Here are some friends with simlar question as we.And I have this question for many days,anyone help us?
Kitty said: Yes.functional properties of proteins in food preparation?-I try seach this on internet but no results found.Maybe this is a stupid question.
Mike said: oh,no,you are wrong.I have found as below for this question(functional properties of proteins in food preparation?),it will help you,my kids.
Answers:
Heat, acidds, or enzymes denature protein. This is what we count on when an egg becomes scrambled. Too much denaturing, however, causes the water molecule in the protein is released. Ever heard of green, water eggs? That's what happened. Denaturing also makes proteins no longer act like proteins, so heat or acid must be added carefully to get the desired result, like soft scrambled eggs or souffles rising.
Try wilkipedia for protein info: http://en.wikipedia.org/wiki/Protein_denaturation
Other Answers:
J. Agric. Food Chem., 47 (2), 411 -416, 1999. 10.1021/jf9806964 S0021-8561(98)00696-7
Web Release Date: December 24, 1998
Copyright ? 1998 American Chemical Society
Preparation and Functional Properties of Rice Bran Protein Isolate
M. Wang, N. S. Hettiarachchy,* M. Qi, W. Burks, and T. Siebenmorgen
Department of Food Science, University of Arkansas, 272 Young Avenue, Fayetteville, Arkansas 72703, Department of Pediatrics, University of Arkansas for Medical Sciences and Arkansas Children's Hospital, 800 Marshall Street, Little Rock, Arkansas 72202, and Department of Biological and Agricultural Engineering, University of Arkansas, Fayetteville, Arkansas 72701
Received for review June 29, 1998. Revised manuscript received November 2, 1998. Accepted November 6, 1998. Financial support from the University of Arkansas and Riceland Food Inc. is appreciated.
Abstract:
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 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.
Keywords: Rice bran; protein isolate; phytase; xylanase; functional properties
Source(s):
http://pubs.acs.org/cgi-bin/abstract.cgi/jafcau/1999/47/i02/abs/jf9806964.html
Read this: All the information of cooking and health post by website user,chineseop.com not guarantee
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Kitty said: Yes.functional properties of proteins in food preparation?-I try seach this on internet but no results found.Maybe this is a stupid question.
Mike said: oh,no,you are wrong.I have found as below for this question(functional properties of proteins in food preparation?),it will help you,my kids.
Answers:
Heat, acidds, or enzymes denature protein. This is what we count on when an egg becomes scrambled. Too much denaturing, however, causes the water molecule in the protein is released. Ever heard of green, water eggs? That's what happened. Denaturing also makes proteins no longer act like proteins, so heat or acid must be added carefully to get the desired result, like soft scrambled eggs or souffles rising.
Try wilkipedia for protein info: http://en.wikipedia.org/wiki/Protein_denaturation
Other Answers:
J. Agric. Food Chem., 47 (2), 411 -416, 1999. 10.1021/jf9806964 S0021-8561(98)00696-7
Web Release Date: December 24, 1998
Copyright ? 1998 American Chemical Society
Preparation and Functional Properties of Rice Bran Protein Isolate
M. Wang, N. S. Hettiarachchy,* M. Qi, W. Burks, and T. Siebenmorgen
Department of Food Science, University of Arkansas, 272 Young Avenue, Fayetteville, Arkansas 72703, Department of Pediatrics, University of Arkansas for Medical Sciences and Arkansas Children's Hospital, 800 Marshall Street, Little Rock, Arkansas 72202, and Department of Biological and Agricultural Engineering, University of Arkansas, Fayetteville, Arkansas 72701
Received for review June 29, 1998. Revised manuscript received November 2, 1998. Accepted November 6, 1998. Financial support from the University of Arkansas and Riceland Food Inc. is appreciated.
Abstract:
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 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.
Keywords: Rice bran; protein isolate; phytase; xylanase; functional properties
Source(s):
http://pubs.acs.org/cgi-bin/abstract.cgi/jafcau/1999/47/i02/abs/jf9806964.html
correctness,It's Non-profit and only for informational purposes.
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