Applied Microbiology and Biotechnology

, Volume 61, Issue 4, pp 323–328 | Cite as

Studies on a thermostable α-amylase from the thermophilic fungus Scytalidium thermophilum

  • A. C. M. M. Aquino
  • J. A. Jorge
  • H. F. Terenzi
  • M. L. T. M. Polizeli
Original Paper

Abstract

An α-amylase produced by Scytalidium thermophilum was purified using DEAE-cellulose and CM-cellulose ion exchange chromatography and Sepharose 6B gel filtration. The purified protein migrated as a single band in 6% PAGE and 7% SDS-PAGE. The estimated molecular mass was 36 kDa (SDS-PAGE) and 49 kDa (Sepharose 6B). Optima of pH and temperature were 6.0 and 60°C, respectively. In the absence of substrate the purified α-amylase was stable for 1 h at 50°C and had a half-life of 12 min at 60°C, but was fully stable in the presence of starch. The enzyme was not activated by several metal ions tested, including Ca2+ (up to 10 mM), but HgCl2 and CuCl2 inhibited its activity. The α-amylase produced by S. thermophilum preferentially hydrolyzed starch, and to a lesser extent amylopectin, maltose, amylose and glycogen in that order. The products of starch hydrolysis (up to 6 h of reaction) analyzed by thin layer chromatography, showed oligosaccharides such as maltotrioses, maltotetraoses and maltopentaoses. Maltose and traces of glucose were formed only after 3 h of reaction. These results confirm the character of the enzyme studied to be an α-amylase (1,4-α-glucan glucanohydrolase).

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Copyright information

© Springer-Verlag 2003

Authors and Affiliations

  • A. C. M. M. Aquino
    • 1
  • J. A. Jorge
    • 1
  • H. F. Terenzi
    • 1
  • M. L. T. M. Polizeli
    • 1
  1. 1.Departamento de Biologia, Faculdade de Filosofia, Ciências e Letras de Ribeirão PretoUniversidade de São PauloSão PauloBrazil

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