Saccharide-based biopreservation is widely studied because of its scientific importance and possible technological outcomes for food and pharmaceutical industries. Ternary protein/saccharide/water systems have been extensively exploited to model the characteristics of the in vivo biopreservation process. A tight, water dependent, protein–matrix coupling has been shown to occur in various simple saccharide amorphous matrices, which is stronger in trehalose. The efficiency as bioprotectant of trehalose has been ascribed to this tight coupling, since the appearance of damages on biological structures will more involve structural variations of the surrounding matrix. Here we present, as an applicative follow-up of this research line, a Fourier transform infrared study on protein–matrix coupling in commercial maltodextrins and trehalosyldextrins solid amorphous systems, with carboxymyoglobin embedded, and compare the results with analogous system containing trehalose and maltose, previously reported. Results point out that trehalosyldextrins are useful candidates as protecting agents, even though with an efficiency lower than trehalose, and could be used when the rheological properties of relative long-chain oligosaccharides are needed.However, it appears that a substantial improvement could be obtained by removal of the small fraction of glucose.

Giuffrida, S., Troia, R., Schiraldi, C., D'Agostino, A., De Rosa, M., Cordone, L. (2011). MbCO embedded in trehalosyldextrin matrices: thermal effects and protein-matrix coupling. FOOD BIOPHYSICS, 6, 217-226 [10.1007/s11483-010-9197-5].

MbCO embedded in trehalosyldextrin matrices: thermal effects and protein-matrix coupling

GIUFFRIDA, Sergio;CORDONE, Lorenzo
2011-01-01

Abstract

Saccharide-based biopreservation is widely studied because of its scientific importance and possible technological outcomes for food and pharmaceutical industries. Ternary protein/saccharide/water systems have been extensively exploited to model the characteristics of the in vivo biopreservation process. A tight, water dependent, protein–matrix coupling has been shown to occur in various simple saccharide amorphous matrices, which is stronger in trehalose. The efficiency as bioprotectant of trehalose has been ascribed to this tight coupling, since the appearance of damages on biological structures will more involve structural variations of the surrounding matrix. Here we present, as an applicative follow-up of this research line, a Fourier transform infrared study on protein–matrix coupling in commercial maltodextrins and trehalosyldextrins solid amorphous systems, with carboxymyoglobin embedded, and compare the results with analogous system containing trehalose and maltose, previously reported. Results point out that trehalosyldextrins are useful candidates as protecting agents, even though with an efficiency lower than trehalose, and could be used when the rheological properties of relative long-chain oligosaccharides are needed.However, it appears that a substantial improvement could be obtained by removal of the small fraction of glucose.
2011
Settore CHIM/02 - Chimica Fisica
Settore FIS/07 - Fisica Applicata(Beni Culturali, Ambientali, Biol.e Medicin)
Giuffrida, S., Troia, R., Schiraldi, C., D'Agostino, A., De Rosa, M., Cordone, L. (2011). MbCO embedded in trehalosyldextrin matrices: thermal effects and protein-matrix coupling. FOOD BIOPHYSICS, 6, 217-226 [10.1007/s11483-010-9197-5].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10447/55051
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