DSC on ovalbumin-hematite “tempera” paints: the role of water and pigment on protein stability

Saitta, Francesca; Signorelli, Marco; Bramanti, Emilia; Pizzimenti, Silvia; Pelosi, Chiara; Duce, Celia; Fessas, Dimitrios; Bonaduce, Ilaria

doi:10.1016/j.tca.2020.178780

Cited by 11 publications

(6 citation statements)

References 39 publications

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“…Moreover, myoglobin’s transition appeared to be narrower, suggesting the early onset of the protein fluctuations caused by the covalent attachment of the polymers. This effect had been reported previously for protein–polymer conjugates in the dry state , and proteins in hydrated powders. , In analogy with previous techniques, we observed a more substantial reduction of protein stability with increasing the polymer hydrophobicity (Figure S6). The polymers’ molar mass did not seem to have a remarkable effect on the PEGylated conjugates (the differences are within the experimental error).…”

Section: Resultssupporting

confidence: 90%

Effect of Polymer Hydrophilicity and Molar Mass on the Properties of the Protein in Protein–Polymer Conjugates: The Case of PPEylated Myoglobin

2021

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Polyphosphoesters (PPEs), a versatile class of biodegradable and biocompatible polymers, have been proposed as alternatives to poly(ethylene glycol) (PEG), which is suspected to be responsible for anaphylactic reactions in some patients after the administration of PEGylated compounds, e.g., in the current Covid-19 vaccines. We present the synthesis and characterization of a novel set of protein–polymer conjugates using the model protein myoglobin and a set of PPEs with different hydrophilicity and molar mass. We report an extensive evaluation of the (bio)physical properties of the protein within the conjugates, studying its conformation, residual activity, and thermal stability by complementary techniques (UV–vis spectroscopy, nano-differential scanning calorimetry, and fluorometry). The data underline the systematic influence of polymer hydrophilicity on protein properties. The more hydrophobic polymers destabilize the protein, the more hydrophilic PPEs protect against thermally induced aggregation and proteolytic degradation. This basic study aims at guiding the design of future PPEylated drugs and protein conjugates.

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Section: Resultssupporting

confidence: 90%

Effect of Polymer Hydrophilicity and Molar Mass on the Properties of the Protein in Protein–Polymer Conjugates: The Case of PPEylated Myoglobin

2021

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“…On the other hand, the denaturation enthalpy was almost unaffected by the different moisture percentages and is ∆dH = (6.4 ± 0.6) J/gdry. The Tmax behaviour, i.e., the entropic stabilization of proteins in water-limiting conditions, is in line with the literature and was also observed for pure protein systems (Saitta et al, 2020). We may note that no exothermic phenomena (typical index for protein aggregation) were observed even at the lowest moisture content.…”

Section: Dsc Analysis Of Carob Flour and Its Constituentssupporting

confidence: 90%

Influence of carob flour ingredients on wheat-based systems

Saitta

Apostolidou

Παπαγεωργίου

et al. 2023

Journal of Cereal Science

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“…Indeed, lentils contain proteins with a distribution of different thermal stabilities [23]. Moreover, the thermal stability of globular proteins in complex systems is moisture-dependent and, in our DSC conditions (i.e., 60% moisture, 2 • C/min), a low-temperature onset of protein denaturation is plausible [24]. The overall enthalpy of these changes corresponds to ∆H raw = 10.5 ± 0.5 J/g dry .…”

Section: Thermal Analysis Highlights the Modification Of Both Starch ...mentioning

confidence: 90%

Impact of Thermal Treatment on the Starch-Protein Interplay in Red Lentils: Connecting Molecular Features and Rheological Properties

et al. 2022

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Thermal treatments are widely applied to gluten-free (GF) flours to change their functionality. Despite the interest in using pulses in GF formulations, the effects of thermal treatment at the molecular level and their relationship with dough rheology have not been fully addressed. Raw and heat-treated red lentils were tested for starch and protein features. Interactions with water were assessed by thermogravimetric analysis and water-holding capacity. Finally, mixing properties were investigated. The thermal treatment of red lentils induced a structural modification of both starch and proteins. In the case of starch, such changes consequently affected the kinetics of gelatinization. Flour treatment increased the temperature required for gelatinization, and led to an increased viscosity during both gelatinization and retrogradation. Regarding proteins, heat treatment promoted the formation of aggregates, mainly stabilized by hydrophobic interactions between (partially) unfolded proteins. Overall, the structural modifications of starch and proteins enhanced the hydration properties of the dough, resulting in increased consistency during mixing.

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DSC on ovalbumin-hematite “tempera” paints: the role of water and pigment on protein stability

Cited by 11 publications

References 39 publications

Effect of Polymer Hydrophilicity and Molar Mass on the Properties of the Protein in Protein–Polymer Conjugates: The Case of PPEylated Myoglobin

Effect of Polymer Hydrophilicity and Molar Mass on the Properties of the Protein in Protein–Polymer Conjugates: The Case of PPEylated Myoglobin

Influence of carob flour ingredients on wheat-based systems

Impact of Thermal Treatment on the Starch-Protein Interplay in Red Lentils: Connecting Molecular Features and Rheological Properties

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