메뉴 건너뛰기




Volumn 100, Issue 6, 2009, Pages 2046-2051

Characterization of a HAP-phytase from a thermophilic mould Sporotrichum thermophile

Author keywords

Characterization; Dephytinization; Histidine acid phosphatase; Phytase; Sporotrichum thermophile

Indexed keywords

ACETONE; ACTIVATION ENERGY; AMINES; AMINO ACIDS; CARBOHYDRATES; CATALYST ACTIVITY; CHROMATOGRAPHIC ANALYSIS; COLLOIDS; COLUMN CHROMATOGRAPHY; ENZYMES; GELATION; ION CHROMATOGRAPHY; ION EXCHANGE; MAGNESIUM PRINTING PLATES; ORGANIC ACIDS; POROUS MATERIALS; PURIFICATION; RATE CONSTANTS; UREA;

EID: 57449117452     PISSN: 09608524     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biortech.2008.10.025     Document Type: Article
Times cited : (48)

References (36)
  • 1
    • 2442591675 scopus 로고    scopus 로고
    • Identification and characterization of a phytase of potential commercial interest
    • Casey A., and Walsh G. Identification and characterization of a phytase of potential commercial interest. J. Biotechnol. 110 3 (2004) 313-322
    • (2004) J. Biotechnol. , vol.110 , Issue.3 , pp. 313-322
    • Casey, A.1    Walsh, G.2
  • 3
    • 0035127555 scopus 로고    scopus 로고
    • Improvement of phytase thermostability by using sorghum liquor wastes supplemented with starch
    • Chen C., Hunag C., and Cheng K. Improvement of phytase thermostability by using sorghum liquor wastes supplemented with starch. Biotechnol. Lett. 23 (2001) 331-333
    • (2001) Biotechnol. Lett. , vol.23 , pp. 331-333
    • Chen, C.1    Hunag, C.2    Cheng, K.3
  • 4
    • 0001796193 scopus 로고
    • An experimental study of the life cycles and taxonomy of Allomyces
    • Emerson R. An experimental study of the life cycles and taxonomy of Allomyces. Lloydia 4 (1941) 77-144
    • (1941) Lloydia , vol.4 , pp. 77-144
    • Emerson, R.1
  • 5
    • 0000154206 scopus 로고
    • The colorimetric determination of phosphorous
    • Fiske C.H., and Subbarow Y. The colorimetric determination of phosphorous. J. Biol. Chem. 65 (1925) 375-380
    • (1925) J. Biol. Chem. , vol.65 , pp. 375-380
    • Fiske, C.H.1    Subbarow, Y.2
  • 7
    • 34447547676 scopus 로고    scopus 로고
    • Production, purification and characterization of thermostable phytase from thermophilic fungus Thermomyces lanuginosus TL-7
    • Gulati H.K., Chadha B.S., and Saini H.S. Production, purification and characterization of thermostable phytase from thermophilic fungus Thermomyces lanuginosus TL-7. Acta Microbiol. Immunol. Hung. 54 2 (2007) 121-138
    • (2007) Acta Microbiol. Immunol. Hung. , vol.54 , Issue.2 , pp. 121-138
    • Gulati, H.K.1    Chadha, B.S.2    Saini, H.S.3
  • 8
    • 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
  • 9
    • 34250779286 scopus 로고    scopus 로고
    • Yeast phytases: present scenario and future perspectives
    • Kaur P., Kunze G., and Satyanarayana T. Yeast phytases: present scenario and future perspectives. Crit. Rev. Biotechnol. 27 2 (2007) 93-109
    • (2007) Crit. Rev. Biotechnol. , vol.27 , Issue.2 , pp. 93-109
    • Kaur, P.1    Kunze, G.2    Satyanarayana, T.3
  • 10
    • 0036392241 scopus 로고    scopus 로고
    • Molecular and catalytic properties of phytate-degrading enzymes (phytases)
    • Konietzny U., and Greiner R. Molecular and catalytic properties of phytate-degrading enzymes (phytases). Int. J. Food Sci. Technol. 37 7 (2002) 791-812
    • (2002) Int. J. Food Sci. Technol. , vol.37 , Issue.7 , pp. 791-812
    • Konietzny, U.1    Greiner, R.2
  • 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 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 0019320450 scopus 로고
    • Behaviour of glycopolypeptides with empirical molecular weight estimation methods. 1. Sodium dodecyl sulphate
    • Leach B.S., Collawan Jr. J.F., and Fish W.W. Behaviour 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
  • 15
    • 0033952704 scopus 로고    scopus 로고
    • Crystal structures of Escherichia coli phytase and its complex with phytate
    • Lim D., Golovan S., Forsberg C.W., and Jia Z. Crystal structures of Escherichia coli phytase and its complex with phytate. Nat. Struct. Biol. 7 2 (2000) 108-113
