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Título: | Diversity of amino acid converting enzymes in wild lactic acid bacteria |
Autor: | Fernández de Palencia, P. CSIC; Plaza, M., de la; Amárita, F.; Requena, Teresa CSIC ORCID ; Peláez, Carmen CSIC ORCID | Palabras clave: | Lactic acid bacteria Wild strains Amino acid catabolism |
Fecha de publicación: | 2006 | Editor: | Elsevier | Citación: | Enzyme and Microbial Technology 38: 88- 93 (2006) | Resumen: | A total of 156 lactic acid bacteria isolates belonging to the genera Lactococcus, Lactobacillus and Leuconostoc were analysed for the amino acid converting enzymes aminotransferases, glutamate dehydrogenase, and α-ketoisovalerate decarboxylase. All isolates showed aminotransferase activity towards phenylalanine (substrate for the aromatic aminotransferase AraT) and isoleucine (substrate for the branched-chain aminotransferase BcaT). Although there was a high variability inter- and intra-species, the lactococcal strains showed the highest values for both aminotransferase activities. Moreover, α-ketoisovalerate decarboxylase (Kivd) activity was only found in lactococcal isolates, although at low relative numbers (16%). On the other hand, glutamate dehydrogenase (Gdh) activity values were highest in facultative heterofermentative lactobacilli (FHL) and the activity was found at high relative numbers (50%) in leuconostocs. Results showed a high variability in amino acid convertase activities within the wild LAB isolates assayed, therefore the utilisation in the dairy industry of new strains with high flavour-forming abilities could be a powerful tool to enhance cheese aroma development. © 2005 Elsevier Inc. All rights reserved. | URI: | http://hdl.handle.net/10261/134011 | DOI: | 10.1016/j.enzmictec.2005.04.018 | Identificadores: | doi: 10.1016/j.enzmictec.2005.04.018 issn: 0141-0229 |
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