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Researchers from the UGR use a bacterium to obtain biopreservatives from food

egies to compete for nutrients in their environment. One of these strategies is to produce antimicrobial compounds such as antibiotics, certain metabolism products, lytic agents, numerous types of protein exotoxins, and bacteriocins. It has become increasingly more necessary to find new antimicrobial agents because of the stronger resistance acquired by bacteria. Researcher Sánchez Hidalgo points out that natural antimicrobial cationic peptides such as bacteriocins "represent a good alternative."

Bacteriocins are proteins that are biologically active against members of the same species or species closely related to the producing bacterium. Some noteworthy bacteriocins those produced by lactic-acid bacteria (LAB), as they have been used to prepare fermented food, improve quality, and extend the average duration of many foods for centuries.

The work presented in the doctoral thesis approaches the molecular aspects of the permeabilization that AS-48 exerts on bacterial membranes. "We designed a strategy to carry out site-directed mutagenesis on the as-48A gene, the one which generates enterocin AS-48", the researcher from Granada pointed out, "and we have studied the role of seven amino acids that could be involved in biological activity and in the hydrophobic nature and thermodynamic stability of the molecule. We made this study by changing the amino acids into others with different properties."

The results of this work made it possible to conclude that while some of the mutated amino acids are essential for biological activity, others improve AS-48 biotechnological characteristics. During the process of obtaining mutated amino acids, it was also determined that three out of the ten genes involved in the production of AS-48 express themselves together. The research also determined the way of that these genes are regulated and expressed as well.


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Source:Universidad de Granada


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