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KMID : 0545120100200091307
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Journal of Microbiology and Biotechnology
2010 Volume.20 No. 9 p.1307 ~ p.1313
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A new protein of α-amylase activity from Lactococcus lactis.
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Adam Wasko
Magdalena Polak-Berecka
Zdzislaw Targonski
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Abstract
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An extracellular α-amylase from Lactococcus lactis IBB500 was purified and characterized. The optimum conditions for the enzyme activity were pH 4.5, temperature of 35°C, enzyme molecular mass of 121 kDa. The genome analysis and a plasmid curing experiment indicated that amy+ genes were located in a plasmid of 30 kb. An analysis of phylogenetic relationships strongly supported a hypothesis of horizontal gene transfer. A strong homology was found for the peptides with the sequence of α-amylases from Ralstonia pikettii and Ralstonia solanacearum. The protein of α-amylase activity purified in this study is the first one described for the Lactococcus lactis species, and this paper is the first report on Lactococcus lactis strain as a microorganism belonging to amylolytic lactic acid bacteria (ALAB).
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KEYWORD
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α-amylase, ALAB, Lactococcus lactis, gene transfer, evolutionary origin
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