A New Protein of alpha-Amylase Activity from Lactococcus lactis

作者：Wasko Adam^*; Polak Berecka Magdalena; Targonski Zdzislaw

来源：Journal of Microbiology and Biotechnology, 2010, 20(9): 1307-1313.

DOI：10.4014/jmb.1002.02005

• alpha-Amylase
• ALAB
• Lactococcus lactis
• gene transfer
• evolutionary origin

An extracellular alpha-amylase from Lactococcus lactis IBB500 was purified and characterized. The optimum conditions for the enzyme activity were a pH of 4.5, temperature of 35 degrees C, and 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 the phylogenetic relationships strongly supported a hypothesis of horizontal gene transfer. A strong homology was found for the peptides with the sequence of alpha-amylases from Ralstonia pikettii and Ralstonia solanacearum. The protein with alpha-amylase activity purified in this study is the first one described for the Lactococcus lactis species, and this paper is the first report on a Lactococcus lactis strain belonging to the amylolytic lactic acid bacteria (ALAB).

• 出版日期2010-9