Functional fungal extracts from the Quorn fermentation co-product as novel partial egg white replacers

Replaced AM with VoR 2020-01-17The production of mycoprotein biomass by Marlow Foods for use in their meat alternative brand Quorn is a potential source of sustainable alternatives to functional ingredients of animal origin for the food industry. The conversion of this viscoelastic biomass into the Quorn meat-like texture relies on functional synergy with egg white (EW), effectively forming a fibre gel composite. In a previous study we reported that an extract (retentate 100 or R100) obtained from the Quorn fermentation co-product (centrate) via ultrafiltration displayed good foaming, emulsifying and rheological properties. This current study investigated if a possible similar synergy between EW and R100 could be exploited to partially replace EW as foaming and/or gelling ingredient. The large hyphal structures characteristic of R100 solutions were observed in EW-R100 mixtures, while EW-R100 gels showed dense networks of entangled hyphal aggregates and filaments. R100 foams prepared by frothing proved less stable than EW ones, however a 75/25 w/w EW-R100 mixture displayed a similar foam stability to EW. Simlarly R100 hydrogels proved less viscoelastic than EW ones, however the viscoelasticity of gels prepared with 50/50 w/w and 75/25 w/w EW-R100 proved similar to those of EW gels while 75/25 w/w EW-R100 gels displayed similar hardness to EW ones. Both results highlighted a functional synergy between the R100 material and EW proteins. In parallel tensiometry measurements highlighted the presence of surface-active material in EW-R100 mixtures contributing to their high foaming properties. These results highlighted the potential of functional extracts from the Quorn fermentation process for partial EW replacement as foaming and gelling agent, and the complex nature of the functional profile of EW-R100 mixtures, with contributions reported for both hyphal structures and surface-active material.This work was supported by the Engineering and Physical Sciences Research Council [grant number EP/J501682/1 Foaming and Fat Replacer Ingredients].https://doi.org/10.1007/s00217-019-03390-1246pubpu

Molecular simulation of partially denatured β-lactoglobulin

From Elsevier via Jisc Publications RouterHistory: accepted 2023-04-22, issued 2023-04-29Article version: AMPublication status: AcceptedFunder: Heriot-Watt University; FundRef: https://doi.org/10.13039/100009767Funder: Engineering & Physical Sciences Research Council; Grant(s): EP/J501682/1Julien Lonchamp - ORCID: 0000-0001-7954-4745 https://orcid.org/0000-0001-7954-4745The unfolding of β-lactoglobulin (β-lac) upon heating was comprehensively studied through molecular dynamics computer simulations. A β-lac molecule in the aqueous solution was firstly heated at 500 K for unfolding and then annealed at 300 K to collect stable conformations. There were five meta-stable conformations observed based on the Free Energy Landscape (FEL). The β-lac molecule was found to exhibit an open and extended conformation on heating followed by limited refolding upon cooling. The cysteine residues –SH121 and S–S66-160 in the most open conformation were located at the opposite ends of the β-lac molecule. This would favour the intermolecular –SH/S–S interchange reactions that are known to occur in β-lac as part of the inter-molecular aggregation process. Furthermore, the unfolding of the β-lac increased the hydrogen bond forming capacity between water molecules and the protein and between water molecules themselves. The interactions and the properties of the water molecules in the protein hydration shell also indicated that the hydration shell was stabilized by protein unfolding. However, it was found that the unfolding of β-lac increased diffusion of hydration water molecules, including those in the first hydration shell that interact more strongly with the protein. This may partly explain why unfolded proteins are more likely to aggregate even though there were more hydration water molecules protecting them. Such results provided more detailed information on the structure-functionality relationship of β-lac based on both the protein molecule and its hydration shell. This provides insight into how we can control the processing of proteins for desirable functional properties such as thickening and gelation, which are modified through protein-water interactions.inpressinpres

Electrostatic complexes of whey protein and pectin as foaming and emulsifying agents

