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dc.contributor.author | Fernández de Palencia, P. | - |
dc.contributor.author | Plaza, M., de la | - |
dc.contributor.author | Amárita, F. | - |
dc.contributor.author | Requena, Teresa | - |
dc.contributor.author | Peláez, Carmen | - |
dc.date.accessioned | 2016-06-24T06:23:42Z | - |
dc.date.available | 2016-06-24T06:23:42Z | - |
dc.date.issued | 2006 | - |
dc.identifier | doi: 10.1016/j.enzmictec.2005.04.018 | - |
dc.identifier | issn: 0141-0229 | - |
dc.identifier.citation | Enzyme and Microbial Technology 38: 88- 93 (2006) | - |
dc.identifier.uri | http://hdl.handle.net/10261/134011 | - |
dc.description.abstract | 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. | - |
dc.description.sponsorship | This work was performed under the auspices of the Consejo Superior de Investigaciones Científicas and was supported by Research Project AGL2002-03277 | - |
dc.publisher | Elsevier | - |
dc.rights | closedAccess | - |
dc.subject | Lactic acid bacteria | - |
dc.subject | Wild strains | - |
dc.subject | Amino acid catabolism | - |
dc.title | Diversity of amino acid converting enzymes in wild lactic acid bacteria | - |
dc.type | artículo | - |
dc.identifier.doi | 10.1016/j.enzmictec.2005.04.018 | - |
dc.date.updated | 2016-06-24T06:23:42Z | - |
dc.description.version | Peer Reviewed | - |
dc.language.rfc3066 | eng | - |
dc.contributor.funder | Consejo Superior de Investigaciones Científicas (España) | - |
dc.relation.csic | Sí | - |
dc.identifier.funder | http://dx.doi.org/10.13039/501100003339 | es_ES |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.fulltext | No Fulltext | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.cerifentitytype | Publications | - |
item.openairetype | artículo | - |
item.grantfulltext | none | - |
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