Presentation Title

Maillard Conjugation with the use of Pea Protein and Dextran for the Stabilization of Multilayered Nanoemulsions.

Faculty Mentor

Gabriel Davidov-Pardo

Start Date

18-11-2017 12:30 PM

End Date

18-11-2017 1:30 PM

Location

BSC-Ursa Minor 81

Session

Poster 2

Type of Presentation

Poster

Subject Area

biological_agricultural_sciences

Abstract

An emulsion is a dispersion of two immiscible liquids, these mixtures are unstable and will separate unless surfactants are used to coat the dispersed phase. Many common foods are emulsions, usually made of oil and water (e.g. salad dressings, margarine, gravies, etc.). Proteins are a viable alternative to artificial surfactants to create emulsions. The main drawback of using proteins as emulsifiers is their precipitation at certain pHs. When reaching the pH of the isoelectric point, proteins lose their electrostatic charge and coagulate. Through Maillard reactions, proteins combined with polysaccharides create conjugates that prevent their coagulation. In recent years pulse proteins have gained interest in the food industry for their sustainability and high biological value. The objective of this work was to determine if pulses are a suitable replacement for typical protein sources for creation of Maillard conjugates. Maillard conjugates were created by mixing protein and saccharides in a 1:1 w/w ratio, freeze-drying, then placing them in a climactic chamber at 60°C and 77.5% relative humidity for 72 hours with samples removed at 24 hour intervals for testing. The initial proteins and saccharides consisted of pea protein and sodium caseinate (control) in conjunction with various molecular weights of dextran (12, 40, 150, and 250KD). To determine conjugation yield, Lowry assays were conducted to assess the stability of the proteins at the isoelectric point. To determine efficiency of conjugation O-phtaldehyde assays were conducted to determine the amount of free amino groups remaining. Current results show that at 24h the pea protein with dextran (40KD) had the greatest yield of 81%, meaning 81% of the protein remained in solution at the isoelectric point, though yield decreased over 48h and 72h samples. The same sample had an efficiency of 22% reduction of total amino groups. In casein samples, the conjugation yield under same conditions reached 97% and the conjugation efficiency 9%. We proved that is possible to stabilize pea proteins through Maillard conjugation. In future research we hope to combine these conjugates with polyphenols and lutein to form stable lutein enriched multilayered emulsions for functional products.

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Nov 18th, 12:30 PM Nov 18th, 1:30 PM

Maillard Conjugation with the use of Pea Protein and Dextran for the Stabilization of Multilayered Nanoemulsions.

BSC-Ursa Minor 81

An emulsion is a dispersion of two immiscible liquids, these mixtures are unstable and will separate unless surfactants are used to coat the dispersed phase. Many common foods are emulsions, usually made of oil and water (e.g. salad dressings, margarine, gravies, etc.). Proteins are a viable alternative to artificial surfactants to create emulsions. The main drawback of using proteins as emulsifiers is their precipitation at certain pHs. When reaching the pH of the isoelectric point, proteins lose their electrostatic charge and coagulate. Through Maillard reactions, proteins combined with polysaccharides create conjugates that prevent their coagulation. In recent years pulse proteins have gained interest in the food industry for their sustainability and high biological value. The objective of this work was to determine if pulses are a suitable replacement for typical protein sources for creation of Maillard conjugates. Maillard conjugates were created by mixing protein and saccharides in a 1:1 w/w ratio, freeze-drying, then placing them in a climactic chamber at 60°C and 77.5% relative humidity for 72 hours with samples removed at 24 hour intervals for testing. The initial proteins and saccharides consisted of pea protein and sodium caseinate (control) in conjunction with various molecular weights of dextran (12, 40, 150, and 250KD). To determine conjugation yield, Lowry assays were conducted to assess the stability of the proteins at the isoelectric point. To determine efficiency of conjugation O-phtaldehyde assays were conducted to determine the amount of free amino groups remaining. Current results show that at 24h the pea protein with dextran (40KD) had the greatest yield of 81%, meaning 81% of the protein remained in solution at the isoelectric point, though yield decreased over 48h and 72h samples. The same sample had an efficiency of 22% reduction of total amino groups. In casein samples, the conjugation yield under same conditions reached 97% and the conjugation efficiency 9%. We proved that is possible to stabilize pea proteins through Maillard conjugation. In future research we hope to combine these conjugates with polyphenols and lutein to form stable lutein enriched multilayered emulsions for functional products.