Article (Scientific journals)
Airewater interfacial properties of enzymatic wheat gluten hydrolyzates determine their foaming behavior
Wouters, Arno G.B.; Rombouts, Ine; Legein, Marie et al.
2016In Food Hydrocolloids, 55, p. 155-162
Peer Reviewed verified by ORBi
 

Files


Full Text
Air-water interfacial properties of enzymatic .pdf
Publisher postprint (988.8 kB)
Request a copy

All documents in ORBi are protected by a user license.

Send to



Details



Keywords :
Gluten hydrolyzates; Protein foam, Languir isotherm; Adsorption kinetics; Protein concentration; Air-water interface
Abstract :
[en] Insight in the link between foaming and interfacial properties of proteins can increase their potential as functional agents in food systems. Here, foaming capacity and stability of structurally different peptic and tryptic wheat gluten hydrolyzates were related to the kinetics of their adsorption at an airewater interface as well as to the properties of a compressed protein film at this interface. Foams from degree of hydrolysis (DH, i.e. the percentage of cleaved peptide bonds) 2 hydrolyzates were more stable than those from their DH 6 counterparts, and this at all protein concentrations tested. However, at protein concentrations from 0.010% to 0.050% (wprot/v), peptic DH 2 and 6 hydrolyzates had better foaming stability than their tryptic counterparts of the same DH. The opposite was observed when protein concentrations ranged from 0.050% to 0.150% (wprot/v). These observations can in part be explained by the molecular mass composition of the samples and, more importantly, by high levels of hydrophobic peptides in the DH 2 samples. The calculation of an average elasticity (up to 20e25 mN/m) from the variation in surface pressure for a variation in surface area in Langmuir isotherms showed that DH 2 samples had higher elasticity than DH 6 samples, which was in agreement with their foaming stabilities at various protein concentrations. Additionally, although not usually considered in literature, it seemed there was a correspondence between surface pressure at different protein surface concentrations and foaming stability at different protein concentrations.
Disciplines :
Food science
Author, co-author :
Wouters, Arno G.B.
Rombouts, Ine
Legein, Marie
Fierens, Ellen
Brijs, Kristof
Blecker, Christophe ;  Université de Liège > Agronomie, Bio-ingénierie et Chimie (AgroBioChem) > Science des alim. et formul.
Language :
English
Title :
Airewater interfacial properties of enzymatic wheat gluten hydrolyzates determine their foaming behavior
Publication date :
2016
Journal title :
Food Hydrocolloids
ISSN :
0268-005X
eISSN :
1873-7137
Publisher :
Elsevier Science
Volume :
55
Pages :
155-162
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 07 January 2016

Statistics


Number of views
73 (6 by ULiège)
Number of downloads
0 (0 by ULiège)

Scopus citations®
 
46
Scopus citations®
without self-citations
27
OpenCitations
 
34

Bibliography


Similar publications



Contact ORBi