On the structure of erythritol and L-threitol in the solid state: An infrared spectroscopic study

Jesus, A. J. Lopes; Redinha, J.S.

doi:10.1016/j.molstruc.2009.09.018

Cited by 13 publications

(5 citation statements)

References 25 publications

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“…At the same temperature, the spectrum of solid erythritol recrystallized from aqueous solution exhibits a rather complex pattern. Three fundamental OH stretching bands have been identified and assigned to the same number of intermolecular H-bonds (Jesus and Redinha, 2009). The two structures are significantly different in respect with the number of intermolecular H-bonds.…”

Section: Fourier Transform Infrared Spectroscopy (Ftir)mentioning

confidence: 99%

Erythritol: Crystal growth from the melt

Jesus

Nunes

Silva

et al. 2010

International Journal of Pharmaceutics

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Section: Fourier Transform Infrared Spectroscopy (Ftir)mentioning

confidence: 99%

Erythritol: Crystal growth from the melt

Jesus

Nunes

Silva

et al. 2010

International Journal of Pharmaceutics

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“…However, complexation decreased when the ERY concentration continued to increase beyond 20 mg/mL. Studies have shown that hydrogen bonding dominates in determining the physical properties of polyols (Jesus and Redinha 2009). Therefore, the decrease in the binding rate may have occurred because of hydrogen bonding disruption caused by the high concentration of ERY altering the WPI structure.…”

Section: Resultsmentioning

confidence: 99%

The influence of the interaction between whey protein and erythritol on protein conformation, interfacial properties and stability

Zhang,

Shao

et al. 2024

Int J of Dairy Tech

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This study investigated the impact of erythritol (ERY) on structural and functional properties of whey protein isolate (WPI). FTIR and CD revealed that WPI underwent structural changes, including formation of β‐folds and random coils, upon interaction with 20 mg/mL ERY. SEM showed increased surface roughness of WPI, indicating enhanced protein exposure. Moreover, binding rate exceeded 85%, accompanied by increased surface hydrophobicity. Fluorescence spectroscopy indicated a red shift in fluorescence of WPI and tyrosine (Tyr) residues, altering polarity of Tyr environment due to ERY coordination. Additionally, ERY presence enhanced the functional properties of WPI, including foaming, freeze–thaw stability, rheology and antioxidant activity.

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“…Another spectral manifestation of this interaction is the increase of the bandwidth and of its integrated intensity. Various methods can be used to obtain the reference spectrum of the molecule free from intermolecular hydrogen bonds (Jesus and Redinha 2009, Jesus, et al 2003, Jesus, et al 2006. Here, it has been calculated by applying quantum chemical methods to the monomer with the conformation exhibited in the crystalline structure.…”

Section: Characterization Of the Hydrogen Bond Network By Infrared Spmentioning

confidence: 99%

“…The occupancy percentages of the two conformations at 22.6 K are found to be 85% and 15%, respectively. Three types of hydrogen bonds have been identified: one of them is common to both conformations and connects the terminal OH groups, while the other two involve the middle OH groups of the conformations A or B, respectively (Ceccarelli, et al 1980, Jesus andRedinha 2009 This situation is more complicated in the beta-adrenergic compounds. Let us consider the crystalline structures of (R,S)-atenolol and betaxolol hydrochloride.…”

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confidence: 99%