevalanien, H.6
  • 9
    • 0027293975 scopus 로고
    • Aspergillus ficuum phytase: complete primary structure elucidation by chemical sequencing
    • Ullah A.H.J., and Dischinger H.C. Aspergillus ficuum phytase: complete primary structure elucidation by chemical sequencing. Biochem Biophys Res Commun 192 (1993) 747-753
    • (1993) Biochem Biophys Res Commun , vol.192 , pp. 747-753
    • Ullah, A.H.J.1    Dischinger, H.C.2
  • 10
    • 2942571354 scopus 로고    scopus 로고
    • Production studies and catalytic properties of phytases (myo-inositol hexakis phosphate phosphor hydrolases): an overview
    • Vats P., and Banerjee U.C. Production studies and catalytic properties of phytases (myo-inositol hexakis phosphate phosphor hydrolases): an overview. Enzyme Microb Technol 35 (2004) 3-14
    • (2004) Enzyme Microb Technol , vol.35 , pp. 3-14
    • Vats, P.1    Banerjee, U.C.2
  • 11
    • 0031747416 scopus 로고    scopus 로고
    • Isolation, characterization, molecular gene cloning and sequencing of a novel phytase from Bacillus subtilis
    • Kerovuo J., Lauraeus M., Nurminen P., Kalkkinen N., and Apajalahti J. Isolation, characterization, molecular gene cloning and sequencing of a novel phytase from Bacillus subtilis. Appl Environ Microbiol 64 (1998) 2079-2085
    • (1998) Appl Environ Microbiol , vol.64 , pp. 2079-2085
    • Kerovuo, J.1    Lauraeus, M.2    Nurminen, P.3    Kalkkinen, N.4    Apajalahti, J.5
  • 12
    • 0027208581 scopus 로고
    • Purification and characterization of two phytases from Escherichia coli
    • Greiner R., Konietzny U., and Jany K.D. Purification and characterization of two phytases from Escherichia coli. Arch Biochem Biophys 303 (1993) 107-113
    • (1993) Arch Biochem Biophys , vol.303 , pp. 107-113
    • Greiner, R.1    Konietzny, U.2    Jany, K.D.3
  • 13
    • 0027340545 scopus 로고
    • 304 of Escherichia coli acid phosphatase is involved in leaving group protonation
    • 304 of Escherichia coli acid phosphatase is involved in leaving group protonation. J Biol Chem 268 (1993) 20778-20784
    • (1993) J Biol Chem , vol.268 , pp. 20778-20784
    • Ostanin, K.1    van Etten, R.L.2
  • 15
    • 0027193329 scopus 로고
    • Influence of culture conditions on the biosynthesis of Schwanniomyces castellii phytase
    • Lambrechts C., Boze H., Segueilha L., Moulin G., and Galzy P. Influence of culture conditions on the biosynthesis of Schwanniomyces castellii phytase. Biotech Lett 15 (1993) 399-404
    • (1993) Biotech Lett , vol.15 , pp. 399-404
    • Lambrechts, C.1    Boze, H.2    Segueilha, L.3    Moulin, G.4    Galzy, P.5
  • 16
    • 0032976125 scopus 로고    scopus 로고
    • Biophysical characterization of fungal phytases (myo-inositolhexakisphosphate-phosphohydrolases): molecular size, glycosylation pattern and engineering of proteolytic resistance
    • Wyss M., Pasamontes L., Friedlein A., Remy R., Tessier M., Kronenberger A., et al. Biophysical characterization of fungal phytases (myo-inositolhexakisphosphate-phosphohydrolases): molecular size, glycosylation pattern and engineering of proteolytic resistance. Appl Environ Microbiol 65 (1999) 359-366
    • (1999) Appl Environ Microbiol , vol.65 , pp. 359-366
    • Wyss, M.1    Pasamontes, L.2    Friedlein, A.3    Remy, R.4    Tessier, M.5    Kronenberger, A.6
  • 17
    • 0033051539 scopus 로고    scopus 로고
