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. 2021 Mar 12;26(6):1575.
doi: 10.3390/molecules26061575.

Effect of Acetylation on Physicochemical and Functional Properties of Commercial Pumpkin Protein Concentrate

Affiliations

Effect of Acetylation on Physicochemical and Functional Properties of Commercial Pumpkin Protein Concentrate

Joanna Miedzianka et al. Molecules. .

Abstract

The purpose of the present study was to determine the effects of acetylation with different doses of acetic anhydride on the chemical composition and chosen functional properties of commercial pumpkin protein concentrate (PPC). The total protein content decreased as compared to unmodified samples. Electrophoretic analysis revealed that in the acetylated pumpkin protein, the content of the heaviest protein (35 kDa) decreased in line with increasing concentrations of modifying reagent. Acetylation of PPC caused a significant increase in water-binding and oil-absorption capacity and for emulsifying properties even at the dose of 0.4 mL/g. Additionally, an increase in foaming capacity was demonstrated for preparations obtained with 2.0 mL/g of acetic anhydride, whereas acetylation with 0.4 and 1.0 mL/g caused a decrease in protein solubility as compared to native PPC.

Keywords: SDS-PAGE; acetylation; amino acid profile; chemical composition; functional properties; in vitro digestibility; pumpkin protein concentrates.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
SDS-PAGE of native and acetylated PPC. PPC—pumpkin protein concentrate; 0.4, 1.0, 2.0—pumpkin protein preparations after acetylation conducted with different concentrations of acetic anhydride (mL/g); MW—molecular weight marker prepared at laboratory (18.4 kDa (β-lactoglobulin), 42, 45 kDa (ovalbumin), 66 kDa (bovine serum albumin).
Figure 2
Figure 2
Effect of anhydride-to-protein ratio on protein solubility (PS) at different pH of native and acetylated PPC. Values are means ± standard deviation; a,b,c,d—the same letters within the same pH were not significantly different; PPC—pumpkin protein concentrate; 0.4, 1.0, 2.0—pumpkin protein preparations after acetylation conducted with different concentrations of acetic anhydride (mL/g).
Figure 3
Figure 3
Effect of anhydride-to-protein ratio on water-binding capacity (WBC) and oil-absorption capacity (OAC) of native and acetylated PPC. a,b,c—the same letters within the same analysis were not significantly different; PPC—pumpkin protein concentrate; 0.4, 1.0, 2.0—pumpkin protein preparations after acetylation conducted with different concentrations of acetic anhydride (mL/g).
Figure 4
Figure 4
Effect of anhydride-to-protein ratio on foam capacity (FC) at different pH of native and acetylated PPC. a,b,c—the same letters within the same pH were not significantly different; PPC—pumpkin protein concentrate; 0.4, 1.0, 2.0—pumpkin protein preparations after acetylation conducted with different concentrations of acetic anhydride (mL/g).
Figure 5
Figure 5
Effect of anhydride-to-protein ratio on emulsion activity (EA) at a different pH of native and acetylated PPC. a,b,c,d—the same letters within the same pH were not significantly different; PPC—pumpkin protein concentrate; 0.4, 1.0, 2.0—pumpkin protein preparations after acetylation conducted with different concentrations of acetic anhydride (mL/g).
Figure 6
Figure 6
Effect of anhydride-to-protein ratio on emulsion activity (ES) at different pH of native and acetylated PPC. a,b,c—the same letters within the same pH were not significantly different; PPC—pumpkin protein concentrate; 0.4, 1.0, 2.0—pumpkin protein preparations after acetylation conducted with different concentrations of acetic anhydride (mL/g).

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