Five types of electrostatic complex (macromolecular complexes, core-shell particles, and mixed homogeneous particles) were formed between whey protein (whey protein concentrate [WPC]) and pectin. By controlling the thermal treatment, composition, and order of mixing, it was possible to produce complexes that for the same biopolymer concentration gave differing functional properties. All protein-pectin complexes showed higher foaming ability and stability than native or heated WPC without pectin. Native WPC had higher emulsifying ability than protein-pectin complexes but exhibited the lowest emulsion stability. Ingredients based on such ideas might offer the food manufacturer greater control over food structure, stability, and organoleptic properties.sch_die20pub5156pubsup

The major proteins of the seed of the fruit of the date palm (phoenix dactylifera l.): Characterisation and emulsifying properties

Proteins were extracted from the seeds of the fruit of the date palm. Proteomic analysis and SDS-PAGE electrophoresis of the extracted proteome suggested it is composed predominantly of the storage proteins glycinin and β-conglycinin, although over 300 proteins were detected, 91 of which were identified with confidence. In terms of protein type, the largest numbers of proteins were associated, not unexpectedly, with metabolism and energy functions, which reflected the requirements of the germinating and growing embryonic plant. The emulsifying properties of the extracted proteins were determined. Date seed protein exhibited a lower emulsifying activity than either whey protein concentrate or soy protein isolate at each of the pH values tested. However, the stability of the emulsions produced with all three proteins was very similar at the different pH values. This combination of large emulsion droplet size and high emulsion stability properties suggested that the date proteins may adsorb as large protein oligomers.https://doi.org/10.1016/j.foodchem.2015.11.046197pubpu

Properties of partially denatured whey protein products: Viscoelastic properties

Partially denatured whey protein products (PDWPC's) can be classified based on the viscoelastic properties of their solutions. Strain sweeps show that PDWPC-A and -B and microparticulated WPC (MPWPC) with compact, spherical aggregated particles exhibit a strong strain overshoot. PDWPC-C and -D, on the other hand, which have open, elongated porous particles show a weak strain overshoot. The concentration dependence of the elastic modulus G' in the linear viscoelastic region has a biphasic power law dependence with concentration for all protein products studied, except for WPC where G' is independent of protein concentration. Frequency sweeps suggest that MPWC solutions form a strong physical gel at all concentrations above 14% (w/w). PDWPC-A and -B form weak gels over the same concentration range. PDWPC-C and -D also form weak gels at 14% protein (w/w) but strong physical gels at higher concentrations. The frequency dependence of G' and G'' for all aggregated proteins show a power law dependence indicating fractal type structures. For all solutions above a critical concentration, the fractal dimensions span the range 1.6-2.3, indicating a range of gel network structures from open and diffuse to compact and dense. Adherence to the empirical Cox-Merz rule was observed in PDWPC-A, -C and -D at concentrations of 14 and 16% (w/w) protein, suggesting liquid-like behaviour. At higher protein concentrations the deviations from the Cox-Merz rule suggest more pronounced elasticity in the structure. For PDWPC-B, the behaviour is complex, with deviation from the Cox-Merz rule at low frequencies/shear rates, but correspondence at higher frequencies/shear rates at all concentrations. This indicates a frequency-dependent change from liquid-like behaviour over long timescale deformations, to a solid-like behaviour at short timescale deformations. MPWPC solutions of all concentrations do not follow the Cox-Merz rule, suggesting solid-like behaviour. The PDWPCs exhibit a complex rheological behaviour which suggests they could be versatile thickening, texturizing and fat replacementsch_die80pub5157pu

Properties of partially denatured whey protein products: Formation and characterisation of structure

Item previously deposited in Heriot-Watt University repository: https://researchportal.hw.ac.uk/en/publications/properties-of-partially-denatured-whey-protein-products-formationPartially denatured whey protein (PDWPC) products have been manufactured using a controlled heating process that allows control of the degree of denaturation of the whey proteins. This is assessed by following the change in free sulphydryl content of the protein as heating progresses. This allows the formation of soluble whey protein aggregates of diverse particle size and morphology. The PDWPC's have been made using different manufacturing conditions (temperature, pH, degree of denaturation) to give aggregated PDWPC powders with a degree of denaturation in the range 45–98% and particle size 3–17 μm. Particle size analysis, scanning electron microscopy and density analysis show that the particles have aggregated structures that range from compact, particulate gel-like to fibrillar phase-separated structures, with intermediate structures formed under some conditions. These structures are consistent with the known gel structures formed in whey protein concentrate gels. The structure of the PDWPC particles differs from that of microparticulated whey proteins. The possibility of using PDWPC's as ingredients tailored to the needs of food manufacturers is discussed.https://doi.org/10.1016/j.foodhyd.2015.06.00952pubpu