    • Biochemical characterization of fungal phytases (myo-inositolhexakisphosphate-phosphohydrolases): catalytic properties
    • Wyss M., Brugger R., Kronenberger A., Remy R., Fimbel R., Oesterhelt O., et al. Biochemical characterization of fungal phytases (myo-inositolhexakisphosphate-phosphohydrolases): catalytic properties. Appl Environ Microbiol 65 (1999) 367-373
    • (1999) Appl Environ Microbiol , vol.65 , pp. 367-373
    • Wyss, M.1    Brugger, R.2    Kronenberger, A.3    Remy, R.4    Fimbel, R.5    Oesterhelt, O.6
  • 18
    • 0030156656 scopus 로고    scopus 로고
    • Mechanisms of intestinal phosphorus absorption and availability of dietary phosphorus in pigs
    • Schroder B., Breves G., and Rodehutscord M. Mechanisms of intestinal phosphorus absorption and availability of dietary phosphorus in pigs. Dtsc Tieraerztl Wochenschr 103 (1996) 209-214
    • (1996) Dtsc Tieraerztl Wochenschr , vol.103 , pp. 209-214
    • Schroder, B.1    Breves, G.2    Rodehutscord, M.3
  • 19
    • 0006135911 scopus 로고
    • Biological availability of phosphorus for pigs
    • Common F.H. Biological availability of phosphorus for pigs. Nature 143 (1989) 370-380
    • (1989) Nature , vol.143 , pp. 370-380
    • Common, F.H.1
  • 20
    • 0007652632 scopus 로고
    • Phytase in nutrition and waste management
    • Ward N.E. Phytase in nutrition and waste management. Poult Dig 52 (1993) 10-15
    • (1993) Poult Dig , vol.52 , pp. 10-15
    • Ward, N.E.1
  • 21
    • 0007659309 scopus 로고    scopus 로고
    • Reduction of nitrogen and phosphorus from livestock waste: a major priority for intensive animal production
    • Yano F., Nakajima T., and Matsuda M. Reduction of nitrogen and phosphorus from livestock waste: a major priority for intensive animal production. Asian-Aust J Anim Sci 12 (1999) 651-656
    • (1999) Asian-Aust J Anim Sci , vol.12 , pp. 651-656
    • Yano, F.1    Nakajima, T.2    Matsuda, M.3
  • 22
    • 0036807749 scopus 로고    scopus 로고
    • Studies on the production of phytase by a newly isolated strain of Aspergillus niger van teigham obtained from rotten wood logs
    • Vats P., and Banerjee U.C. Studies on the production of phytase by a newly isolated strain of Aspergillus niger van teigham obtained from rotten wood logs. Process Biochem 38 (2002) 211-217
    • (2002) Process Biochem , vol.38 , pp. 211-217
    • Vats, P.1    Banerjee, U.C.2
  • 23
    • 2942748504 scopus 로고    scopus 로고
    • Production of phytase (myo-inositolhexakisphosphate phosphohydrolase) by Aspergillus niger van Teighem in Laboratory-Scale Fermenter
    • Vats P., Sahoo D.K., and Banerjee U.C. Production of phytase (myo-inositolhexakisphosphate phosphohydrolase) by Aspergillus niger van Teighem in Laboratory-Scale Fermenter. Biotechnol Prog 20 (2004) 737-743
    • (2004) Biotechnol Prog , vol.20 , pp. 737-743
    • Vats, P.1    Sahoo, D.K.2    Banerjee, U.C.3
  • 24
    • 0019830545 scopus 로고
    • A new and convenient colorimetric determination of inorganic orthophosphate and its application to the assay of inorganic pyrophosphatase
    • Heinonen J.K., and Lahti R.J. A new and convenient colorimetric determination of inorganic orthophosphate and its application to the assay of inorganic pyrophosphatase. Anal Biochem 113 (1981) 313-317
    • (1981) Anal Biochem , vol.113 , pp. 313-317
    • Heinonen, J.K.1    Lahti, R.J.2
  • 25
