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. 2023 May 17;12(10):2030.
doi: 10.3390/foods12102030.

Co-Gelation of Pumpkin-Seed Protein with Egg-White Protein

Marta Tomczyńska-Mleko  1 , Konrad Terpiłowski  2 , Salvador Pérez-Huertas  3 , Viktoria Sapiga  4 , Galina Polischuk  4 , Bartosz Sołowiej  5 , Maciej Nastaj  5 , Marta Wesołowska-Trojanowska  6 , Stanisław Mleko  5
Affiliations

Co-Gelation of Pumpkin-Seed Protein with Egg-White Protein

Marta Tomczyńska-Mleko et al. Foods. .

Abstract

The aim of this study was to investigate the gelation process of binary mixes of pumpkin-seed and egg-white proteins. The substitution of pumpkin-seed proteins with egg-white proteins improved the rheological properties of the obtained gels, i.e., a higher storage modulus, lower tangent delta, and larger ultrasound viscosity and hardness. Gels with a larger egg-white protein content were more elastic and more resistant to breaking structure. A higher concentration of pumpkin-seed protein changed the gel microstructure to a rougher and more particulate one. The microstructure was less homogenous, with a tendency to break at the pumpkin/egg-white protein gel interface. The decrease in the intensity of the amide II band with an increase in the pumpkin-seed protein concentration showed that the secondary structure of this protein evolved more toward a linear amino acid chain compared with the egg-white protein, which could have an impact on the microstructure. The supplementation of pumpkin-seed proteins with egg-white proteins caused a decrease in water activity from 0.985 to 0.928, which had important implications for the microbiological stability of the obtained gels. Strong correlations were found between the water activity and rheological properties of the gels; an improvement of their rheological properties resulted in a decrease in water activity. The supplementation of pumpkin-seed proteins with egg-white proteins resulted in more homogenous gels with a stronger microstructure and better water binding.

Keywords: FTIR; egg white; gelation; microstructure; protein; pumpkin; rheology; texture.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Influence of frequency on storage modulus of mixed gels.
Figure 2
Figure 2
Influence of frequency on tangent delta of mixed gels.
Figure 3
Figure 3
Ultrasound viscosity of mixed gels. Means with different letters (a–g) were significantly different (p ≤ 0.05).
Figure 4
Figure 4
Hardness of mixed gels. Means with different letters (a–g) were significantly different (p ≤ 0.05).
Figure 5
Figure 5
Correlation between ultrasound viscosity and hardness for PSP/EWP mixed gels.
Figure 6
Figure 6
Correlation between storage modulus at 10 Hz and ultrasound viscosity for PSP/EWP mixed gels.
Figure 7
Figure 7
Polarizing optical microscopy view of mixed gels: (a) 12% EWP; (b) 8% EWP and 4% PSP; (c) 4% EWP and 8% PSP; (d) 12% PSP.
Figure 8
Figure 8
Scanning electron microscopy of mixed gels. (a,a’)—4% egg-white protein (EWP) mixed with pumpkin seeds protein (PSP), (b,b’)—8% EWP + 4% PSP, (c,c’)—12% EWP, (d,d’)—12% PSP. Images were obtained at different magnifications (top row 500×, bottom row 5000× respectively).
Figure 9
Figure 9
Surface roughness of mixed gels. Means with different letters (a–f) were significantly different (p ≤ 0.05).
Figure 10
Figure 10
FRIR absorption spectra of investigated gels: (a) spectrum noted for 12% PSP gel; (b) spectra for mixed gels.
Figure 11
Figure 11
Water activity of mixed gels. Means with different letters (a–f) were significantly different (p ≤ 0.05).
See this image and copyright information in PMC

References

    1. Pérez-Huertas S., Terpiłowski K., Tomczyńska-Mleko M., Nishinari K., Mleko S. Surface and rheological properties of egg white albumin/gelatin dispersions gelled on cold plasma-activated glass. Food Hydrocoll. 2015;96:224–230. doi: 10.1016/j.foodhyd.2019.05.029. - DOI
    1. Aschemann-Witzel J., Gantriis R.F., Fraga P., Perez-Cueto F.J. Plant-based food and protein trend from a business perspective: Markets, consumers, and the challenges and opportunities in the future. Crit. Rev. Food Sci. Nutr. 2021;61:3119–3128. doi: 10.1080/10408398.2020.1793730. - DOI - PubMed
    1. Gomes A., Sobral P.J.D.A. Plant protein-based delivery systems: An emerging approach for increasing the efficacy of lipophilic bioactive compounds. Molecules. 2021;27:60. doi: 10.3390/molecules27010060. - DOI - PMC - PubMed
    1. Weng Y., Sun Z. Major cucurbit crops. In: Wang Y.-H., Behera T.K., Kole C., editors. Genetics, Genomics and Breeding of Cucurbits. CRC Press; Boca Raton, FL, USA: 2012. pp. 1–16.
    1. Miedzianka J., Zambrowicz A., Zielińska-Dawidziak M., Drożdż W., Nemś A. Effect of acetylation on physicochemical and functional properties of commercial pumpkin protein concentrate. Molecules. 2021;26:1575. doi: 10.3390/molecules26061575. - DOI - PMC - PubMed

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