Towards recombinantly produced milk proteins: Physicochemical and emulsifying properties of engineered whey protein beta-lactoglobulin variants

Keppler, Julia K.; Heyse, Anja; Scheidler, Eva; Uttinger, Maximilian J.; Fitzner, Laura; Jandt, Uwe; Heyn, Timon R.; Lautenbach, Vanessa; Loch, J.I.; Lohr, Jonas; Kieserling, Helena; Günther, Gabriele; Kempf, Elena; Grosch, Jan Hendrik; Lewiński, K.; Jahn, Dieter; Lübbert, Christian; Peukert, Wolfgang; Kulozik, Ulrich; Drusch, Stephan; Krull, Rainer; Schwarz, Karin; Biedendieck, Rebekka

doi:10.1016/j.foodhyd.2020.106132

Cited by 35 publications

(29 citation statements)

References 78 publications

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“…The dominating proteins in WPI are β-LG and α-lactalbumin (Foegeding et al, 2011). The interfacial tension of β-LG was 15.3 ± 0.2 mN/m whereby a similar value was reported earlier for the same interfacial system (Keppler et al, 2021). The interfacial tension of 0.1% αlactalbumin at pH 7 against oil was reported to be 15 mN/m as well Phase angle (°) 6.9 ± 0.7 5.1 ± 0.5 9.5 ± 0.9 10.0 ± 1.0 TA B L E 3 Interfacial tension and phase angle of 0.1 % β-LG with addition of 0.005 % Lecithin, Citrem or MoDi at MCT-oil/ water-interface after 14 h drop ripening and at 2.8 % amplitude and 0.01 Hz (Lam & Nickerson, 2015).…”

Section: Interfacial Tension and Dilatational Rheology Influenced By Lmwesupporting

confidence: 87%

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Spray drying of emulsions: Influence of the emulsifier system on changes in oil droplet size during the drying step

Taboada

Heiden-Hecht

Brückner-Gühmann

et al. 2021

J. Food Process. Preserv.

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Section: Interfacial Tension and Dilatational Rheology Influenced By Lmwesupporting

confidence: 87%

“…β-LG shows a viscoelastic behavior (Table 3) comparable to previous studies (Böttcher et al, 2017;Keppler et al, 2021). The phase angle of 6.9 ± 0.7° indicates a high elastic portion in the interfacial film.…”

Section: Interfacial Tension and Dilatational Rheology Influenced By Lmwesupporting

confidence: 84%

Spray drying of emulsions: Influence of the emulsifier system on changes in oil droplet size during the drying step

Taboada

Heiden-Hecht

Brückner-Gühmann

et al. 2021

J. Food Process. Preserv.

Self Cite

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show abstract

“…Generally stated the functional properties of readily available ingredients are not optimised for meat analogue applications, since their fractionation processes were designed before this application became important. It is therefore interesting to investigate options to tune the properties of these ingredients towards meat analogue applications, by blending ingredients (for example proteins with polysaccharides) or by inducing modification through post-treatments (inducing covalent interactions during processing for example [ 164 ]).…”

Section: Plant-based Ingredients For Meat Analoguesmentioning

confidence: 99%

“…There are additionally new developments on protein sources concerning recombinant or cellular agriculture, which use fungi, yeast and bacteria for the production of animal proteins or for proteins that are natural for the microorganism. However, also for this downstream processing and determination of their functional properties are still subjects to recent research [ 164 ].…”

Section: Steps For the Production Of The Future Meat Analoguesmentioning

confidence: 99%

Functionality of Ingredients and Additives in Plant-Based Meat Analogues

Kyriakopoulou

Keppler

Goot

2021

Foods

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355

197

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Meat analogue research and development focuses on the production of sustainable products that recreate conventional meat in its physical sensations (texture, appearance, taste, etc.) and nutritional aspects. Minced products, like burger patties and nuggets, muscle-type products, like chicken or steak-like cuts, and emulsion products, like Frankfurter and Mortadella type sausages, are the major categories of meat analogues. In this review, we discuss key ingredients for the production of these novel products, with special focus on protein sources, and underline the importance of ingredient functionality. Our observation is that structuring processes are optimized based on ingredients that were not originally designed for meat analogues applications. Therefore, mixing and blending different plant materials to obtain superior functionality is for now the common practice. We observed though that an alternative approach towards the use of ingredients such as flours, is gaining more interest. The emphasis, in this case, is on functionality towards use in meat analogues, rather than classical functionality such as purity and solubility. Another trend is the exploration of novel protein sources such as seaweed, algae and proteins produced via fermentation (cellular agriculture).

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“…The solubility values were obtained by the proteins equilibration time was set to 120 s. The zeta potential is correlated with the proteins' net surface charge (Keppler et al, 2021), hence, the pH value for which the measured zeta potential value reaches 0 mV was determined as the bulk IEP of the corresponding protein.…”

Section: Zeta Potential Measurementsmentioning

confidence: 99%

Isoelectric Point of Proteins at Hydrophobic Interfaces

2021

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Structural and colloidal stability of proteins at different surfaces and interfaces is of great importance in many fields including medical, pharmaceutical, or material science. Due to their flexibility, proteins tend to respond to their environmental conditions and can undergo structural and conformational changes. For instance, alterations in physiological factors such as temperature, ions concentration, or pH as well as the adsorption to an interface can initiate protein aggregation. Therefore, at different surfaces and interfaces the characterization of the structural and colloidal stability of proteins, which is mainly influenced by their electrostatic and hydrophobic interactions, is of fundamental importance. In this study, we utilized sum frequency generation (SFG) spectroscopy to assess the role of solution pH on the polarity and magnitude of the electric field within the hydration shell of selected model proteins adsorbed to a hydrophobic surface. We used polystyrene (PS) as a model hydrophobic surface and determined the isoelectric point (IEP) of four structurally different model proteins. Comparing the measured IEP of proteins at the PS/solution or air/solution interface with that determined in the bulk solution via zeta potential measurement, we found significant similarities between the IEP of surface adsorbed proteins and those in the bulk aqueous phase. The pH dependence behavior of proteins was correlated to their amino acid composition and degree of hydrophobicity.

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Towards recombinantly produced milk proteins: Physicochemical and emulsifying properties of engineered whey protein beta-lactoglobulin variants

Cited by 35 publications

References 78 publications

Spray drying of emulsions: Influence of the emulsifier system on changes in oil droplet size during the drying step

Spray drying of emulsions: Influence of the emulsifier system on changes in oil droplet size during the drying step

Functionality of Ingredients and Additives in Plant-Based Meat Analogues

Isoelectric Point of Proteins at Hydrophobic Interfaces

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