Properties of partially denatured whey protein products 2: Solution flow properties

Partial denaturation of whey protein concentrates has been used to make protein powders with differing viscosity properties. PDWPC particles have been manufactured to have a range of aggregate sizes (3.3–17 μm) and structures (compact particle gel to open fibrillar gel). In solution the PDWPC samples show complex viscosity behaviour dependant on the size and morphology of the PDWPC aggregate particles. For the same protein content the compact particles have a lower viscosity than open, fibrillar particles. The viscosity also appears to depend on the surface structure of the particles, with particles of a similar size, but having a rougher surface giving higher viscosity than similar smooth particles. The viscosity of the WPC, MPWPC and PDWPC solutions are explained in terms of the postulated interactions between the protein aggregates in solution.Engineering & Physical Sciences Research Council grant No. EP/J501682/1.https://doi.org/10.1016/j.foodhyd.2015.12.01256pubpu

Novel palm shortening substitute using a combination of rapeseed oil, linseed meal and beta-glucan

This study investigated the potential of a novel sustainable ingredient composed of rapeseed oil, linseed meal and beta-glucan (PALM-ALT) to mimic palm shortening functionality in cake. The combined functional properties of linseed meal and beta-glucan led to stable semi-solid emulsion-gels (20–31 μm oil droplet size, 105–115 Pa.s viscosity and 60–65 Pa yield stress). PALM-ALT contained 25 and 88% less total and saturated fat than palm shortening, whilst PALM-ALT cakes contained 26 and 75% less total and saturated fat than the palm-based control. PALM-ALT cakes matched the flavour profile of the palm-based control, while rapeseed oil cakes tasted more sour and less sweet than the control (p < 0.05). PALM-ALT cakes proved less hard and more cohesive than the control (p < 0.05), with 100% of the consumer panel preferring PALM-ALT formulations. This study demonstrated the unique potential of PALM-ALT as healthier, sustainable and competitive alternative to palm shortening.https://doi.org/10.1016/j.foodchem.2024.140134457pubpu

Experimental Induction of Paromomycin Resistance in Antimony-Resistant Strains of L. donovani: Outcome Dependent on In Vitro Selection Protocol

Paromomycin (PMM) has recently been introduced for treatment of visceral leishmaniasis in India. Although no clinical resistance has yet been reported, proactive vigilance should be warranted. The present in vitro study compared the outcome and stability of experimental PMM-resistance induction on promastigotes and intracellular amastigotes. Cloned antimony-resistant L. donovani field isolates from India and Nepal were exposed to stepwise increasing concentrations of PMM (up to 500 µM), either as promastigotes or intracellular amastigotes. One resulting resistant strain was cloned and checked for stability of resistance by drug-free in vitro passage as promastigotes for 20 weeks or a single in vivo passage in the golden hamster. Resistance selection in promastigotes took about 25 weeks to reach the maximal 97 µM inclusion level that did not affect normal growth. Comparison of the IC50 values between the parent and the selected strains revealed a 9 to 11-fold resistance for the Indian and 3 to 5-fold for the Nepalese strains whereby the resistant phenotype was also maintained at the level of the amastigote. Applying PMM pressure to intracellular amastigotes produced resistance after just two selection cycles (IC50 = 199 µM) compared to the parent strain (IC50 = 45 µM). In the amastigote-induced strains/clones, lower PMM susceptibilities were seen only in amastigotes and not at all in promastigotes. This resistance phenotype remained stable after serial in vitro passage as promastigote for 20 weeks and after a single in vivo passage in the hamster. This study clearly demonstrates that a different PMM-resistance phenotype is obtained whether drug selection is applied to promastigotes or intracellular amastigotes. These findings may have important relevance to resistance mechanism investigations and the likelihood of resistance development and detection in the field