Ute Schweiggert-Weisz

Prof. Dr. Ute Schweiggert-Weisz

Department Food Process Development, Fraunhofer Institute for Process Engineering and Packaging (IVV), 85354 Freising, Germany
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Research Focus & Metrics

Academic Career Length

9Years (2018-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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25 February 2021 in Molecules
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Journal Article
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MPMelanie Platzer
Melanie Platzer
SKSandra Kiese
Sandra Kiese
THThomas Herfellner
Thomas Herfellner
Ute Schweiggert-WeiszUte Schweiggert-Weisz
Ute Schweiggert-Weisz
OMOliver Miesbauer
Oliver Miesbauer
PEPeter Eisner
Peter Eisner
Numerous assays were developed to measure the antioxidant activity, but each has limitations and the results obtained by different methods are not always comparable. Popular examples are the DPPH and ABTS assay. Our aim was to study similarities and differences of these two assay regarding the measured antioxidant potentials of 24 phenolic compounds using the same measurement and evaluation methods. This should allow conclusions to be drawn as to whether one of the assays is more suitable for measuring specific subgroups like phenolic acids, flavonols, flavanones, dihydrochalcones or flavanols. The assays showed common trends for the mean values of most of the subgroups. Some dihydrochalcones and flavanones did not react with the DPPH radical in contrast to the ABTS radical, leading to significant differences. Therefore, to determine the antioxidant potential of dihydrochalcone or flavanone-rich extracts, the ABTS assay should be preferred. We found that the results of the flavonoids in the DPPH assay were dependent on the Bors criteria, whereas the structure–activity relationship in the ABTS assay was not clear. For the phenolic acids, the results in the ABTS assay were only high for pyrogallol structures, while the DPPH assay was mainly determined by the number of OH groups.

20 May 2021 in Antioxidants
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MPMelanie Platzer
Melanie Platzer
SKSandra Kiese
Sandra Kiese
THThomas Herfellner
Thomas Herfellner
Ute Schweiggert-WeiszUte Schweiggert-Weisz
Ute Schweiggert-Weisz
PEPeter Eisner
Peter Eisner
Plants produce a diverse array of secondary metabolites that are generally nonessential but facilitate ecological interactions. Fruits, vegetables, seeds and nuts can accumulate bioactive secondary metabolites with health-promoting properties, including the potent antioxidant activities of phenolic compounds. Several in vitro assays have been developed to measure the polyphenol content and antioxidant activity of plant extracts, e.g., the simple and highly popular Folin-Ciocalteu (FC) assay. However, the literature contains a number of different descriptions of the assay and it is unclear whether the assay measures the polyphenol content or reducing capacity of the sample. To determine the influence of phenolic structures on the outcome of the FC assay, we tested phenols representing different subgroups (phenolic acids, flavonols, flavanols, dihydrochalcones and flavanones). We observed different results for each reference substance and subgroup. Accordingly, we concluded that the FC assay does not measure the polyphenol content of a sample but determines its reducing capacity instead. Assigning the substances to five structural classes showed that the FC results depend on the number of fulfilled Bors criteria. If a molecule fulfills none of the Bors criteria, the FC results depend on the number of OH groups. We did not find a correlation with other single electron transfer assays (e.g., ABTS and DPPH assays). Furthermore, the FC assay was compatible with all five subgroups and should be preferred over the DPPH assay, which is specific for extracts rich in dihydrochalcones or flavanones.

1 January 2021 in Current Research in Food Science
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Journal Article
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VAVerónica García Arteaga
Verónica García Arteaga
SLSophia Leffler
Sophia Leffler
IMIsabel Muranyi
Isabel Muranyi
PEPeter Eisner
Peter Eisner
Ute Schweiggert-WeiszUte Schweiggert-Weisz
Ute Schweiggert-Weisz
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.

