Location: Healthy Processed Foods Research
Title: Maillard reaction products of rice protein hydrolysates with mono-, oligo- and polysaccharides Authors
|Li, Yue -|
|Zhong, Fang -|
|Ji, Wei -|
|Shoemaker, Charles -|
|Zhu, Song -|
|Xia, Wenshui -|
Submitted to: Food Hydrocolloids Journal
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: April 26, 2012
Publication Date: May 15, 2012
Repository URL: http://dx.doi.org/10.1016/j.foodhyd.2012.04.013
Citation: Li, Y., Zhong, F., Ji, W., Yokoyama, W.H., Shoemaker, C.F., Zhu, S., Xia, W. 2012. Maillard reaction products of rice protein hydrolysates with mono-, oligo- and polysaccharides. Food Hydrocolloids Journal. 30(1):53-60. DOI: 10.1016/j.foodhyd.2012.04.013. Interpretive Summary: The functionality of rice protein was improved by hydrolysis followed by combining and reacting the hydrolysates with small carbohydrates. The reaction products are called Maillard products and had improved solubility and emulsification properties. The properties of the protein hydrolysate peptide size and carbohydrate size were found to be important properties.
Technical Abstract: Rice protein, a byproduct of rice syrup production, is abundant but, its lack of functionality prevents its wide use as a food ingredient. Maillard reaction products of (MRPs) hydrolysates from the limited hydrolysis of rice protein (LHRP) and various mono-, oligo- and polysaccharides were evaluated for their functional properties. LHRPs (degree of hydrolysis (DH) 4-7%) by 3 proteases were reacted with glucose, lactose, maltodextrin DE20, or dextran T20. Hydrolysates of Protease N at 5% DH with dextran T20 (20 mins at 100 oC) produced MRPs with the greatest improvement in solubility (NS), emulsification activity (EA), and emulsification stability (ES). The NS, EA and ES of the MRP increased by factors of 3.5, 5.3 and 7.3 times, respectively as compared to MRP formed with native rice proteins. Amino acid analysis indicated that lysine and arginine decreased significantly in the MRPs. HPLC and fluorescence analysis suggested that formation of late stage MRPs occurred after 20 minutes. The functional properties of MRPs and the mechanisms of formation were affected by the peptide chain length.