Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Production of Maltopentaose and Biochemical Characterization of Maltopentaose-Forming Amylase

  • Kim, Young-Min (Department of Biomedical Engineering, Chonnam National University) ;
  • Ryu, Hwa-Ja (Department of Fine Chemical Engineering, Chonnam National University) ;
  • Lee, Sun-Ok (Department of Materials and Biochemical Engineering, Chonnam National University) ;
  • Seo, Eun-Seong (Department of Materials and Biochemical Engineering, Chonnam National University) ;
  • Lee, So-Young (Department of Materials and Biochemical Engineering, Chonnam National University) ;
  • Yoo, Sun-Kyun (The Engineering Research Institute, Chonnam National University) ;
  • Cho, Dong-Lyun (Department of Fine Chemical Engineering, Chonnam National University) ;
  • Kim, Do-Man (Division of Chemical Engineering and Research Institute for Catalysis, Chonnam National University/East Coastal Marine Bioresources Research Center at Kangnung National University) ;
  • Kimura, Atsuo (Graduate School of Agriculture, Hokkaido University) ;
  • Chiba, Seiya (Graduate School of Agriculture, Hokkaido University) ;
  • Lee, Jin-Ha (Graduate School of Agriculture, Hokkaido University)
  • Published : 2001.08.01
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Abstract

Bacillus sp. AIR-5, a strain from soil, produced an extracellular maltopentaose-forming amylase from amylose and soluble starch. This bacterium produced 8.9 g/l of maltopentaose from 40 g/l of soluble starch in a batch fermentation and the maltopentaose made up 90 % of the maltooligosaccharides produced (from maltose to maltoheptaose). The culture supernatant was concentrated using a 30 K molecular weight cut-off membrane and purified by DEAE-Cellulose and Sephadex G-150 column chromatographies. The purified protein showed one band on a native-PAGE and its molecular mass was estimated as 250 kDa. The 250-kDa protein was composed of tetramers of a 63-kDa protein. the isoelectric point of the purified protein was pH 6.9, and the optimum temperature for the enzyme activity was $45^{\circ}C$. The enzyme was quickly inactivated above $55^{\circ}C$, and showed a maximum activity at pH 8.5 and over 90% stability between a pH of 6 to 10. The putative N-terminal amino acid sequence of AIR-5 amylase, ATINNGTLMQYFEWYVPNDG, showed a 96% sequence similarity with that of BLA, a general liquefying amylase.

Keywords

References

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