Evento

Ability of thermophilic lactobacilli to hydrolyze food animal and vegetable proteins

Pescuma, Micaela Icon; Espeche Turbay, Maria Beatriz Icon; Vignolo, Graciela Margarita Icon; Mozzi, Fernanda Beatriz Icon; Font, Graciela Maria Icon; Savoy, Graciela Icon; Hebert, Elvira Maria Icon

Otros responsables

Fecha

2012

Editorial

Nobel Akademik Yayıncılık

Revista

Título del libro

Nombre del evento

23rd International Committee on Food Microbiology and Hygiene Symposium

Fecha del evento

2012-09-03

Institución organizadora

Istambul Technical University
International Committee on Food Microbiology and Hygiene

ISSN

eISSN

ISBN

978-975-561-423-6

Idioma

Inglés

Tipo del evento

Simposio

Clasificación temática

Resumen

The cell envelope-associated proteinase (CEP) of lactobacilli has a key role for bacterial nutrition and contributes to the development of the organoleptic properties of fermented milk and vegetable products; moreover, it can release bioactive health-beneficial peptides from milk proteins and diminish allergic reactions. The aim of this study was to compare the ability of industrially relevant species of thermophilic lactobacilli strains to hydrolyze proteins from animal (caseins and β-lactoglobulin) and vegetable (soybean and wheat) sources. In addition, the influence of the peptide content in the growth medium on the CEP activity was evaluated. Lactobacillus delbrueckii subsp. lactis (CRL 581 and 654), L. delbrueckii subsp. bulgaricus (CRL 454 and 656), L. acidophilus (CRL636 and 1063) and L. helveticus (CRL 1062 and 1177) were grown in a chemically defined medium supplemented or not with casitone (1%). Protein hydrolysis was evaluated by SDS-PAGE and RP-HPLC. Proteinase production was inhibited by the presence of casitone in different extent and was Lactobacillus species-dependent; the L. delbrueckii subsp. lactis species was the most affected (97-99% inhibition) while L. acidophilus the least influenced one (33-50% inhibition). All strains hydrolyzed mainly β-casein while the degradation of α-casein was strain-dependent. Contrariwise, -Casein was poorly degraded by the studied strains. L. delbrueckii subsp. bulgaricus CRL 656, L. acidophilus CRL 636 and L. helveticus CRL 1062 were able to hydrolyze the major milk allergenic protein β-lactoglobulin while L. delbrueckii subsp. lactis strains, L. delbrueckii subsp. bulgaricus CRL 656 and L. helveticus CRL 1177 degraded the gliadin cereal protein in a higher extent. Respect to soy proteins, the L. acidophilus and L. helveticus strains showed the lowest proteolytic ability. This study deepens into the understanding of the proteolytic diversity of lactic acid bacteria for exploiting this complex system in the manufacture of novel functional foods. The rational selection of proper strains when formulating hydrolyzed food products of different origin (dairy or vegetable) is of utmost importance since proteinases specificities are strain-dependent.

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