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. PolizeliEmail author
Original Paper


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).


Thermophilic Fungus Amylolytic Activity Maltotetraoses Glucoamylase Activity Maltopentaoses 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.



This work was supported by grants from Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) and Conselho de Desenvolvimento Científico e Tecnológico (CNPq). H.F.T., J.A.J. and M.L.T.M.P. are Research Fellows of CNPq. A.C.M.M.A. was the recipient of a CAPES Fellowship. This work was part of a Master Dissertation submitted by A.C.M.M.A. to the Departamento de Biologia, FFCLRP, USP. We thank Ricardo Alarcon and Mauricio de Oliveira for technical assistance.


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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
    Email author
  1. 1.Departamento de Biologia, Faculdade de Filosofia, Ciências e Letras de Ribeirão PretoUniversidade de São PauloSão PauloBrazil

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