Thermal stability and starch degradation profile of α-amylase from streptomyces avermitilis

Sang Youn Hwang, Kazunori Nakashima, Naoko Okai, Fumiyoshi Okazaki, Michiru Miyake, Koichi Harazono, Chiaki Ogino, Akihiko Kondo

Research output: Contribution to journalArticlepeer-review

13 Citations (Scopus)


Amylases from Streptomyces are useful in the production of maltooligosaccharides, but they have weak thermal stability at temperatures higher than 40 °C. In this study, α-amylase (SAV5981 gene of Streptomyces avermitilis) was expressed from Streptomyces lividans 1326 and purified by ammonium sulfate fractionation followed by anionic chromatography (Q-HP sepharose). The properties of the purified SAV5981 amylase were determined by the starch-iodine method. The effect of metal ions on amylase activity was investigated. The optimal temperature shifted from 25 to 50 °C with the addition of the Ca2+ ion. The thermal stability of SAV5981 was also dramatically enhanced by the addition of 10mM CaCl2. Improvement of the thermal stability of SAV5981 was examined by CD spectra in the presence and the absence of the Ca2+ ion. Thin-layer chromatography (TLC) analysis and HPLC analysis of starch degradation revealed that SAV5981 mainly produced maltose and maltotriose, not glucose. The maltoorigosaccharide-producing amylase examined in this study has the potential in the industrial application of oligosaccharide production.

Original languageEnglish
Pages (from-to)2449-2453
Number of pages5
JournalBioscience, Biotechnology and Biochemistry
Issue number12
Publication statusPublished - 2013
Externally publishedYes


  • Calcium-dependent thermal stability
  • Maltogenic α-amylase
  • Streptomyces avermitilis

ASJC Scopus subject areas

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry


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