Effect of high-pressure treatment on in-vitro digestibility of β-lactoglobulin

Michael G Zeece, Thom Huppertz, Alan Kelly

Research output: Contribution to journalArticle

79 Citations (Scopus)

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 (Leu32-Leu54 and Phe82-Leu104) and to the N- and C-terminals regions (Leu1-Leu10 and Ser150-Leu156) 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.

Original languageEnglish (US)
Pages (from-to)62-69
Number of pages8
JournalInnovative Food Science and Emerging Technologies
Volume9
Issue number1
DOIs
StatePublished - Jan 1 2008

Fingerprint

lactoglobulins
Lactoglobulins
in vitro digestibility
high pressure treatment
pepsin
Pressure
Pepsin A
digestion
Digestion
Peptides
peptides
allergenicity
Proteins
Food
digestibility
whey protein isolate
In Vitro Techniques
milk proteins
Allergens
Epitopes

Keywords

  • High-pressure
  • In-vitro pepsin digestion
  • Proteolysis
  • β-Lactoglobulin

ASJC Scopus subject areas

  • Food Science
  • Chemistry(all)
  • Industrial and Manufacturing Engineering

Cite this

Effect of high-pressure treatment on in-vitro digestibility of β-lactoglobulin. / Zeece, Michael G; Huppertz, Thom; Kelly, Alan.

In: Innovative Food Science and Emerging Technologies, Vol. 9, No. 1, 01.01.2008, p. 62-69.

Research output: Contribution to journalArticle

Zeece, Michael G ; Huppertz, Thom ; Kelly, Alan. / Effect of high-pressure treatment on in-vitro digestibility of β-lactoglobulin. In: Innovative Food Science and Emerging Technologies. 2008 ; Vol. 9, No. 1. pp. 62-69.
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