A New Protein of α-Amylase Activity from Lactococcus lactis

被引：11
|
作者：
Wasko, Adam [1 ]
Polak-Berecka, Magdalena [1 ]
Targonski, Zdzislaw [1 ]
机构：
[1] Univ Life Sci Lublin, Dept Biotechnol Human Nutr & Food Commod, PL-20704 Lublin, Poland
来源：
JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY | 2010年 / 20卷 / 09期
关键词：
alpha-Amylase; ALAB; Lactococcus lactis; gene transfer; evolutionary origin; LACTOBACILLUS-AMYLOVORUS; SP; NOV; PURIFICATION; STARCH; STRAINS; PLANTARUM; FERMENTUM; SEQUENCE; GENES;
D O I：
10.4014/jmb.1002.02005
中图分类号：
Q81 [生物工程学（生物技术）]; Q93 [微生物学];
学科分类号：
071005 ; 0836 ; 090102 ; 100705 ;
摘要：
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).
引用
收藏
页码：1307 / 1313
页数：7
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