Articolo in rivista, 2007, ENG, 10.1016/j.ijfoodmicro.2006.10.026
Zotta, Teresa; Ricciardi, Annamaria; Parente, Eugenio
Universita degli Studi della Basilicata
Forty-one strains of lactic acid bacteria (LAB) isolated from Cornetto di Matera sourdoughs were screened for their enzymatic activities, to elucidate their possible roles during the fermentation process. Urease, peptidase, phytase, phosphatase and ?-glucosidase activities were measured spectrophotometrically using synthetic substrates. Proteolytic activities were examined in model doughs, using neutral and acidified sterile doughs as controls. All strains had low urease, glutamyl aminopeptidase and iminopeptidase activities, whereas differences within species were observed for the other enzymatic activities. Leuconostoc mesenteroides and Lactobacillus curvatus strains generally showed high aminopeptidase, X-prolyl dipeptidyl aminopeptidase, ?-glucosidase and phytase activities, while the enzymatic activities of Lactobacillus plantarum, Lactobacillus pentosus and Weissella cibaria varied between strains. In order to classify the strains on the basis of similar enzymatic profiles, a hierarchical cluster analysis was carried out. Several strains of L. plantarum, L. curvatus and Leuc. mesenteroides showed an interesting combination of proteolytic, peptidase, ?-glucosidase and phytase activities, suggesting their possible usefulness as a mixed starter culture in bread-making processes. © 2006 Elsevier B.V. All rights reserved.
International journal of food microbiology 115 (2), pp. 165–172
?-glucosidase, Lactic acid bacteria, Phytase, Proteolysis, Sourdoughs, Urease
ID: 310982
Year: 2007
Type: Articolo in rivista
Creation: 2015-02-17 16:10:33.000
Last update: 2016-03-07 12:14:45.000
CNR authors
External links
OAI-PMH: Dublin Core
OAI-PMH: Mods
OAI-PMH: RDF
DOI: 10.1016/j.ijfoodmicro.2006.10.026
URL: http://www.scopus.com/record/display.url?eid=2-s2.0-33847660504&origin=inward
External IDs
CNR OAI-PMH: oai:it.cnr:prodotti:310982
DOI: 10.1016/j.ijfoodmicro.2006.10.026
Scopus: 2-s2.0-33847660504