PURIFICATION AND AMINO-ACID-SEQUENCE OF A BACTERIOCIN PRODUCED BY PEDIOCOCCUS-ACIDILACTICI

被引:132
作者
LOZANO, JCN
MEYER, JN
SLETTEN, K
PELAZ, C
NES, IF
机构
[1] NLVF, MICROBIAL GENE TECHNOL LAB, POST BOX 51, N-1432 AS, NORWAY
[2] CSIC, INST FRIO, MADRID 6, SPAIN
[3] UNIV OSLO, DEPT BIOCHEM, OSLO 3, NORWAY
来源
JOURNAL OF GENERAL MICROBIOLOGY | 1992年 / 138卷
关键词
D O I
10.1099/00221287-138-9-1985
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
A bacteriocin produced by Pediococcus acidilactici has been purified to homogeneity by a rapid and simple four-step purification procedure which includes ammonium sulphate precipitation, chromatography with a cation-exchanger and Octyl Sepharose, and reverse-phase chromatography. The purification resulted in an approximately 80000-fold increase in the specific activity and about a 6-fold increase in the total activity. The amino acid composition and sequencing data indicated that the bacteriocin contained 43-44 amino acid residues. The predicted M(r) and isoelectric point of the bacteriocin are about 4600 and 8.6, respectively. Comparing the amino acid sequence of this bacteriocin with the sequences of leucocin A-UAL 187, sakacin P and curvacin A (bacteriocins produced by Leuconostoc gelidum, Lactobacillus sake and Lactobacillus curvatus, respectively) revealed that all four bacteriocins had in their N-terminal region the sequence Tyr-Gly-Asn-Gly-Val-Xaa-Cys, indicating that this concensus sequence is of fundamental importance for this group of bacteriocins. The bacteriocin from P. acidilactici and sakacin P were very similar, having at least 25 common amino acid residues. The sequence similarity was greatest in the N-terminal half of the molecules - 17 of the first 19 residues were common - indicating the fundamental importance of this region. Leucocin A-UAL 187 and curvacin A had, respectively, at least 16 and 13 amino acid residues in common with the bacteriocin from P. acidilactici.
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页码:1985 / 1990
页数:6
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