Purification and properties of a maltotetraose- and maltotriose-producing amylase from Chloroflexus aurantiacus

K. Ratanakhanokchai, J. Kaneko, Y. Kamio, K. Izaki

研究成果: Article査読

35 被引用数 (Scopus)

抄録

A maltotetraose- and maltotriose-producing amylase which is stable at alkaline pHs and high temperatures was detected in the culture filtrate of a strain of Chloroflexus aurantiacus J-10-F1, a thermophilic, green, photosynthetic bacterium. The enzyme was purified to homogeneity, as demonstrated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, by means of ultrafiltration, ammonium sulfate fractionation, and DEAE-cellulose, hydroxyapatite, and high-performance liquid chromatographies. The molecular mass of the purified enzyme was estimated to be about 210,000 Da. The isoelectric point of the enzyme was estimated to be 6.24 by polyacrylamide gel electrofocusing. The amylase was stable up to 55°C and at alkaline pHs of up to 12.0. The optimum pH and temperature of the enzyme activity were 7.5 and 71°C, respectively. Metal ions such as Hg2+, Zn2+, Cu2+, Mn2+, and Ni2+ strongly inhibited the enzyme activity. The enzyme activity was reactivated specifically by Ca2+ after the enzyme was treated with 1 mM EDTA. This enzyme could digest various kinds of raw-starch granules from corn, cassava, and potato. Both maltotetraose and maltotriose were formed as the main enzymatic products from soluble starch.

本文言語English
ページ(範囲)2490-2494
ページ数5
ジャーナルApplied and environmental microbiology
58
8
DOI
出版ステータスPublished - 1992

ASJC Scopus subject areas

  • バイオテクノロジー
  • 食品科学
  • 応用微生物学とバイオテクノロジー
  • 生態学

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