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Removal and Replacement of Endogenous Ligands from Lipid-Bound Proteins and Allergens
Published on: February 24, 2021
Transglutaminase polymerization of peanut proteins
D A Clare1, G Gharst, T H Sanders
1Department of Food Science, Agricultural Research Service, U.S. Department of Agriculture, North Carolina State University, Raleigh, North Carolina 27695-7624, USA.
Journal of Agricultural and Food Chemistry
|January 18, 2007
Summary
Transglutaminase enzyme modifies peanut proteins, creating polymers and dimers. This enzymatic modification of peanut proteins did not enhance allergic responses, suggesting new food ingredient potential.
Area of Science:
- Food Science
- Biochemistry
- Protein Chemistry
Background:
- Transglutaminase (TG) is known to cross-link various proteins via an acyl transferase mechanism.
- Previous studies have focused on TG's effects on soy, casein, and whey proteins, but its impact on peanut proteins is less explored.
Purpose of the Study:
- To investigate the catalytic activity of exogenous transglutaminase on peanut protein fractions, including purified Ara h 1.
- To analyze the structural changes, polymerization degree, and functional properties of TG-modified peanut proteins.
- To assess the potential impact of TG modification on the allergenic potential of peanut proteins.
Main Methods:
- Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) to analyze protein polymerization and molecular weight changes.
- Ortho-phthaldialdehyde (OPA) assays to quantify the degree of protein coupling and polymerization.
- Rheological measurements to assess changes in viscosity of TG-modified peanut extracts.
- Immunoglobulin E (IgE) binding assays to evaluate allergic response potential.
Main Results:
- Transglutaminase induced the formation of high molecular weight polymers in most peanut protein fractions and distinct dimer formation in purified Ara h 1.
- Ortho-phthaldialdehyde assays indicated significant protein coupling, with approximately 21% and 30% coupling in hexane-extracted fractions and roasted flour dispersions, respectively.
- Transglutaminase treatment resulted in decreased viscosity of peanut protein extracts.
- Peanut protein polymers and glycoprotein conjugates showed similar IgE binding activity to controls, suggesting no enhancement of allergic responses.
Conclusions:
- Exogenous transglutaminase effectively catalyzes cross-linking reactions in peanut protein fractions, leading to polymerization and dimer formation.
- Enzymatic modification of peanut proteins with transglutaminase alters their functional properties, such as reducing viscosity.
- The study indicates that transglutaminase modification does not increase the allergenic potential of peanut proteins.
- These findings suggest the development of novel peanut-based food ingredients with unique functionalities for diverse food applications.
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