Rheological properties of patatin gels compared with β-lactoglobulin, ovalbumin, and glycinin

BACKGROUND: The thermal unfolding and rheological properties of patatin gels were compared with those of commonly used proteins (β‐lactoglobulin, ovalbumin, glycinin). RESULTS: A significant difference between these proteins was observed in both the denaturation temperature (59 °C for patatin; about...

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Veröffentlicht in:	Journal of the science of food and agriculture 2011-01, Vol.91 (2), p.253-261
Hauptverfasser:	Creusot, Nathalie, Wierenga, Peter A, Laus, Marc C, Giuseppin, Marco LF, Gruppen, Harry
Format:	Artikel
Sprache:	eng
Schlagworte:	Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts Biological and medical sciences Carboxylic Ester Hydrolases - chemistry Elasticity Food industries Food Technology Fundamental and applied biological sciences. Psychology gelation Gels Globulins - chemistry Hydrophobic and Hydrophilic Interactions Lactoglobulins - chemistry Milk and cheese industries. Ice creams novel proteins Ovalbumin - chemistry patatin plant proteins Plant Proteins - chemistry Protein Denaturation Rheology Solanum tuberosum - chemistry Soybean Proteins - chemistry Temperature
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