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Effect of microbial transglutaminase on the protein fractions of rice, pea and their blends
Author(s) -
Marco Cristina,
Pérez Gabriela,
Ribotta Pablo,
Rosell Cristina M
Publication year - 2007
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.3006
Subject(s) - tissue transglutaminase , globulin , chemistry , polyacrylamide gel electrophoresis , electrophoresis , gel electrophoresis , protein aggregation , solubility , biochemistry , storage protein , pea protein , molecular mass , sodium dodecyl sulfate , chromatography , disulfide bond , glutelin , food science , enzyme , biology , organic chemistry , gene , immunology
BACKGROUND: Transglutaminase (TG) is a transferase that has been used for crosslinking proteins. In general, those interactions are promoted within proteins of the same nature, and very few studies have been conducted for creating new bonds between proteins from different sources catalysed by TG. The effect of TG on the protein fractions of rice flour, pea protein isolate and their blends was studied by using different electrophoretic analyses (simple sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS‐PAGE) and multistaking SDS‐PAGE under reducing and non‐reducing conditions). RESULTS: TG induced the disappearance of numerous protein bands as a consequence of the formation of large protein polymers, linked by isopeptidic and disulfide bonds, with reduced solubility. The main protein fractions involved in those interactions were the albumins and globulins, from the pea protein isolate, and the rice flour; and the glutelins were also crosslinked. CONCLUSION: Composite flours containing the rice flour and the pea protein isolate are proposed for obtaining a protein‐enriched dough with better amino acid balance. Also a protein network formed of protein aggregates of high molecular weight can be created in the presence of transglutaminase. Copyright © 2007 Society of Chemical Industry