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SUBMITTED FINAL Krentz Thesis 2021.pdf (45.67 MB)

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Use of casein micelles to improve the solubility of hydrophobic pea proteins in aqueous solutions via low-temperature homogenization

Krentz, Abigail L
http://orcid.org/0000-0002-9431-9578
http://rave.ohiolink.edu/etdc/view?acc_num=osu1626189040190757

Abstract Details

2021, Master of Science, Ohio State University, Food Science and Technology.
Bovine milk has played a quintessential role in human nutrition for generations. Specifically, caseins -the major milk protein- have the unique ability to assemble into micelles that efficiently protect and deliver calcium from mother to neonate. The casein micelle structure can be further harnessed as a delivery system for hydrophobic plant-based proteins to increase their solubility in aqueous solutions. Amid declining fluid milk sales and rising demand for plant-based alternatives, there is an emerging category in the market for hybrid milk products, containing both dairy and plant-based protein. The objective of this study was to utilize common dairy processing equipment to create a stable colloidal dispersion of casein micelles with pea protein to improve its solubility in aqueous solutions. It is hypothesized that low-temperature homogenization can be applied to an unstable dispersion of disrupted casein micelles and pea protein, and the resulting blend will be a stable colloidal dispersion in which the insoluble pea proteins associate with casein micelles in suspension. Unlike previous research studies, this protocol utilizes readily available dairy processing equipment that can be easily reproduced in any dairy facility. The first objective of this study was to improve the solubility of pea proteins in aqueous solutions through interactions with casein micelles. The efficacy of the proposed blending method was analyzed via sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and high-performance liquid chromatography (HPLC). Both analyses indicated that insoluble pea protein incorporated with casein micelles in solution, rather than with whey proteins or self-association with other pea proteins. Additionally, the soluble protein and hydrodynamic diameter of the dispersed particles in the mixed protein blends both significantly increased (P < 0.05) post-processing. This indicates that the proposed blending method was successful at increasing pea protein solubility. The second objective of this study was to maintain or improve the functional properties of casein micelles within the mixed protein blend. The mixed protein blends coagulated upon the addition of chymosin, a crucial functional property of caseins. The textures of the coagulated mixed protein blends were analyzed via a texture profile analyzer. Most notably, as the amount of pea protein in the blend increased, the hardness of the coagulate also increased (P < 0.05). Additionally, as the amount of pea protein in the blend increased, the foaming capacity and foaming stability decreased significantly (P < 0.05). The addition of pea protein did not affect the emulsion capacity or emulsion stability of the mixed protein blends (P > 0.05). A comprehensive understanding of the functional properties of the mixed protein blends is critical to utilizing them in future food applications. In summary, the blending method proposed here within successfully prepared a co-dispersion between pea protein and casein micelles that significantly increased the stability of the hydrophobic pea proteins in colloidal suspension. There is great potential to apply this research to other plant-based proteins or nutraceuticals with low solubility to be further utilized in an innovative way that allows the dairy industry to provide highly nutritious protein products, while also capitalizing on current consumer trends.
Rafael Jimenez-Flores (Advisor)
106 p.
Food Science
casein micelle; pea protein; homogenization; colloidal dispersion

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Citations

  • Krentz, A. L. (2021). Use of casein micelles to improve the solubility of hydrophobic pea proteins in aqueous solutions via low-temperature homogenization [Master's thesis, Ohio State University]. OhioLINK Electronic Theses and Dissertations Center. http://rave.ohiolink.edu/etdc/view?acc_num=osu1626189040190757

    APA Style (7th edition)

  • Krentz, Abigail. Use of casein micelles to improve the solubility of hydrophobic pea proteins in aqueous solutions via low-temperature homogenization. 2021. Ohio State University, Master's thesis. OhioLINK Electronic Theses and Dissertations Center, http://rave.ohiolink.edu/etdc/view?acc_num=osu1626189040190757.

    MLA Style (8th edition)

  • Krentz, Abigail. "Use of casein micelles to improve the solubility of hydrophobic pea proteins in aqueous solutions via low-temperature homogenization." Master's thesis, Ohio State University, 2021. http://rave.ohiolink.edu/etdc/view?acc_num=osu1626189040190757

    Chicago Manual of Style (17th edition)

osu1626189040190757
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This open access ETD is published by The Ohio State University and OhioLINK.