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Production and evaluation of rice br...

Landers, Patti Sue Stone.

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Production and evaluation of rice bran protein concentrate as a potential human food source.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Production and evaluation of rice bran protein concentrate as a potential human food source./
Author:	Landers, Patti Sue Stone.
Description:	145 p.
Notes:	Source: Dissertation Abstracts International, Volume: 53-08, Section: B, page: 3859.
Contained By:	Dissertation Abstracts International53-08B.
Subject:	Agriculture, Food Science and Technology. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9237325

Production and evaluation of rice bran protein concentrate as a potential human food source.
Landers, Patti Sue Stone.

Production and evaluation of rice bran protein concentrate as a potential human food source. - 145 p.

Source: Dissertation Abstracts International, Volume: 53-08, Section: B, page: 3859.

Thesis (Ph.D.)--University of Arkansas, 1992.

Three rice bran protein concentrates (RBPC) were obtained from defatted rice bran. Two of the RBPC had 45% and 57% protein content and were respectively produced by washing bran in water (WE-RBPC) or dilute alkali solution at pH 9 (AE-RBPC) and isoelectrically precipitating proteins with HCl at pH 4.5. The third RBPC of 40% protein was also obtained by alkaline extraction, but the bran slurry was centrifuged, neutralized and spray dried prior to lsoelectric precipitation. All RBPC were low in ash and fiber, but had approximately 30% nitrogen free extract. The alkali extracted RBPCs had Subjects--Topical Terms:

1017813
Agriculture, Food Science and Technology.

Production and evaluation of rice bran protein concentrate as a potential human food source.
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008 130610s1992 eng d
035 $a (UnM)AAI9237325
035 $a AAI9237325
040 $a UnM $c UnM
100 1 $a Landers, Patti Sue Stone. $3 1905833
245 1 0 $a Production and evaluation of rice bran protein concentrate as a potential human food source.
300 $a 145 p.
500 $a Source: Dissertation Abstracts International, Volume: 53-08, Section: B, page: 3859.
500 $a Major Professor: Bruce R. Hamaker.
502 $a Thesis (Ph.D.)--University of Arkansas, 1992.
520 $a Three rice bran protein concentrates (RBPC) were obtained from defatted rice bran. Two of the RBPC had 45% and 57% protein content and were respectively produced by washing bran in water (WE-RBPC) or dilute alkali solution at pH 9 (AE-RBPC) and isoelectrically precipitating proteins with HCl at pH 4.5. The third RBPC of 40% protein was also obtained by alkaline extraction, but the bran slurry was centrifuged, neutralized and spray dried prior to lsoelectric precipitation. All RBPC were low in ash and fiber, but had approximately 30% nitrogen free extract. The alkali extracted RBPCs had $< $1 % residual lipids, but the WE-RBPC had an unexpectedly high lipid content of 17%. Sonication improved protein recovery.
520 $a in vivo digestibility was 90% for WE- and AE-RBPC. No differences were found between in vitro digestibility values for RBPC which had been autoclaved when compared to unheated samples, indicating a lack of trypsin inhibitor.
520 $a Protein digestibility-corrected amino acid scores (PDCAAS) were determined. When compared to amino acid requirements established by FAO/WHO/UNU (1985) for the 2- to 5-year old child, PDCAAS for WE- and AE-RBPC were 0.96 and 0.86, respectively. Lysine was the limiting amino acid (AA) in both RBPC, and threonine content was also marginal. When compared to requirements for infants (FAO/WHO/UNU 1985) PDCAAS were 0.70 (TRP first limiting AA) for WE-RBPC and 0.77 (LYS first limiting AA) for AE-RBPC as compared to 0.60 for soy protein isolate. The RBPC might be useful if supplemented with amino acids, in combination with complimentary proteins such as from soy or in a mixed diet.
520 $a AE-RBPC, soy protein isolate (SPI) and milk were tested for relative antigenicity. Rabbit polyclonal IgG antibody titers were highest for SPI (21,845,000) followed by AE-RBPC (653,000) and milk (27,300). Western blotting showed a protein band of approximately 16,000 Da. from the AE-RBPC with strong reactivity against the polyclonal antibody. The protein was not present in the albumin and globulin fractions of rice bran, or in the WE-RBPC. Gut lymphoid tissue was grossly normal upon pathological examination and had negative reaction when stained for IgE.
590 $a School code: 0011.
650 4 $a Agriculture, Food Science and Technology. $3 1017813
650 4 $a Health Sciences, Nutrition. $3 1017801
690 $a 0359
690 $a 0570
710 2 0 $a University of Arkansas. $3 1017562
773 0 $t Dissertation Abstracts International $g 53-08B.
790 1 0 $a Hamaker, Bruce R., $e advisor
790 $a 0011
791 $a Ph.D.
792 $a 1992
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9237325