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram amounts of protein using the principal of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for quantitation of microgram amounts of protein using the principal of protein-dye binding. Anal Biochem 72 (1976) 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 26
    • 20044364585 scopus 로고    scopus 로고
    • Biochemical characterization of extracellular phytase (myo-inositol hexakisphosphate phosphohydrolase) from a hyper producing strain of Aspergillus niger van Teighem
    • Vats P., and Banerjee U.C. Biochemical characterization of extracellular phytase (myo-inositol hexakisphosphate phosphohydrolase) from a hyper producing strain of Aspergillus niger van Teighem. J Ind Microbiol Biotechnol 32 (2005) 141-147
    • (2005) J Ind Microbiol Biotechnol , vol.32 , pp. 141-147
    • Vats, P.1    Banerjee, U.C.2
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Lammeli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Lammeli, U.K.1
  • 28
    • 0016711037 scopus 로고
    • High resolution two-dimensional gel electrophoresis of proteins
    • O'Farrell P.H. High resolution two-dimensional gel electrophoresis of proteins. J Biol Chem 250 (1975) 4007-4021
    • (1975) J Biol Chem , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 29
    • 0019320450 scopus 로고
    • Behavior of glycopolypeptides with empirical molecular weight estimation methods. 1. Sodium dodecyl sulphate
    • Leach B.S., Collawan Jr. J.F., and Fish W.W. Behavior of glycopolypeptides with empirical molecular weight estimation methods. 1. Sodium dodecyl sulphate. Biochemistry 19 (1980) 5734-5741
    • (1980) Biochemistry , vol.19 , pp. 5734-5741
    • Leach, B.S.1    Collawan Jr., J.F.2    Fish, W.W.3
  • 30
    • 0030152708 scopus 로고    scopus 로고
    • Isolation and identification of phytase producing bacterium, Enterobacter sp.4 and enzymatic properties of phytase enzyme
    • Yoon S.J., Choi Y.J., Min K., Cho K.K., Kim J.W., Lee S.C., et al. Isolation and identification of phytase producing bacterium, Enterobacter sp.4 and enzymatic properties of phytase enzyme. Enzyme Microb Technol 18 (1996) 449-454
    • (1996) Enzyme Microb Technol , vol.18 , pp. 449-454
    • Yoon, S.J.1    Choi, Y.J.2    Min, K.3    Cho, K.K.4    Kim, J.W.5    Lee, S.C.6
  • 31
    • 0028278712 scopus 로고
    • Two distinct molecular forms of phytase from Klebsiella aerogenes: evidence for unusually small active enzyme peptide
    • Tambe S.M., Kaklij G.S., Kelkar S.M., and Parekh L.J. Two distinct molecular forms of phytase from Klebsiella aerogenes: evidence for unusually small active enzyme peptide. J Ferment Bioeng 77 (1994) 23-27
    • (1994) J Ferment Bioeng , vol.77 , pp. 23-27
    • Tambe, S.M.1    Kaklij, G.S.2    Kelkar, S.M.3    Parekh, L.J.4
  • 32
    • 0030743558 scopus 로고    scopus 로고
    • Soil isolates of Pseudomonas sp. that utilize inositol phosphates
    • Richardson A.E., and Hadobas P.A. Soil isolates of Pseudomonas sp. that utilize inositol phosphates. Can J Microbiol 43 (1997) 509-516
    • (1997) Can J Microbiol , vol.43 , pp. 509-516
    • Richardson, A.E.1    Hadobas, P.A.2
  • 33
    • 0000095725 scopus 로고    scopus 로고
    • High-level expression of a recombinant thermostable phytase in Bacillus subtilis
    • Kim Y.O., Lee J.K., Oh B.C., and Oh T.K. High-level expression of a recombinant thermostable phytase in Bacillus subtilis. Biosci Biotechnol Biochem 63 (1999) 2205-2207
