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231224s2014 xx |||||o 00| ||eng c |
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|a 10.1021/la503606c
|2 doi
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|a pubmed24n0810.xml
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|a (DE-627)NLM243197276
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|a (NLM)25360639
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|a DE-627
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|c DE-627
|e rakwb
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| 041 |
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|a eng
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| 100 |
1 |
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|a Munialo, Claire D
|e verfasserin
|4 aut
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| 245 |
1 |
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|a Modification of ovalbumin with fructooligosaccharides
|b consequences for network morphology and mechanical deformation responses
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| 264 |
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|c 2014
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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| 338 |
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 05.10.2015
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|a Date Revised 26.11.2014
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a The Maillardation of proteins has been used as a natural alternative to improve its functionality by covalent coupling of proteins with saccharides. However, the impact of Maillard reaction on the structural aspects of protein networks and, as a consequence, the mechanical breakdown properties of the gel networks has not been reported. The objective of this study was to evaluate how the attachment of linear oligo-sugar moieties onto ovalbumin affects its aggregation, network morphology, and consequently the mechanical deformation properties including the ability of the networks to elastically store energy in this material. To potentially alter the morphology of the network structure, ovalbumin was modified by conjugating some of its amino groups with fructooligosaccharide (FOS) moieties via the Maillard reaction. It was demonstrated that the attachment of FOS to ovalbumin does not affect the integrity of the secondary and tertiary structure as characterized using circular dichroism and tryptophan fluorescence. Differences in the network morphology were observed by scanning electron microscopy for FOS-modified ovalbumin variants. Upon increased modification, the microstructure of the gels had more and larger pores and had thinner strands than nonmodified variants. Evaluation of the large deformation properties of the gels demonstrated that FOS-modified gels were less strong and less brittle and showed lower stiffness than nonmodified variants. The recoverable energy (elastically stored energy) of gels reduced with an increase in the degree of modification. The results show that the attachment of FOS to ovalbumin alters the structural and mechanical (large) breakdown properties of the protein gels. The consequences of the alteration of the network structure and large deformation properties of FOS-modified ovalbumin offer opportunities to efficiently design food materials with desirable techno-functional applications
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|a Journal Article
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|a Oligosaccharides
|2 NLM
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|a Protein Aggregates
|2 NLM
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| 650 |
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|a fructooligosaccharide
|2 NLM
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| 650 |
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|a Ovalbumin
|2 NLM
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| 650 |
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7 |
|a 9006-59-1
|2 NLM
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| 700 |
1 |
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|a Ortega, Rodrigo G
|e verfasserin
|4 aut
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| 700 |
1 |
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|a van der Linden, Erik
|e verfasserin
|4 aut
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| 700 |
1 |
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|a de Jongh, Harmen H J
|e verfasserin
|4 aut
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| 773 |
0 |
8 |
|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 30(2014), 46 vom: 25. Nov., Seite 14062-72
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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| 773 |
1 |
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|g volume:30
|g year:2014
|g number:46
|g day:25
|g month:11
|g pages:14062-72
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| 856 |
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|u http://dx.doi.org/10.1021/la503606c
|3 Volltext
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