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Purification and biochemical characterization of thermostable alkaline phosphatases produced by Rhizopus microsporus var. rhizopodiformis

Barbosa Junior, A.,Universidade de Sao Paulo (Brazil). Departamento De Bioquimica e Imunologia ; Guimaraes, L.H.S.,Universidade de Sao Paulo (Brazil). Departamento De Biologia ; Terenzi, H.F.,Universidade de Sao Paulo (Brazil). Departamento De Biologia ; Jorge, J.A.,Universidade de Sao Paulo (Brazil). Departamento De Biologia ; Leone, F.A.,Universidade de Sao Paulo (Brazil). Departamento De Quimica ; Polizeli, M.L.T.M.,Universidade de Sao Paulo (Brazil). Departamento De Biologia

Folia microbiologica, 2008-01, Vol.53 (6), p.509-516 [Periódico revisado por pares]

Dordrecht: Springer Netherlands

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Título:
Purification and biochemical characterization of thermostable alkaline phosphatases produced by Rhizopus microsporus var. rhizopodiformis
Autor: Barbosa Junior, A.,Universidade de Sao Paulo (Brazil). Departamento De Bioquimica e Imunologia ; Guimaraes, L.H.S.,Universidade de Sao Paulo (Brazil). Departamento De Biologia ; Terenzi, H.F.,Universidade de Sao Paulo (Brazil). Departamento De Biologia ; Jorge, J.A.,Universidade de Sao Paulo (Brazil). Departamento De Biologia ; Leone, F.A.,Universidade de Sao Paulo (Brazil). Departamento De Quimica ; Polizeli, M.L.T.M.,Universidade de Sao Paulo (Brazil). Departamento De Biologia
Assuntos: ACTIVADOR ENZIMATICO ; ACTIVATEUR D'ENZYME ; ACTIVIDAD ENZIMATICA ; ACTIVITE ENZYMATIQUE ; ALKALINE PHOSPHATASE ; Alkaline Phosphatase - isolation & purification ; Alkaline Phosphatase - metabolism ; ALUMINIO ; ALUMINIUM ; Applied Microbiology ; BIOCHEMISTRY ; BIOCHIMIE ; Biomedical and Life Sciences ; BIOQUIMICA ; Cations - pharmacology ; Chromatography, Agarose ; Chromatography, DEAE-Cellulose ; Chromatography, Gel ; CINC ; CULTURE MEDIA ; ELECTROFORESIS ; ELECTROPHORESE ; ELECTROPHORESIS ; Electrophoresis, Polyacrylamide Gel ; Environmental Engineering/Biotechnology ; ENZYME ACTIVATORS ; ENZYME ACTIVITY ; ESTABILIDAD ; FOSFATASA ALCALINA ; Fungal Proteins - isolation & purification ; Fungal Proteins - metabolism ; HIDROLISIS ; Hot Temperature ; http://www.fao.org/aos/agrovoc#c_10204 ; http://www.fao.org/aos/agrovoc#c_24940 ; http://www.fao.org/aos/agrovoc#c_2523 ; http://www.fao.org/aos/agrovoc#c_2604 ; http://www.fao.org/aos/agrovoc#c_267 ; http://www.fao.org/aos/agrovoc#c_27513 ; http://www.fao.org/aos/agrovoc#c_317 ; http://www.fao.org/aos/agrovoc#c_36930 ; http://www.fao.org/aos/agrovoc#c_4517 ; http://www.fao.org/aos/agrovoc#c_4570 ; http://www.fao.org/aos/agrovoc#c_4892 ; http://www.fao.org/aos/agrovoc#c_5753 ; http://www.fao.org/aos/agrovoc#c_6377 ; http://www.fao.org/aos/agrovoc#c_6568 ; http://www.fao.org/aos/agrovoc#c_7145 ; http://www.fao.org/aos/agrovoc#c_7657 ; http://www.fao.org/aos/agrovoc#c_8517 ; http://www.fao.org/aos/agrovoc#c_910 ; Hydrogen-Ion Concentration ; HYDROLYSE ; HYDROLYSIS ; Immunology ; Life Sciences ; MAGNESIO ; MAGNESIUM ; MANGANESE ; MANGANESO ; MEDIO DE CULTIVO ; Microbiology ; MILIEU DE CULTURE ; MOLECULAR WEIGHT ; PESO MOLECULAR ; PHOSPHATASE ALCALINE ; POIDS MOLECULAIRE ; PURIFICACION ; PURIFICATION ; RHIZOPUS ; Rhizopus - enzymology ; Rhizopus microsporus ; SODIO ; SODIUM ; STABILITE ; STABILITY ; TEMPERATURA ; TEMPERATURE ; Triticum aestivum ; ZINC
É parte de: Folia microbiologica, 2008-01, Vol.53 (6), p.509-516
Notas: P34
2009000371
http://www.cssm.info/priloha/fm2008_509.pdf
ObjectType-Article-1
SourceType-Scholarly Journals-1
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Descrição: The purification and kinetic characterization of intra- and extracellular alkaline phosphatases (AIPs) produced by the thermotolerant fungus Rhizopus microsporus var. rhizopodiformis is described in this article. High enzymic levels were produced within 1-2 d in agitated cultures with 1% of wheat bran. Intra- and extracellular AIPs were purified 5.0 and 9.3x, respectively, by DEAE-cellulose and ConA-sepharose chromatography. Molar mass of 118 and 120 kDa was estimated by gel filtration for both forms of phosphatases. SDS-PAGE indicated dimeric structures of 57 kDa for both forms. Mn2+, Na+ and Mg2+ stimulated the activity, while Al3+ and Zn2+ activated only the extracellular form. Optimum temperature and pH for both phosphatases were 65 deg C and pH 8.0, resp. The enzymes were stable at 50 deg C for at least 15 min. Hydrolysis of 4-nitrophenyl phosphate exhibited a Km 0.28 and 0.22 mmol/L, with Vlim 5.89 and 4.84 U/mg, for intra- and extracellular phosphatases, respectively. The properties of the reported AIPs may be suitable for biotechnological applications.
Editor: Dordrecht: Springer Netherlands
Idioma: Inglês

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Purification and biochemical characterization of thermostable alkaline phosphatases produced by Rhizopus microsporus var. rhizopodiformis

Dordrecht: Springer Netherlands

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