    • (1999) Biosci Biotechnol Biochem , vol.63 , pp. 2205-2207
    • Kim, Y.O.1    Lee, J.K.2    Oh, B.C.3    Oh, T.K.4
  • 34
    • 0033952605 scopus 로고    scopus 로고
    • Characterization and overproduction of the Escherichia coli appA encoded bifunctional enzyme that exhibits both phytase and acid phosphatase activities
    • Golovan S., Wang G.R., Zhang J., and Forsberg C.W. Characterization and overproduction of the Escherichia coli appA encoded bifunctional enzyme that exhibits both phytase and acid phosphatase activities. Can J Microbiol 46 (2000) 59-71
    • (2000) Can J Microbiol , vol.46 , pp. 59-71
    • Golovan, S.1    Wang, G.R.2    Zhang, J.3    Forsberg, C.W.4
  • 35
    • 0032512539 scopus 로고    scopus 로고
    • Differences in the active site environment of Aspergillus ficuum phytases
    • Ullah A.H.J., and Sethumadhavan K. Differences in the active site environment of Aspergillus ficuum phytases. Biochem Biophys Res Commun 243 (1998) 458-462
    • (1998) Biochem Biophys Res Commun , vol.243 , pp. 458-462
    • Ullah, A.H.J.1    Sethumadhavan, K.2
  • 36
    • 0023493960 scopus 로고
    • Purification N-terminal amino acid sequence and characterization of pH 2.5 optimum acid phosphatase (E.C. 3.1.3.2) from Aspergillus ficuum
    • Ullah A.H.J., and Cummins B.J. Purification N-terminal amino acid sequence and characterization of pH 2.5 optimum acid phosphatase (E.C. 3.1.3.2) from Aspergillus ficuum. Prep Biochem 17 (1987) 397-422
    • (1987) Prep Biochem , vol.17 , pp. 397-422
    • Ullah, A.H.J.1    Cummins, B.J.2
  • 37
    • 0024254188 scopus 로고
    • Production, rapid purification and catalytic characterization of extracellular phytase from Aspergillus ficuum
    • Ullah A.H.J. Production, rapid purification and catalytic characterization of extracellular phytase from Aspergillus ficuum. Prep Biochem 18 (1988) 443-458
    • (1988) Prep Biochem , vol.18 , pp. 443-458
    • Ullah, A.H.J.1
  • 38
    • 0023706503 scopus 로고
    • Aspergillus ficuum extracellular pH 6.0 optimum acid phosphatase: purification, N-terminal amino acid sequence and biochemical characterization
    • Ullah A.H.J., and Cummins B.J. Aspergillus ficuum extracellular pH 6.0 optimum acid phosphatase: purification, N-terminal amino acid sequence and biochemical characterization. Prep Biochem 18 (1988) 37-65
    • (1988) Prep Biochem , vol.18 , pp. 37-65
    • Ullah, A.H.J.1    Cummins, B.J.2
  • 40
    • 0344289519 scopus 로고    scopus 로고
    • Role of glycosylation in functional expression of an Aspergillus niger phytase (phyA) in Pichia pastoris
    • Han Y.W., and Lei X.G. Role of glycosylation in functional expression of an Aspergillus niger phytase (phyA) in Pichia pastoris. Arch Biochem Biophys 364 (1999) 83-90
    • (1999) Arch Biochem Biophys , vol.364 , pp. 83-90
    • Han, Y.W.1    Lei, X.G.2
  • 41
    • 0032500806 scopus 로고    scopus 로고
    • Myo-inositol hexasulphate is a potent inhibitor of Aspergillus ficuum phytase
    • Ullah A.H.J., and Sethumadhavan K. Myo-inositol hexasulphate is a potent inhibitor of Aspergillus ficuum phytase. Biochem Biophys Res Commun 251 (1998) 260-263
    • (1998) Biochem Biophys Res Commun , vol.251 , pp. 260-263
    • Ullah, A.H.J.1    Sethumadhavan, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.