| 1. |
- Auer, Jaqueline, et al.
(author)
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Nordic Crops as Alternatives to Soy-An Overview of Nutritional, Sensory, and Functional Properties
- 2023
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In: Foods. - 2304-8158. ; 12
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Research review (peer-reviewed)abstract
- Soy (Glycine max) is used in a wide range of products and plays a major role in replacing animal-based products. Since the cultivation of soy is limited by cold climates, this review assessed the nutritional, sensory, and functional properties of three alternative cold-tolerant crops (faba bean (Vicia faba), yellow pea (Pisum sativum), and oat (Avena sativa)). Lower protein quality compared with soy and the presence of anti-nutrients are nutritional problems with all three crops, but different methods to adjust for these problems are available. Off-flavors in all pulses, including soy, and in cereals impair the sensory properties of the resulting food products, and few mitigation methods are successful. The functional properties of faba bean, pea, and oat are comparable to those of soy, which makes them usable for 3D printing, gelation, emulsification, and extrusion. Enzymatic treatment, fermentation, and fibrillation can be applied to improve the nutritional value, sensory attributes, and functional properties of all the three crops assessed, making them suitable for replacing soy in a broad range of products, although more research is needed on all attributes.
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| 2. |
- Herneke, Anja
(author)
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Plant protein nanofibrils : characterising properties for future food
- 2022
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Doctoral thesis (other academic/artistic)abstract
- This thesis explores the potential of protein nanofibrils (PNFs) as an ingredient to generate structure in food. Proteins from whey and from plants were used to form PNFs, with particular focus on proteins extracted from plants. PNFs were formed by heating (85-90 °C) the proteins at pH 2 for 24-96 h. Various microstructural features were observed on casting whey-based PNFs with nanoscale variations (length, morphology) into films. Length of the PNFs, rather than morphology, had the greatest effect on microstructural attributes. Whey is a well-studied food protein with good ability to form PNFs. Whey-based and plant-based PNFs were compared to understand better how plant proteins can be used to form PNFs with similar length. Characterisation of the secondary structure and morphology of PNFs made from plant-based sources, such as legumes, cereals, oilseeds and tubers, showed that all proteins could form PNFs, but with some variation in morphology (curved/straight). Analysis of extracted protein size and purity to investigate their effects on formation of PNFs revealed that smaller and purer proteins gave better PNFs production. Increased pH after fibril formation affected PNF morphology and the viscosity of fibrillated samples of fava bean, fava bean globular fractions 11S and 7S, and mung bean. Straight PNFs from fava beans and curved PNFs from mung beans were examined for their ability to form and stabilise foams. At relatively low concentrations, fibrillated proteins (independent of PNF morphology) generated more voluminous and more stable foam than the corresponding protein at the same concentration. At very low concentrations, only curved PNFs gave stable foams at pH close to the isoelectric point of the protein. Preliminary results indicated that curved PNFs from mung beans can also be assembled into microfibres with the help of a flow-focusing method, which has potential for use in creating meat-like textures in future food applications.
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| 3. |
- Herneke, Anja, et al.
(author)
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Protein Nanofibrils from Fava Bean and Its Major Storage Proteins : Formation and Ability to Generate and Stabilise Foams
- 2023
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In: Foods. - : MDPI AG. - 2304-8158. ; 12:3
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Journal article (peer-reviewed)abstract
- Protein nanofibrils (PNFs) have potential for use in food applications as texture inducers. This study investigated the formation of PNFs from protein extracted from whole fava bean and from its two major storage proteins, globulin fractions 11S and 7S. PNFs were formed by heating (85 degrees C) the proteins under acidic conditions (pH 2) for 24 h. Thioflavin T fluorescence and atomic force microscopy techniques were used to investigate PNF formation. The foaming properties (capacity, stability, and half-life) were explored for non-fibrillated and fibrillated protein from fava bean, 11S, and 7S to investigate the texturing ability of PNFs at concentrations of 1 and 10 mg/mL and pH 7. The results showed that all three heat-incubated proteins (fava bean, 11S, and 7S) formed straight semi-flexible PNFs. Some differences in the capacity to form PNFs were observed between the two globulin fractions, with the smaller 7S protein being superior to 11S. The fibrillated protein from fava bean, 11S, and 7S generated more voluminous and more stable foams at 10 mg/mL than the corresponding non-fibrillated protein. However, this ability for fibrillated proteins to improve the foam properties seemed to be concentration-dependent, as at 1 mg/mL, the foams were less stable than those made from the non-fibrillated protein.
