Neutron scattering and HPLC study on l-ascorbic acid and its degradation

Bellocco, Ersilia; Barreca, Davide; Laganà, Giuseppina; Leuzzi, Ugo; Migliardo, F.; Torre, R. La; Galli, G.; Galtieri, Antonio; Minutoli, Letteria; Squadrito, Francesco

doi:10.1016/j.chemphys.2007.07.006

Cited by 14 publications

(2 citation statements)

References 15 publications

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“…One arises from the fact that the incoherent scattering cross section of 1 H is much higher than 2 H [16], and this makes it possible to differentiate between the dynamics of hydrogen nuclei that are differently labeled in an inelastic neutron scattering experiment. Such experiments have been performed on food-relevant systems like proteins [17], saccharides [18][19][20], vitamins [21], and even on food products such as fruits and vegetables [22] or bread [23]. The other arises from the fact that the coherent cross section of 1 H and 2 H are very different [16], and this means that selectively deuterating either the solvent or the dispersed phase makes it possible to determine the distribution of species.…”

Section: Introductionmentioning

confidence: 99%

An alternative analysis of contrast-variation neutron scattering data of casein micelles in semi-deuterated milk

Smith

2021

Eur. Phys. J. E

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Contrast-variation small-angle neutron scattering (CV-SANS) is an excellent way to determine the structure of complex, hierarchical colloids, including self-assembled biological systems. In these experiments, the scattering length density of solvents is changed (by varying the ratio of water or H2O and heavy water or D2O) to highlight or mask scattering from different components in the system. This approach has been used with synthetic colloids, but it is also increasingly being used in the biological and food sciences. Perhaps the most studied food colloid is the "casein micelle", a self-assembled nanometer-scale colloid of the structure-forming casein protein in milk. CV-SANS data available in the literature are typically analyzed using approximations, which may be invalid for casein micelles, as they have been shown to be sticky spheres. To assess the applicability of this approximate approach, a comprehensive set of CV-SANS data from casein micelles in diluted milk was reanalyzed using a model-based approach, where the casein micelles were formally treated as interacting spheres. In general, the conclusions of the previous study are reproduced, but this new approach makes it more straightforward to distinguish the different components in milk and can be applied to any dairy sample with known form of interparticle interactions, which offers the possibility of studying semi-deuterated milk at its native concentration.

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Section: Introductionmentioning

confidence: 99%

An alternative analysis of contrast-variation neutron scattering data of casein micelles in semi-deuterated milk

Smith

2021

Eur. Phys. J. E

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“…L-ascorbic acid (L-threo-2-hexenono-1,4-lactone), also known as vitamin C, is a water soluble vitamin with many health benefits, such as photo protection, melanin reduction and scavenging of free radicals (Bellocco et al, 2008;Liu et al, 2011). These functions are closely related to the well-known beneficial and antioxidant properties of this compound as shown by epidemiological studies (Flagg et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

Simultaneous Determination of L-Ascorbic Acid and L-Ascorbylpalmitate Using RP-HPLC Method

Tian

Wang

Leng

et al. 2013

AMR

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A rapid reversed phase highperformance liquid chromatography (RP-HPLC) method was developed for the simultaneous analysis of L-ascorbic acid and L-ascorbylpalmitate (AP). The chromatography was performed on a SSI model 2300-525 high performance liquid chromatographequipped with anAlltechApollo C18 column at 30 oC.The mobile phase was acetonitrile-water (90:10,v/v) with the flow rate of 1.0 mL/min. UV detection wavelength was 250 nm. This method permits the simultaneous determination of ascorbic acid and AP in the synthesis of AP transesterified with methyl palmitate and ascorbic acid. The detection limit of ascorbic acid and AP was 0.07μg/mL and 0.12μg/mL, respectively. The recovery was 90.59 ± 3.04% for ascorbic acid and 101.3 ± 4.81% for AP. The linearity range for ascorbic acid and AP was in the range of 0.1 - 0.7 mg/mL and 0.4 - 4.0 mg/mL, respectively. Correlation coefficients (R2) were 0.9910 for ascorbic acid and 0.9986 for AP. The proposed method could be used for routine quality control of AP synthesis with methyl palmitate and ascorbic acidby enzymatic transesterification.

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Spectroscopic Determination of Lysozyme Conformational Changes in the Presence of Trehalose and Guanidine

Barreca

Laganà

Ficarra

et al. 2012

Cell Biochem Biophys

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The bioprotective action of the disaccharide trehalose has been studied against the well-known denaturating agent, guanidine hydrochloride. The results indicated a direct influence of trehalose on both enzymatic activity and conformational changes of lysozyme, as shown by the decrease of the inactivation rate constant of about 1.48-fold and the loss of α-helix structure of lysozyme. In addition, ESI-MS hydrogen-deuterium (H/D) exchange experiments allowed us to correlate the structural and dynamic features of the protein in the presence of the two additives, highlighting as trehalose remarkably influenced this exchange by decreasing local protein environment changes and solvent accessibility to the amide peptide backbone, as further evidenced by circular dichroism and (1)H NMR measurements.

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Neutron scattering and HPLC study on l-ascorbic acid and its degradation

Cited by 14 publications

References 15 publications

An alternative analysis of contrast-variation neutron scattering data of casein micelles in semi-deuterated milk

An alternative analysis of contrast-variation neutron scattering data of casein micelles in semi-deuterated milk

Simultaneous Determination of L-Ascorbic Acid and L-Ascorbylpalmitate Using RP-HPLC Method

Spectroscopic Determination of Lysozyme Conformational Changes in the Presence of Trehalose and Guanidine

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