Preparation and functional properties of rice bran protein isolate.
Rice bran protein isolate (RBPI) containing approximately 92.0% protein was prepared from unstabilized and defatted rice bran using phytase and xylanase. The yield of RBPI increased from 34% to 74.6% through the use of the enzymatic treatment. Nitrogen solubilities of RBPI were 53, 8, 62, 78, 82, and 80% at pHs 2.0, 4.0, 6.0, 8.0, 10.0, and 12.0, respectively. Differential scanning calorimetry showed that RBPI had denaturation temperature of 83.4 degrees C with low endotherm (0.96 J/g of protein). RBPI had similar foaming properties in comparison to egg white. But emulsifying properties of RBPI were significantly lower than those of bovine serum albumin. The result of amino acid analysis showed that RBPI had a similar profile of essential amino acid requirements for 2-5-year-old children in comparison to that of casein and soy protein isolate.
Wang
M
M
Department of Food Science, University of Arkansas, Fayetteville, 72703, USA.
Hettiarachchy
N S
NS
Qi
M
M
Burks
W
W
Siebenmorgen
T
T
D010832:6-Phytase / Q000737:chemistry; D000596:Amino Acids / Q000032:analysis; D002152:Calorimetry, Differential Scanning; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004655:Emulsions; D012275:Oryza / Q000737:chemistry*; D010940:Plant Proteins / Q000737:chemistry / Q000302:isolation & purification*; D043325:Xylan Endo-1,3-beta-Xylosidase; D014995:Xylosidases / Q000737:chemistry
D000596:Amino Acids; D004655:Emulsions; D010940:Plant Proteins; D010832:6-Phytase; D014995:Xylosidases; D043325:Xylan Endo-1,3-beta-Xylosidase