PURIFICATION AND AMINO-ACID-SEQUENCE OF SAKACIN-A, A BACTERIOCIN FROM LACTOBACILLUS-SAKE LB706

被引：166

作者：

HOLCK, A ^{[1
]}

AXELSSON, L ^{[1
]}

BIRKELAND, SE ^{[1
]}

AUKRUST, T ^{[1
]}

BLOM, H ^{[1
]}

机构：

[1] NORWEGIAN DAIRIES ASS, N-0133 OSLO, NORWAY

来源：

JOURNAL OF GENERAL MICROBIOLOGY | 1992年 / 138卷

关键词：

D O I：

10.1099/00221287-138-12-2715

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Sakacin A, a bacteriocin produced by Lactobacillus sake Lb706 and which inhibits the growth of Listeria monocytogenes, was purified to homogeneity by ammonium sulphate precipitation and ion-exchange, hydrophobic-interaction and reversed-phase chromatography. The complete amino acid sequence of sakacin A was determined by Edman degradation. The bacteriocin consisted of 41 amino acid residues and had a calculated M(r) of 4308.7, which is in good agreement with the value determined by mass spectrometry. The structural gene encoding sakacin A (sakA) was cloned and sequenced. The gene encoded a primary translation product of 59 amino acid residues which was cleaved between amino acids 18 and 19 to yield the active sakacin A. Sakacin A shared some sequence similarities with other bacteriocins.

引用

页码：2715 / 2720

页数：6

共 29 条

[1] IDENTIFICATION AND CLONING OF A PLASMID-ENCODED ERYTHROMYCIN RESISTANCE DETERMINANT FROM LACTOBACILLUS-REUTERI [J].