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A thermophilic alkalophilic α-amylase from Bacillus sp. AAH-31 shows a novel domain organization among glycoside hydrolase family 13 enzymes.

Bioscience, biotechnology, and biochemistry - 1 Jan 2013

Saburi Wataru, Morimoto Naoki, Mukai Atsushi, Kim Dae Hoon, Takehana Toshihiko, Koike Seiji, Matsui Hirokazu, Mori Haruhide

Abstract excerpt

α-Amylases (EC 3.2.1.1) hydrolyze internal α-1,4-glucosidic linkages of starch and related glucans. Bacillus sp. AAH-31 produces an alkalophilic thermophilic α-amylase (AmyL) of higher molecular mass, 91 kDa, than typical bacterial α-amylases. In this study, the AmyL gene was cloned to determine its primary structure, and the recombinant enzyme, produced in Escherichia coli, was characterized. AmyL shows no...

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PMID: 24018662
DOI: 10.1271/bbb.130284

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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