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image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Journal of the Scien...arrow_drop_down
image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
Journal of the Science of Food and Agriculture
Article . 2010 . Peer-reviewed
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Emulsifying properties of the transglutaminase‐treated crosslinked product between peanut protein and fish (Decapterus maruadsi) protein hydrolysates

Authors: Xiao, Hu; Jiaoyan, Ren; Mouming, Zhao; Chun, Cui; Pengchen, He;

Emulsifying properties of the transglutaminase‐treated crosslinked product between peanut protein and fish (Decapterus maruadsi) protein hydrolysates

Abstract

AbstractBACKGROUND: Defatted peanut meal, a protein‐rich by‐product from the oil extraction industry, is underutilised owing to its inferior functional properties. In this study, transglutaminase (TGase) crosslinking and proteolysis were used to improve the emulsifying properties of peanut protein isolate (PPI) extracted from the meal. PPI and PPI hydrolysate (PPIH) were conjugated separately with fish (Decapterus maruadsi) protein hydrolysate (DPH), catalysed by TGase to obtain improvements in the emulsifying properties.RESULTS: Analyses by electrophoresis and high‐performance liquid chromatography indicated that polymers were formed in all TGase‐treated samples. In emulsions of PPIH, PPI‐DPH and PPIH‐DPH the volume/surface average particle diameter (d32), creaming and instability phenomenon were decreased and the zeta‐potential was increased after TGase treatment, showing improved emulsifying activity and emulsion stability. In the case of PPI, TGase treatment had no effect on the emulsifying activity, but the emulsion stability of TGase‐treated PPI was improved.CONCLUSION: The study showed that TGase crosslinking and proteolysis could improve the emulsifying properties of PPI, while proteolysis followed by TGase crosslinking proved more efficient. The emulsifying properties of the heterologous protein systems of PPI‐DPH and PPIH‐DPH were also improved by TGase treatment. Copyright © 2010 Society of Chemical Industry

Related Organizations
Keywords

Fish Proteins, Transglutaminases, Arachis, Polymers, Protein Hydrolysates, Hydrolysis, Fishes, Protein Prenylation, Cross-Linking Reagents, Emulsifying Agents, Seeds, Animals, Emulsions, Particle Size, Plant Proteins

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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
36
Top 10%
Top 10%
Average
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