Affordable Access

Publisher Website

Effect of high-pressure treatment onin-vitrodigestibility of β-lactoglobulin

Authors
Journal
Innovative Food Science & Emerging Technologies
1466-8564
Publisher
Elsevier
Publication Date
Volume
9
Issue
1
Identifiers
DOI: 10.1016/j.ifset.2007.05.004
Keywords
  • β-Lactoglobulin
  • High-Pressure
  • In-Vitropepsin Digestion
  • Proteolysis
Disciplines
  • Biology
  • Medicine

Abstract

Abstract The effect of high-pressure (HP)-treatment on β-lactoglobulin (β-Lg) was investigated using in-vitro pepsin digestion under simulated gastric conditions. HP-treatment of β-Lg at 400 MPa for 10 min only slightly increased its subsequent hydrolysis by pepsin. However, higher pressure treatments (600 and 800 MPa) resulted in rapid digestion of β-Lg. After these higher pressure treatments, β-Lg disappeared in less than 1 min of pepsin incubation as determined by SDS-PAGE analysis. Mass spectrometry analysis of the digestion products at corresponding incubation times revealed rapid and progressive degradation of β-Lg. Most (> 90%) of the peptide products following pepsin digestion of HP-treated β-Lg were less than 1500 Da in size. Peptide products from pepsin digestion were identified and mapped to β-strand regions (Leu 32–Leu 54 and Phe 82–Leu 104) and to the N- and C-terminals regions (Leu 1–Leu 10 and Ser 150–Leu 156) of β-Lg. While these regions corresponded to known IgE epitopes of β-Lg, the predominant peptides resulting from 60 s of incubation were short (7–10 residues) in length. These results demonstrate that HP-treatment increased the digestibility of β-Lg and represents a promising processing technology for reducing the allergenicity of known allergens in a wide variety of food materials. Industrial relevance High-pressure treatment is widely used to enhance the functional attributes of food proteins. The potential for enhanced nutritional value of β-Lg was also demonstrated here by its increased digestibility. High-pressure treatment followed by incubation with proteases may represent a method for the commercial production of bioactive peptides such as inhibitors of angiotensin converting enzyme. More importantly, high-pressure-induced unfolding of milk proteins may reduce their allergenicity. Unfolded proteins are less likely to become agents of immunological sensitization because they are more readily hydrolyzed. Thus high-pressure treatment applied to food ingredients such as whey protein isolate may contribute to the development of hypoallergenic foods.

There are no comments yet on this publication. Be the first to share your thoughts.