    • (2000) Nat. Struct. Biol. , vol.7 , Issue.2 , pp. 108-113
    • Lim, D.1    Golovan, S.2    Forsberg, C.W.3    Jia, Z.4
  • 17
    • 0031034203 scopus 로고    scopus 로고
    • The phytase subfamily of histidine acid phosphatases: isolation of genes for two novel phytases from the 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 phosphatases: isolation of genes for two novel phytases from the fungi Aspergillus terreus and Myceliophthora thermophila. Microbiology 143 Pt 1 (1997) 245-252
    • (1997) Microbiology , vol.143 , Issue.PART 1 , pp. 245-252
    • Mitchell, D.B.1    Vogel, K.2    Weimann, B.J.3    Pasamontes, L.4    van Loon, A.P.G.M.5
  • 19
    • 0030271204 scopus 로고    scopus 로고
    • Comparative thermostability of glucose dehydrogenase from Haloferax mediterranei. Effects of salts and polyols
    • Obon J.M., Manjon A., and Iborra J.L. Comparative thermostability of glucose dehydrogenase from Haloferax mediterranei. Effects of salts and polyols. Enzyme Microb. Technol. 19 (1996) 352-360
    • (1996) Enzyme Microb. Technol. , vol.19 , pp. 352-360
    • Obon, J.M.1    Manjon, A.2    Iborra, J.L.3
  • 20
    • 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 5 (1997) 1696-1700
    • (1997) Appl. Environ. Microbiol. , vol.63 , Issue.5 , pp. 1696-1700
    • Pasamontes, L.1    Haiker, M.2    Wyss, M.3    Tessier, M.4    van Loon, A.P.G.M.5
  • 21
    • 0026702174 scopus 로고
    • Purification and properties of the phytase from Schwanniomyces castellii
    • Segueilha L., Lambrechts C., Boze H., Moulin G., and Galzy P. Purification and properties of the phytase from Schwanniomyces castellii. J. Ferment. Bioeng. 74 1 (1992) 7-11
    • (1992) J. Ferment. Bioeng. , vol.74 , Issue.1 , pp. 7-11
    • Segueilha, L.1    Lambrechts, C.2    Boze, H.3    Moulin, G.4    Galzy, P.5
  • 22
    • 0014645175 scopus 로고
    • Regulation of the formation of acid phosphatase by inorganic phosphate in Aspergillus ficuum
    • Shieh T.R., Wodzinski R.J., and Ware J.H. Regulation of the formation of acid phosphatase by inorganic phosphate in Aspergillus ficuum. J. Bacteriol. 100 (1969) 1161-1165
    • (1969) J. Bacteriol. , vol.100 , pp. 1161-1165
    • Shieh, T.R.1    Wodzinski, R.J.2    Ware, J.H.3
  • 23
    • 84925491834 scopus 로고
    • Purification and characterization of phytase and acid phosphatase produced by Aspergillus oryzae K1
    • Shimizu M. Purification and characterization of phytase and acid phosphatase produced by Aspergillus oryzae K1. Biosci. Biotechnol. Biochem. 57 (1993) 1364-1365
    • (1993) Biosci. Biotechnol. Biochem. , vol.57 , pp. 1364-1365
    • Shimizu, M.1
  • 24
    • 38849180346 scopus 로고    scopus 로고
    • Fungal phytases for improving the nutritional status of foods and combating environmental phosphorus pollution
    • Chauhan A.K., and Verma A. (Eds), IK International Publishers, New Delhi, India
    • Singh B., Kaur P., and Satyanarayana T. Fungal phytases for improving the nutritional status of foods and combating environmental phosphorus pollution. In: Chauhan A.K., and Verma A. (Eds). Microbes: Health and Environment (2006), IK International Publishers, New Delhi, India 289-326
    • (2006) Microbes: Health and Environment , pp. 289-326
    • Singh, B.1    Kaur, P.2    Satyanarayana, T.3
  • 25
    • 33745085451 scopus 로고    scopus 로고
    • Phytase production by a thermophilic mould Sporotrichum thermophile in solid state fermentation and its application in dephytinization of sesame oil cake
    • Singh B., and Satyanarayana T. Phytase production by a thermophilic mould Sporotrichum thermophile in solid state fermentation and its application in dephytinization of sesame oil cake. Appl. Biochem. Biotechnol. 133 3 (2006) 239-250
    • (2006) Appl. Biochem. Biotechnol. , vol.133 , Issue.3 , pp. 239-250
    • Singh, B.1    Satyanarayana, T.2
  • 26
    • 33745958259 scopus 로고    scopus 로고
    • A marked enhancement in phytase production by a thermophilic mould Sporotrichum thermophile using statistical designs in a cost-effective cane molasses medium
