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KMID : 0545120010110040636
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Journal of Microbiology and Biotechnology
2001 Volume.11 No. 4 p.636 ~ p.643
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Production of Maltopentaose and Biochemical Characterization of Maltopentaose-Forming Amylase
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KIM, YOUNG-MIN
RUY, HWA-JA/LEE, SUN-OK/SEO, EUN-SEONG/LEE, SO-YOUNG/YOO, SUM-KYUN/CHO, DONG-LYUN
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Abstract
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Bacillus sp. AIR-5, a strain from soil, produced an extracellular maltohentaose-forming amylase from amylose and soluble starch. This bacterium produced 8.9g/l of maltopentaose from 40g/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 30K 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 250kDa. 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℃. The enzyme was quickly inactivated above 55℃, 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.
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