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Characterisation of an acid trehalase produced by the thermotolerant fungus Rhizopus microsporus var. rhizopodiformis: Biochemical properties and immunochemical localisation

de Aquino, Ana Carla Medeiros Morato ; Peixoto-Nogueira, Simone Carvalho ; Jorge, João Atílio ; Terenzi, Héctor Francisco ; Polizeli, Maria de Lourdes Teixeira de Moraes

FEMS microbiology letters, 2005-10, Vol.251 (1), p.169-175 [Periódico revisado por pares]

Oxford, UK: Elsevier B.V

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Título:
Characterisation of an acid trehalase produced by the thermotolerant fungus Rhizopus microsporus var. rhizopodiformis: Biochemical properties and immunochemical localisation
Autor: de Aquino, Ana Carla Medeiros Morato ; Peixoto-Nogueira, Simone Carvalho ; Jorge, João Atílio ; Terenzi, Héctor Francisco ; Polizeli, Maria de Lourdes Teixeira de Moraes
Assuntos: Acids ; Biological and medical sciences ; Carbohydrates ; Carbohydrates - analysis ; Cell surface ; Dimerization ; Edetic Acid - pharmacology ; Endoglycosidase H ; Enzyme Activators - pharmacology ; Enzyme Stability ; Enzymes ; Exoenzymes ; Fundamental and applied biological sciences. Psychology ; Fungi ; Gel electrophoresis ; Growth, nutrition, metabolism, transports, enzymes. Molecular biology ; Homogeneity ; Hydrogen-Ion Concentration ; Immunochemical localisation ; Isoelectric Point ; Kinetics ; Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - metabolism ; Metals - pharmacology ; Microbiology ; Molecular Weight ; Mycology ; Rhizopus ; Rhizopus - chemistry ; Rhizopus - enzymology ; Rhizopus microsporus ; Sodium lauryl sulfate ; Temperature ; Trehalase - chemistry ; Trehalase - isolation & purification ; Trehalase - metabolism ; Trehalose ; Trehalose - metabolism ; α,α-Trehalase
É parte de: FEMS microbiology letters, 2005-10, Vol.251 (1), p.169-175
Notas: Edited by M. Moracci
ObjectType-Article-1
SourceType-Scholarly Journals-1
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Descrição: An acid trehalase from Rhizopus microsporus var. rhizopodiformis was purified to apparent homogeneity. The molecular weight by SDS–PAGE (60 kDa) or Sephacryl S-200 filtration (105 kDa) suggested a homodimer. The carbohydrate content was 72%. Endoglycosidase H digestion resulted in one sharp band of 51.5 kDa in SDS–PAGE. pH and temperature optima were 4.5 and 45 °C, respectively. The isoelectric point was 6.69 and activation energy was 1.14 kcal mol −1. The enzyme was stable for 1 h at 50 °C and decayed at 60 °C ( t 50 of 1.3 min.). Apparent K M for trealose was 0.2 mM. Immunolocalisation studies showed the enzyme tightly packed at the surface of the cells.
Editor: Oxford, UK: Elsevier B.V
Idioma: Inglês

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Characterisation of an acid trehalase produced by the thermotolerant fungus Rhizopus microsporus var. rhizopodiformis: Biochemical properties and immunochemical localisation

de Aquino, Ana Carla Medeiros Morato ; Peixoto-Nogueira, Simone Carvalho ; Jorge, João Atílio ; Terenzi, Héctor Francisco ; Polizeli, Maria de Lourdes Teixeira de Moraes

Oxford, UK: Elsevier B.V

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