Geopolymers
Inorganic polymeric new materials
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Michele Iafisco
Michele Iafisco
Dipartimento di Chimica “G. Ciamician”, Alma Mater Studiorum, Università di Bologna, Via Selmi 2, 40126, Bologna, Italy
Dipartimento di Scienze Mediche, Università del Piemonte Orientale, Via Solaroli 4, 28100, Novara, Italy ismaela.foltran@unibo.it
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Dipartimento di Scienze Mediche, Università del Piemonte Orientale, Via Solaroli 4, 28100, Novara, Italy ismaela.foltran@unibo.it
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Ismaela Foltran
Ismaela Foltran
Dipartimento di Chimica “G. Ciamician”, Alma Mater Studiorum, Università di Bologna, Via Selmi 2, 40126, Bologna, Italy
Dipartimento di Scienze Mediche, Università del Piemonte Orientale, Via Solaroli 4, 28100, Novara, Italy ismaela.foltran@unibo.it
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Dipartimento di Scienze Mediche, Università del Piemonte Orientale, Via Solaroli 4, 28100, Novara, Italy ismaela.foltran@unibo.it
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Michele Di Foggia
Michele Di Foggia
Dipartimento di Biochimica ‘G. Moruzzi’ Alma Mater Studorium, Università di Bologna, Via Belmeloro 8/2, 40126, Bologna, Italy
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Sergio Bonora
Sergio Bonora
Dipartimento di Biochimica ‘G. Moruzzi’ Alma Mater Studorium, Università di Bologna, Via Belmeloro 8/2, 40126, Bologna, Italy
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Norberto Roveri
Norberto Roveri
Dipartimento di Chimica “G. Ciamician”, Alma Mater Studiorum, Università di Bologna, Via Selmi 2, 40126, Bologna, Italy
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Abstract
Lactoferrin (LF), a non-heme iron-binding protein of blood plasma and milk with antioxidant, cariostatic, anticarcinogenic, and anti-inflammatory properties, has been studied by differential scanning calorimetry (DSC) and Raman spectroscopy over a wide pH range (4.0–9.0). Using these two techniques, the modifications in the quantity of iron bounded in the cow's milk LF and in the secondary structures, as a function of pH and heating, have been evaluated. DSC curves showed higher value of denaturation temperatures and enthalpy changes when LF was saturated with iron (holo-form) than when it was in its unsaturated form (apo-form). The denaturation curves of the protein solutions at pH ≥ 5.5 confirming that LF is a mix of apo- and holo-forms; on the contrary at pH 4.0, the holo-form is practically absent. Spectroscopic investigation showed that, as a function of pH, the content of α-helix increases up to pH 7.4, followed by a small decrease by further pH increase. The β-sheet percentage exhibits the opposite behavior, while the random-coil and turn structures do not change noticeably. In contrast, after heat-induced denaturation, strong variations were observed in the secondary structure, with an evident increase of β-sheet and decrease of the α-helix percentage. Finally, both thermal and spectroscopic analysis pointed out that the structure of cow's milk LF is strictly sensible to pH variation and it has the highest thermal stability at physiological pH.
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| Journal of Thermal Analysis and Calorimetry | |
|---|---|
| Language | English |
| Size | A4 |
| Year of Foundation |
1969 |
| Volumes per Year |
1 |
| Issues per Year |
24 |
| Founder | Akadémiai Kiadó |
| Founder's Address |
H-1117 Budapest, Hungary 1516 Budapest, PO Box 245. |
| Publisher | Akadémiai Kiadó Springer Nature Switzerland AG |
| Publisher's Address |
H-1117 Budapest, Hungary 1516 Budapest, PO Box 245. CH-6330 Cham, Switzerland Gewerbestrasse 11. |
| Responsible Publisher |
Chief Executive Officer, Akadémiai Kiadó |
| ISSN | 1388-6150 (Print) |
| ISSN | 1588-2926 (Online) |
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Temperature dependence of the rate of reaction in thermal analysis
The Arrhenius equation in condensed phase kinetics
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