During hydrolysis of bovine milk caseins, cell envelope-associated proteinases (CEPs) of lactic acid bacteria (LAB) may be able to produce hydrolysates that possess immunomodulatory activity. In this study, the selection of LAB by screening for bacterial CEP genes as well as by testing the proteolytic activity on bovine milk caseins was performed. Diverse hydrolytic ability against αS1- and β-casein fractions was observed. Our experiments demonstrated that immunomodulatory activity of obtained casein hydrolysates (CHs) cannot be attributed to casein-derived bioactive peptides only and underlined the necessity to thoroughly remove bacterial components before assessing bioactivity of CHs. On this basis, this study established that 3kDa-ultrafiltered CHs, produced after digestion with proteinases of Lactobacillus acidophilus ATCC 4356 and Lactococcus lactis subsp. lactis GR5, significantly decreased the basal nuclear factor (NF)-κB activity in Caco-2 cells, demonstrating immunomodulatory activity.

Potential immunomodulatory activity of bovine casein hydrolysates produced after digestion with proteinases of lactic acid bacteria / M. Stuknytè, I. De Noni, S. Guglielmetti, M. Minuzzo, D. Mora. - In: INTERNATIONAL DAIRY JOURNAL. - ISSN 0958-6946. - 21:10(2011 Oct), pp. 763-769.

Potential immunomodulatory activity of bovine casein hydrolysates produced after digestion with proteinases of lactic acid bacteria

M. Stuknytè
Primo
;
I. De Noni
Secondo
;
S. Guglielmetti;M. Minuzzo
Penultimo
;
D. Mora
Ultimo
2011

Abstract

During hydrolysis of bovine milk caseins, cell envelope-associated proteinases (CEPs) of lactic acid bacteria (LAB) may be able to produce hydrolysates that possess immunomodulatory activity. In this study, the selection of LAB by screening for bacterial CEP genes as well as by testing the proteolytic activity on bovine milk caseins was performed. Diverse hydrolytic ability against αS1- and β-casein fractions was observed. Our experiments demonstrated that immunomodulatory activity of obtained casein hydrolysates (CHs) cannot be attributed to casein-derived bioactive peptides only and underlined the necessity to thoroughly remove bacterial components before assessing bioactivity of CHs. On this basis, this study established that 3kDa-ultrafiltered CHs, produced after digestion with proteinases of Lactobacillus acidophilus ATCC 4356 and Lactococcus lactis subsp. lactis GR5, significantly decreased the basal nuclear factor (NF)-κB activity in Caco-2 cells, demonstrating immunomodulatory activity.
envelope-associated proteinase; nf-kappa-b; lactobacillus-helveticus; streptococcus-thermophilus; bioactive peptides; genetic-characterization; dairy fermentation; milk fermentation; pharyngeal mucosa; putting microbes
Settore AGR/16 - Microbiologia Agraria
Settore AGR/15 - Scienze e Tecnologie Alimentari
Settore BIO/11 - Biologia Molecolare
Settore BIO/13 - Biologia Applicata
ott-2011
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/166775
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