Presentation Title

Impact of Maillard Conjugation on Stability and Antioxidant Activity of pea protein or caseinate nanoemulsions.

Faculty Mentor

Gabriel Davidov-Pardo

Start Date

23-11-2019 10:00 AM

End Date

23-11-2019 10:45 AM

Location

117

Session

poster 3

Type of Presentation

Poster

Subject Area

biological_agricultural_sciences

Abstract

Due to their amphiphilic nature, proteins have been employed as “clean-label” emulsifiers in the food industry. To ensure successful incorporation into food, emulsions must be stable at a variety of pH values and temperatures. Successfully utilized with animal proteins, Maillard conjugation covalently binds proteins with polysaccharides, generating emulsion stability through physical repulsion. However, consumers are increasingly seeking plant-based alternatives to animal products. To compare animal and plant-based proteins, casein and pea proteins were each conjugated with dextran (40kDa) through Maillard reaction for durations of 24 (C24) or 48 (P48) hours, respectively.

Maillard conjugates (MC) were characterized by SDS-Page and FTIR demonstrating the binding of dextran and proteins. Nanoemulsions were fabricated using MC as emulsifiers and were compared for stability at pH=4.6 (isoelectric point) and various temperatures, and indirect antioxidant activity. Particle size was measured as a mode of recording stability. C24 produced droplets with mean diameters of 125±12nm and 123±12nm, while P48 produced droplets with mean diameters of 269±36nm and 396±15nm at pH=7 and pH=4.6, respectively. Both remained stable against separation. P0 and C0 both separated at Ip, producing droplet diameters >1000nm. To measure the effects of temperature on stability nanoemulsions were incubated at temperatures 4˚C-55˚C at pH=4.6. C24 remained stable at all temperatures except 55oC, while P48 remained stable at 4-25oC. Antioxidant activity was determined by color retention of lutein, a bright-yellow, oxidatively-unstable pigment. There was no significant difference in the color degradation between MC and the non-conjugated proteins. Casein nanoemulsions exhibited the highest rate of color fading at 1.52-1.57dE/day, whereas pea protein nanoemulsions exhibited only 0.98-1.36dE/day, probably due to the larger surface area in the casein nanoemulsions compared to the pea protein ones. Overall, P48 is a viable alternative to milk-based proteins for dairy-substitute foods and beverages. MC increased stability in processing conditions without detrimentally impacting antioxidant activity.

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Nov 23rd, 10:00 AM Nov 23rd, 10:45 AM

Impact of Maillard Conjugation on Stability and Antioxidant Activity of pea protein or caseinate nanoemulsions.

117

Due to their amphiphilic nature, proteins have been employed as “clean-label” emulsifiers in the food industry. To ensure successful incorporation into food, emulsions must be stable at a variety of pH values and temperatures. Successfully utilized with animal proteins, Maillard conjugation covalently binds proteins with polysaccharides, generating emulsion stability through physical repulsion. However, consumers are increasingly seeking plant-based alternatives to animal products. To compare animal and plant-based proteins, casein and pea proteins were each conjugated with dextran (40kDa) through Maillard reaction for durations of 24 (C24) or 48 (P48) hours, respectively.

Maillard conjugates (MC) were characterized by SDS-Page and FTIR demonstrating the binding of dextran and proteins. Nanoemulsions were fabricated using MC as emulsifiers and were compared for stability at pH=4.6 (isoelectric point) and various temperatures, and indirect antioxidant activity. Particle size was measured as a mode of recording stability. C24 produced droplets with mean diameters of 125±12nm and 123±12nm, while P48 produced droplets with mean diameters of 269±36nm and 396±15nm at pH=7 and pH=4.6, respectively. Both remained stable against separation. P0 and C0 both separated at Ip, producing droplet diameters >1000nm. To measure the effects of temperature on stability nanoemulsions were incubated at temperatures 4˚C-55˚C at pH=4.6. C24 remained stable at all temperatures except 55oC, while P48 remained stable at 4-25oC. Antioxidant activity was determined by color retention of lutein, a bright-yellow, oxidatively-unstable pigment. There was no significant difference in the color degradation between MC and the non-conjugated proteins. Casein nanoemulsions exhibited the highest rate of color fading at 1.52-1.57dE/day, whereas pea protein nanoemulsions exhibited only 0.98-1.36dE/day, probably due to the larger surface area in the casein nanoemulsions compared to the pea protein ones. Overall, P48 is a viable alternative to milk-based proteins for dairy-substitute foods and beverages. MC increased stability in processing conditions without detrimentally impacting antioxidant activity.