    • Singh B., and Satyanarayana T. A marked enhancement in phytase production by a thermophilic mould Sporotrichum thermophile using statistical designs in a cost-effective cane molasses medium. J. Appl. Microbiol. 101 2 (2006) 344-352
    • (2006) J. Appl. Microbiol. , vol.101 , Issue.2 , pp. 344-352
    • Singh, B.1    Satyanarayana, T.2
  • 27
    • 36049031172 scopus 로고    scopus 로고
    • Improved phytase production by a thermophilic mould Sporotrichum thermophile in submerged fermentation due to statistical optimization
    • Singh B., and Satyanarayana T. Improved phytase production by a thermophilic mould Sporotrichum thermophile in submerged fermentation due to statistical optimization. Bioresour. Technol. 99 4 (2008) 824-830
    • (2008) Bioresour. Technol. , vol.99 , Issue.4 , pp. 824-830
    • Singh, B.1    Satyanarayana, T.2
  • 28
    • 38849085992 scopus 로고    scopus 로고
    • Phytase production by Sporotrichum thermophile in solid state fermentation and its applications
    • Singh B., and Satyanarayana T. Phytase production by Sporotrichum thermophile in solid state fermentation and its applications. Bioresour. Technol. 99 8 (2008) 2824-2830
    • (2008) Bioresour. Technol. , vol.99 , Issue.8 , pp. 2824-2830
    • Singh, B.1    Satyanarayana, T.2
  • 29
    • 56649097463 scopus 로고    scopus 로고
    • Phytase production by Sporotrichum thermophile in a cost-effective cane molasses medium in submerged fermentation and its application in bread
    • 10.1111/j.1365-2672.2008.03929.x
    • Singh B., and Satyanarayana T. Phytase production by Sporotrichum thermophile in a cost-effective cane molasses medium in submerged fermentation and its application in bread. J. Appl. Microbiol. (2008) 10.1111/j.1365-2672.2008.03929.x
    • (2008) J. Appl. Microbiol.
    • Singh, B.1    Satyanarayana, T.2
  • 30
    • 33646252921 scopus 로고    scopus 로고
    • Hydrolysis of precipitated phytate by three distinct families of phytases
    • Tang J., Leung A., Leung C., and Lim B.L. Hydrolysis of precipitated phytate by three distinct families of phytases. Soil Biol. Biochem. 38 (2006) 1316-1324
    • (2006) Soil Biol. Biochem. , vol.38 , pp. 1316-1324
    • Tang, J.1    Leung, A.2    Leung, C.3    Lim, B.L.4
  • 31
    • 20044364585 scopus 로고    scopus 로고
    • Biochemical characterisation of extracellular phytase (myo-inositol hexakisphosphate phosphohydrolase) from a hyper-producing strain of Aspergillus niger van Teighem
    • Vats P., and Banerjee U.C. Biochemical characterisation of extracellular phytase (myo-inositol hexakisphosphate phosphohydrolase) from a hyper-producing strain of Aspergillus niger van Teighem. J. Ind. Microbiol. Biotechnol. 32 4 (2005) 141-147
    • (2005) J. Ind. Microbiol. Biotechnol. , vol.32 , Issue.4 , pp. 141-147
    • Vats, P.1    Banerjee, U.C.2
  • 32
    • 0036789458 scopus 로고    scopus 로고
    • Purification and characterization of a thermostable and acid-stable phytase from Pichia anomala
    • Vohra A., and Satyanarayana T. Purification and characterization of a thermostable and acid-stable phytase from Pichia anomala. World J. Microbiol. Biotechnol. 18 (2002) 687-691
    • (2002) World J. Microbiol. Biotechnol. , vol.18 , pp. 687-691
    • Vohra, A.1    Satyanarayana, T.2
  • 33
    • 0037247952 scopus 로고    scopus 로고
    • Phytases: microbial sources, production, purification and potential biotechnological applications
    • Vohra A., and Satyanarayana T. Phytases: microbial sources, production, purification and potential biotechnological applications. Crit. Rev. Biotechnol. 23 1 (2003) 29-60
    • (2003) Crit. Rev. Biotechnol. , vol.23 , Issue.1 , pp. 29-60
    • Vohra, A.1    Satyanarayana, T.2
  • 35
    • 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., and Oesterhelt O. 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
  • 36
    • 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., and Kronenberger A. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.