Exploring the breakdown of dairy protein gels during in vitro gastric digestion using time-lapse synchrotron deep-UV fluorescence microscopy.

Abstract:

:A novel time-lapse synchrotron deep-UV microscopy methodology was developed that made use of the natural tryptophan fluorescence of proteins. It enabled the monitoring in situ of the microstructural changes of protein gels during simulated gastric digestion. Two dairy gels with an identical composition, but differing by the coagulation mode, were submitted to static in vitro gastric digestion. The kinetics of gel particle breakdown were quantified by image analysis and physico-chemical analyses of digesta. The results confirm the tendency of rennet gels, but not acid gels, to form compact protein aggregates under acidic conditions of the stomach. Consequently, the kinetics of proteolysis were much slower for the rennet gel, confirming the hypothesis of a reduced pepsin accessibility to its substrate. The particle shapes remained unchanged and the disintegration kinetics followed an exponential trend, suggesting that erosion was the predominant mechanism of the enzymatic breakdown of dairy gels in these experimental conditions.

journal_name

Food Chem

journal_title

Food chemistry

authors

Floury J,Bianchi T,Thévenot J,Dupont D,Jamme F,Lutton E,Panouillé M,Boué F,Le Feunteun S

doi

10.1016/j.foodchem.2017.07.023

subject

Has Abstract

pub_date

2018-01-15 00:00:00

pages

898-910

eissn

0308-8146

issn

1873-7072

pii

S0308-8146(17)31167-6

journal_volume

239

pub_type

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