2020
DOI: 10.1021/acs.biomac.0c00186
|View full text |Cite
|
Sign up to set email alerts
|

Processing Induced Changes in Food Proteins: Amyloid Formation during Boiling of Hen Egg White

Abstract: Amyloid fibrils (AFs) are highly ordered protein nanofibers composed of cross β-structure that occur in nature, but that also accumulate in age-related diseases. Amyloid propensity is a generic property of proteins revealed by conditions that destabilize the native state, suggesting that food processing conditions may promote AF formation. This had only been shown for foie gras, but not in common foodstuffs. We here extracted a dense network of fibrillar proteins from commonly consumed boiled hen egg white (EW… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
1
1

Citation Types

6
62
0

Year Published

2021
2021
2024
2024

Publication Types

Select...
5
1
1

Relationship

2
5

Authors

Journals

citations
Cited by 42 publications
(68 citation statements)
references
References 49 publications
6
62
0
Order By: Relevance
“…In a black 96-well plate (Greiner Bio-One), samples were prepared as in Monge-Morera et al (2020) and measured in triplicate in a Synergy Multi-Mode Microplate Reader (BioTek). The excitation and emission wavelengths were 440 nm and 480 nm, respectively.…”
Section: Analysis Of Thioflavin T Fluorescencementioning
confidence: 99%
See 3 more Smart Citations
“…In a black 96-well plate (Greiner Bio-One), samples were prepared as in Monge-Morera et al (2020) and measured in triplicate in a Synergy Multi-Mode Microplate Reader (BioTek). The excitation and emission wavelengths were 440 nm and 480 nm, respectively.…”
Section: Analysis Of Thioflavin T Fluorescencementioning
confidence: 99%
“…The apparent MW distribution of (un)heated EWSD, EWSD 50°C/50% and EWSD 60°C/80% (see section 2.4) was also monitored with both UV (at 280 nm) and ThT fluorescence measurements (with 450 and 480 nm as excitation and emission wavelengths, respectively) as described in Monge-Morera et al (2020). In this case, samples (25 µl) were loaded on the same column type, eluted at 30 °C and the analysis was performed using a modular system similar to the above one.…”
Section: Size Exclusion Chromatographymentioning
confidence: 99%
See 2 more Smart Citations
“…[27] Wheat gluten is also known to form amyloid fibrils in certain experimental conditions. [28] There have also been reports of in-vitro formation of amyloid-like fibrils by seed storage proteins of maize, wheat, pea, and soybean. [29] The seed storage proteins, interestingly, are reported to possess carbohydrate-affinity due to lectin-like activity.…”
Section: Introductionmentioning
confidence: 99%