Sensory profile, functional properties and molecular weight distribution of fermented pea protein isolate.
| Autor: | García Arteaga V; Fraunhofer Institute for Process Engineering and Packaging IVV, Germany.; Center of Life and Food Sciences Weihenstephan, Technical University of Munich, Germany., Leffler S; Fraunhofer Institute for Process Engineering and Packaging IVV, Germany., Muranyi I; Fraunhofer Institute for Process Engineering and Packaging IVV, Germany., Eisner P; Fraunhofer Institute for Process Engineering and Packaging IVV, Germany.; ZIEL - Institute for Food & Health, Technical University of Munich, Germany.; Steinbeis-Hochschule, School of Technology and Engineering, Germany., Schweiggert-Weisz U; Fraunhofer Institute for Process Engineering and Packaging IVV, Germany. |
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| Jazyk: | angličtina |
| Zdroj: | Current research in food science [Curr Res Food Sci] 2020 Dec 13; Vol. 4, pp. 1-10. Date of Electronic Publication: 2020 Dec 13 (Print Publication: 2021). |
| DOI: | 10.1016/j.crfs.2020.12.001 |
| Abstrakt: | Pea protein isolate (PPI, from Pisum sativum L.) was fermented with six different lactic acid bacteria strains for 24 h and 48 h. The fermented samples were analyzed regarding their retronasal aroma and taste, their protein solubility, emulsifying and foaming capacity. Changes in the molecular weight distribution were analyzed to monitor potential effects of fermentation on the main allergenic protein fractions of PPI. After 24-h fermentation, PPI's characteristic aroma attributes and bitter taste decreased for all fermented PPI. However, after 48-h fermentation, cheesy aroma, and acid and salty tastes were increased. The PPI fermented with L. plantarum showed the most neutral taste and the panel's highest preference; instead, fermentation with L. fermentum led to a fecal aroma and was the least preferred. The protein solubility and emulsifying capacity decreased after PPI fermentation, while foaming capacity remained constant in comparison to the untreated PPI. The electrophoretic results showed a reduction in the intensity of the allergenic protein fractions; however, these changes might be attributed to the reduced protein solubility rather than to a high proteolytic effect of the strains. Fermentation of PPI for 24 h and 48 h might not be a suitable method for the production of highly functional pea proteins. Further modification methods have to be investigated in the future. Competing Interests: The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper. (© 2020 The Authors.) |
| Databáze: | MEDLINE |
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