INVESTIGADORES
MOZZI Fernanda Beatriz
congresos y reuniones científicas
Título:
Lactic acid bacteria with potential to reduce the allergenic content of whey beta-lactoglobulin
Autor/es:
M. PESCUMA; M. DALGALARRONDO; E. M. HÉBERT; F. MOZZI; J.M. CHOBERT; G FONT DE VALDEZ
Reunión:
Simposio; 9th Symposium on Lactic Acid Bacteria; 2008
Resumen:
Whey, a by-product of the cheese industry, is used as food ingredient in dairy products due
to its biological and functional valuable proteins. Beta-lactoglobulin (BLG) is the major whey
protein and the main elicitor of milk allergies. Recently, it has been claimed
that fermented products have lower antigenic response towards BLG than milk
itself. The aim of this work was to assess the capacity of two lactic acid
bacteria (LAB) strains to degrade BLG and to carry out the characterization and
structural analysis of the released peptides. Hydrolysis of BLG by
cell wall-associated proteinases using a non-proliferating cell system was
evaluated. The maximum hydrolysis values (52 and 48%) corresponded to Lactobacillus
acidophilus CRL 636 and L. delbrueckii subsp. bulgaricus CRL
454, respectively, after 8 h of incubation. RP-HPLC analysis showed that L.
acidophilus CRL 636 released six hydrophilic and two hydrophobic peptides
while L. delbrueckii subsp. bulgaricus CRL 454 released small
amounts of two hydrophilic and three less-hydrophilic peptides. Bands of 9.6 and 14 kDa, corresponding to BLG
degradation, were observed in SDS-PAGE. Mass spectroscopy (LC-MS/MS) analysis
revealed the presence of peptides with molecular mass in the range of 658-4119
Da. The sequence analysis of these peptides indicated that L. acidophilus
CRL 636 was able to hydrolyze the three main BLG epitopes (41-60, 102-124 and
149-162) while L. delbrueckii subsp. bulgaricus CRL 454 only degraded the
latter two releasing the complete allergenic sequence 41-60. Our results
suggest that L. acidophilus CRL 636 could be used to reduce the
allergenic content of BLG in whey-based or whey-containing foods.