Isolation, purification, and amino acid sequence of lactobin A, one of the two bacteriocins produced by Lactobacillus amylovorus LMG P-13139

Article Abstract:

Lactobacillus amylovorus LMG P-13139 produces a 4.5 kDa bacteriocin, lactobin A, that is a heat stable, non-lanthionine-containing membrane-active peptide. It belongs to the class IIb bacteriocins. The peptide's N-terminal contains 50 amino acids. The bacteriocin consists of 26% glycine residues and 40% hydrophobic residues. It shows structural homology with the lafX gene product. A hydrophobic membrane-integrated stretch extends from residues 24 to 45, and the extreme N- and C-terminals of lactobin A have a hydrophilic nature.

Bacterial proteins, Amino acid sequence, Amino acid sequencing

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Starch-binding domain affects catalysis in two Lactobacillus alpha-amylases

Article Abstract:

A kinetic study of Lactobacillus plantarum and Lactobacillus amylovorus alpha-amylases acting on starch in both granular and soluble forms is reported and their adsorption capacities to consider the implications of a soluble enzyme acting upon a solid substrate is studied. The amylases produced by both lactobacilli were purified from the supernatant by affinity chromatography on beta-cyclodextrin-Sepharose.

Organizational history, Genetic aspects, Company restructuring/company reorganization, Reorganization and restructuring, Catalysis, Company organization, Lactobacillus plantarum, Affinity chromatography

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Comparative characterization of complete and truncated forms of Lactobacillus amylovorus alpha-amylase and role of the C-terminal direct repeats in raw-starch binding

Article Abstract:

The 66-kDa carboxyl-terminal direct-repeating-unit region of alpha amylase from Lactobacillus amylovorus is necessary for binding and hydrolyzing raw starch. A

Amylases, Industrial microbiology

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