Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9121427 | FEMS Microbiology Letters | 2005 | 7 Pages |
Abstract
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 molâ1. The enzyme was stable for 1 h at 50 °C and decayed at 60 °C (t50 of 1.3 min.). Apparent KM for trealose was 0.2 mM. Immunolocalisation studies showed the enzyme tightly packed at the surface of the cells.
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Authors
Ana Carla Medeiros Morato de Aquino, Simone Carvalho Peixoto-Nogueira, João AtÃlio Jorge, Héctor Francisco Terenzi, Maria de Lourdes Teixeira de Moraes Polizeli,