25 July 2019 in Food Science & Nutrition
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KSKatharina Schlegel
Katharina Schlegel
KSKatharina Sontheimer
Katharina Sontheimer
AHAndrea Hickisch
Andrea Hickisch
AWAli Abas Wani
Ali Abas Wani
PEPeter Eisner
Peter Eisner
Ute Schweiggert-WeiszUte Schweiggert-Weisz
Ute Schweiggert-Weisz
Enzymatic hydrolysis of lupin protein isolates (LPI; Lupinus angustifolius L.) was performed with nine different protease preparations to investigate their effect on technofunctionality, sensory properties, and the integrity of the proteins to estimate the reduction of the immunoreactivity. Alcalase 2.4 L, papain, and pepsin were most effective in the degradation of the α‐ and β‐conglutin examined by SDS–PAGE analysis, although the degree of hydrolysis only slightly increased. The technofunctional properties of LPI—solubility, emulsifying, and foaming activity—were improved by most of the proteolytic enzymes with the most impressive increase from 980% foam activity for LPI up to 3,614% foam activity for pepsin hydrolysate. The formation of bitterness, most likely linked to generation of bitter peptides, was pronounced in the Alcalase hydrolysate, while the other hydrolysates did not show an extensive increase in bitterness compared to the LPI. Other sensory attributes of the hydrolysates—with the exception of Alcalase treatment—were also very similar to the LPI. The results of this study show the potential of enzymatic degradation of LPI to modify the IgE‐reacting polypeptides and to improve the technofunctionality of the isolates and therefore their use as food ingredients.

Verified
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Susanne Naumann-GolaSusanne Naumann-Gola
Susanne Naumann-Gola
DHDirk Haller
Dirk Haller
PEPeter Eisner
Peter Eisner
Ute Schweiggert-WeiszUte Schweiggert-Weisz
Ute Schweiggert-Weisz
Plant compounds are described to interact with bile acids during small intestinal digestion. This review will summarise mechanisms of interaction between bile acids and plant compounds, challenges in in vivo and in vitro analyses, and possible consequences on health. The main mechanisms of interaction assume that increased viscosity during digestion results in reduced micellar mobility of bile acids, or that bile acids and plant compounds are associated or complexed at the molecular level. Increasing viscosity during digestion due to specific dietary fibres is considered a central reason for bile acid retention. Furthermore, hydrophobic interactions are proposed to contribute to bile acid retention in the small intestine. Although frequently hypothesised, no mechanism of permanent binding of bile acids by dietary fibres or indigestible protein fractions has yet been demonstrated. Otherwise, various polyphenolic structures were recently associated with reduced micellar solubility and modification of steroid and bile acid excretion but underlying molecular mechanisms of interaction are not yet fully understood. Therefore, future research activities need to consider the complex composition and cell-wall structures as influenced by processing when investigating bile acid interactions. Furthermore, influences of bile acid interactions on gut microbiota need to be addressed to clarify their role in bile acid metabolism.

25 June 2019 in Nutrients
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Susanne Naumann-GolaSusanne Naumann-Gola
Susanne Naumann-Gola
Ute Schweiggert-WeiszUte Schweiggert-Weisz
Ute Schweiggert-Weisz
JEJulia Eglmeier
Julia Eglmeier
DHDirk Haller
Dirk Haller
PEPeter Eisner
Peter Eisner
Dietary fibres are reported to interact with bile acids, preventing their reabsorption and promoting their excretion into the colon. We used a method based on in vitro digestion, dialysis, and kinetic analysis to investigate how dietary fibre enriched food ingredients affect the release of primary and secondary bile acids as related to viscosity and adsorption. As the main bile acids abundant in humans interactions with glyco- and tauroconjugated cholic acid, chenodesoxycholic acid and desoxycholic acid were analysed. Viscous interactions were detected for apple, barley, citrus, lupin, pea, and potato derived ingredients, which slowed the bile acid release rate by up to 80%. Adsorptive interactions of up to 4.7 μmol/100 mg DM were significant in barley, oat, lupin, and maize preparations. As adsorption directly correlated to the hydrophobicity of the bile acids the hypothesis of a hydrophobic linkage between bile acids and dietary fibre is supported. Delayed diffusion in viscous fibre matrices was further associated with the micellar properties of the bile acids. As our results indicate changes in the bile acid pool size and composition due to interactions with dietary fibre rich ingredients, the presented method and results could add to recent fields of bile acid research.