Format

Send to

Choose Destination
J Dairy Sci. 2016 Jul;99(7):5144-5154. doi: 10.3168/jds.2016-11036. Epub 2016 May 11.

Proteolytic activity of Enterococcus faecalis VB63F for reduction of allergenicity of bovine milk proteins.

Author information

1
Food Research Center, Department of Food and Experimental Nutrition, Faculty of Pharmaceutical Sciences, University of São Paulo, 580, Professor Lineu Prestes, 13 B, Sao Paulo, SP, 05508-000, Brazil. Electronic address: vbiscola@usp.br.
2
Department of Food Engineering, Faculty of Animal Sciences and Food Engineering, University of São Paulo, 225, Duque de Caxias Norte, Avenue, Pirassununga, SP, 13635-900, Brazil.
3
UR 1268 Biopolymères Interactions Assemblages, INRA, Protein Functions and Interactions Research Team, B.P. 71627, 44316, Nantes Cedex 03, France.
4
Department of General and Applied Microbiology, Faculty of Biology, Sofia University "St. Kliment Ohridski," Dragan Tzankov Blvd 8, 1164 Sofia, Bulgaria.
5
Food Research Center, Department of Food and Experimental Nutrition, Faculty of Pharmaceutical Sciences, University of São Paulo, 580, Professor Lineu Prestes, 13 B, Sao Paulo, SP, 05508-000, Brazil.
6
UR 1268 Biopolymères Interactions Assemblages, INRA, Protein Functions and Interactions Research Team, B.P. 71627, 44316, Nantes Cedex 03, France; Department of Animal Nutrition and Feed Management, Poznan University of Life Sciences, ul. Wołyńska 33, 60-637 Poznan, Poland.

Abstract

With the aim of screening proteolytic strains of lactic acid bacteria to evaluate their potential for the reduction of allergenicity of the major bovine milk proteins, we isolated a new proteolytic strain of Enterococcus faecalis (Ent. faecalis VB63F) from raw bovine milk. The proteases produced by this strain had strong activity against caseins (αS1-, αS2-, and β-casein), in both skim milk and sodium caseinate. However, only partial hydrolysis of whey proteins was observed. Proteolysis of Na-caseinate and whey proteins, observed after sodium dodecyl sulfate-PAGE, was confirmed by analysis of peptide profiles by reversed-phase HPLC. Inhibition of proteolysis with EDTA indicated that the proteases produced by Ent. faecalis VB63F belonged to the group of metalloproteases. The optimal conditions for their activity were 42°C and pH 6.5. The majority of assessed virulence genes were absent in Ent. faecalis VB63F. The obtained results suggest that Ent. faecalis VB63F could be efficient in reducing the immunoreactivity of bovine milk proteins.

KEYWORDS:

casein; milk allergy; protein hydrolysis; whey protein

PMID:
27179865
DOI:
10.3168/jds.2016-11036
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center