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Extraction, denaturation and hydrophobic Properties of Rice Flour Proteins

Ju, Z.Y., Hettiarachchy, N.S., Rath, N.·2001·Journal of Food Science

Abstract

ABSTRACT: Rice proteins were extracted from defatted rice flour. Turbidity measurement of supernatants revealed isoelectric points of albumin (pH 4.1), globulin (pH 4.3 and pH 7.9), and glutelin (pH 4.8), at which they were precipitated with 82.3 to 93.2% recovery efficiency. Prolamin did not aggregate and precipitate upon pH adjustment, but was precipitated by acetone. Denaturation temperatures (73.3, 78.9, and 82.2 °C) as well as enthalpy values (2.88, 3.14, and 3.79 J/g), of albumin, globulin, and glutelin were different. Prolamin did not show any thermographic denaturation peak. Heat‐denaturation of globulin and glutelin resulted in progressive increases in their surface hydrophobicities. Measurement of surface hydrophobicity would be an effective parameter to evaluate rice protein denaturation.

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Metadata

Authors
Ju, Z. Y., Hettiarachchy, N. S., & Rath, N.
Venue
Journal of Food Science
Publisher
Wiley
Published
2001-03
Volume
66
Issue
2
Pages
229-232
ISSN
  • 0022-1147 (ISSN-L)
  • 1750-3841
OpenAlex
W2117799144
Cited by
290
References
0
FWCI
2.31
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Extraction, denaturation and hydrophobic Properties of Rice Flour Proteins. https://app.cochat.ai/papers/10.1111/j.1365-2621.2001.tb11322.x
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Ju, Z. Y., Hettiarachchy, N. S., & Rath, N. (2001). Extraction, denaturation and hydrophobic Properties of Rice Flour Proteins. Journal of Food Science. https://doi.org/10.1111/j.1365-2621.2001.tb11322.x

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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