Heat-Induced Gelation of Pea Legumin: Comparison with Soybean Glycinin

Gel network formation of pea legumin (8.4% on a protein basis, pH 7.6) was monitored via dynamic rheological measurements. Gelation was performed in the absence and presence of the thiol-blocking reagent N-ethylmaleimide, at different rates of heating and cooling. Overall, it was shown that pea legu...

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Bibliographic Details
Published in:	Journal of agricultural and food chemistry 2004-08, Vol.52 (16), p.5071-5078
Main Authors:	O'Kane, Francesca E, Happe, Randolph P, Vereijken, Johan M, Gruppen, Harry, van Boekel, Martinus A. J. S
Format:	Article
Language:	English
Subjects:	Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts behaviors Biological and medical sciences broad beans disulfide bonds Ethylmaleimide - pharmacology Food industries Fruit and vegetable industries functional properties Fundamental and applied biological sciences. Psychology gelation gels Gels - chemistry globulins Globulins - chemistry Glycine max - chemistry glycinin heat treatment Hot Temperature Hydrogen-Ion Concentration legumin Legumins Microscopy, Electron ovalbumin peas Pisum sativum - chemistry Plant Proteins - chemistry protein gelation rheological characterization rheological properties Rheology solubility Soybean Proteins soybeans texture vicilin
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