Cereals & Grains Association
Log In

Physicochemical Properties of Rice Endosperm Proteins Extracted by Chemical and Enzymatic Methods

November 2006 Volume 83 Number 6
Pages 663 — 667
Ilankovan Paraman , 1 N. S. Hettiarachchy , 1 , 2 Christian Schaefer , 3 and Markus I. Beck 3

Dept. Food Science, University of Arkansas, 2650 N. Young Avenue, Fayetteville, AR 72704. Corresponding author. Phone: 479-575-4779. Fax: 479-575-6936. E-mail: nhettiar@uark.edu DSM Nutritional Products Ltd, Dept. NRD/CF-Nutrition Research and Development/Center Formulation, PO Box 3255, 4002 Basel, Switzerland.


Go to Article:
Accepted July 27, 2006.
ABSTRACT

Rice proteins are nutritional, hypoallergenic, and healthy for human consumption. Efficient extraction with approved food-grade enzymes and chemicals are essential for commercial production and application of rice protein as a functional ingredient. Rice endosperm proteins were isolated by alkali, salt, and enzymatic methods and evaluated for extractability and physicochemical properties. Alkali (RPA) and salt (RPS) methods extracted 86.9 and 87.3% of proteins with 65.9 and 58.9% yield, respectively. The enzymatic methods with Termamyl (RPET) and amylase S (RPEA) extracted 85.8 and 81.0% proteins with 85.2 and 86.2% yield, respectively. Enthalpy values of RPA (1.79 J/g), RPS (1.22 J/g), RPET (nondetectable), and RPEA (0.17 J/g), determined by differential scanning calorimetry, demonstrated that the varying level of denaturation of proteins depends on the method of extraction. Surface hydrophobicity data supported this observation. Alkali- and salt-extracted proteins had higher solubility and emulsifying properties than those of enzyme-extracted proteins. Comparatively, more favorable protein composition, lower surface hydrophobicity, higher solubility, and a lower degree of thermal denaturation of alkali- and salt-extracted proteins contributed to higher emulsifying and foaming properties than those of enzyme-extracted proteins; therefore, alkali- and salt-extracted proteins can have enhanced functional use and a potential starting material for preparing tailored rice protein isolates.



© 2006 AACC International, Inc.