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Diversity of amino acid converting enzymes in wild lactic acid bacteria

AuthorsFernández de Palencia, P. ; Plaza, M., de la; Amárita, F.; Requena, Teresa ; Peláez, Carmen
KeywordsLactic acid bacteria
Wild strains
Amino acid catabolism
Issue Date2006
CitationEnzyme and Microbial Technology 38: 88- 93 (2006)
AbstractA 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.
Identifiersdoi: 10.1016/j.enzmictec.2005.04.018
issn: 0141-0229
Appears in Collections:(IF) Artículos
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