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| 4. |
- Herneke, Anja, et al.
(author)
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Protein nanofibrils from mung bean : The effect of pH on morphology and the ability to form and stabilise foams
- 2023
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In: Food Hydrocolloids. - : Elsevier BV. - 0268-005X .- 1873-7137. ; 136
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Journal article (peer-reviewed)abstract
- Protein nanofibrils (PNFs) have potential food uses due to their favorable mechanical and rheological properties. In order to use plant-based protein nanofibrils (PNFs) in new sustainable food applications, a better under-standing is needed of the impact of pH on PNFs and their functional properties. In this study, we developed an improved method for generating PNFs from mung bean protein isolate and its globular 8S fraction. We then investigated how these PNFs are affected by increased pH and how pH affects their ability to form stable foams. PNFs were generated in acidic conditions (pH 2) by heating at 85 degrees C for 2-48 h. Formation of PNFs and the effect of increased pH on their stability were evaluated using thioflavin T fluorescence, electrophoretic gel separation, circular dichroism spectroscopy, atomic force microscopy and viscosity profiling. Foams were made by intense mixing with a homogeniser and evaluated for foam capacity, foam stability and bubble size distribution, using confocal imaging. The results showed that it is possible to optimise the fibrillation conditions for mung bean by generating a more pure initial protein isolate by salt extraction. The results also showed that pH alters the structure of PNFs by degradation and aggregation around the isoelectric point of the protein isolate. At neutral pH, the PNFs were slightly shorter than at the starting pH, but no longer formed aggregates. Fibrillated mung bean protein at pH 4-8 was found to have good foaming properties compared with non-fibrillated protein at the same conditions. The new knowledge generated in this study about how pH alters the structure and foaming properties of PNFs can pave the way for use of PNFs in new innovative food applications.
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| 5. |
- Kamada, Ayaka, et al.
(author)
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Hierarchical propagation of structural features in protein nanomaterials
- 2022
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In: Nanoscale. - : Royal Society of Chemistry (RSC). - 2040-3372 .- 2040-3364. ; 14:6, s. 2502-2510
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Journal article (peer-reviewed)abstract
- Natural high-performance materials have inspired the exploration of novel materials from protein building blocks. The ability of proteins to self-organize into amyloid-like nanofibrils has opened an avenue to new materials by hierarchical assembly processes. As the mechanisms by which proteins form nanofibrils are becoming clear, the challenge now is to understand how the nanofibrils can be designed to form larger structures with defined order. We here report the spontaneous and reproducible formation of ordered microstructure in solution cast films from whey protein nanofibrils. The structural features are directly connected to the nanostructure of the protein fibrils, which is itself determined by the molecular structure of the building blocks. Hence, a hierarchical assembly process ranging over more than six orders of magnitude in size is described. The fibril length distribution is found to be the main determinant of the microstructure and the assembly process originates in restricted capillary flow induced by the solvent evaporation. We demonstrate that the structural features can be switched on and off by controlling the length distribution or the evaporation rate without losing the functional properties of the protein nanofibrils.
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| 6. |
- Rahman, M. Mahafuzur, et al.
(author)
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Food protein-derived amyloids do not accelerate amyloid beta aggregation
- 2023
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In: Scientific Reports. - : Springer Nature. - 2045-2322. ; 13:1
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Journal article (peer-reviewed)abstract
- The deposition of proteins in the form of amyloid fibrils is closely associated with several serious diseases. The events that trigger the conversion from soluble functional proteins into insoluble amyloid are not fully understood. Many proteins that are not associated with disease can form amyloid with similar structural characteristics as the disease-associated fibrils, which highlights the potential risk of cross-seeding of disease amyloid by amyloid-like structures encountered in our surrounding. Of particular interest are common food proteins that can be transformed into amyloid under conditions similar to cooking. We here investigate cross-seeding of amyloid-beta (A beta), a peptide known to form amyloid during the development of Alzheimer's disease, by 16 types of amyloid fibrils derived from food proteins or peptides. Kinetic studies using thioflavin T fluorescence as output show that none of the investigated protein fibrils accelerates the aggregation of A beta. In at least two cases (hen egg lysozyme and oat protein isolate) we observe retardation of the aggregation, which appears to originate from interactions between the food protein seeds and A beta in aggregated form. The results support the view that food-derived amyloid is not a risk factor for development of A beta pathology and Alzheimer's disease.
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