Are Citric Acid-Iron II Complexes True Chelates or Just Physical Mixtures and How to Prove This?

Although mineral chelates are widely produced to be used as food fortifiers, the proof that these complexes are chelates is still missing. In our present work, iron II complexes using citric acid in different ratios are produced, and the occurrence of chelation is investigated along with its behavior according to a molar ratio between the ligand and the mineral. High performance liquid chromatography (HPLC), flame atomic absorption spectroscopy (FAAS), ultraviolet-visible spectroscopy (UV-Vis), Fourier-transform infrared (FTIR), and near infrared spectroscopy (NIR) were used for a non-structural characterization of these complexes.

Preparing a Personalized Meal by Using Soy, Cricket, and Egg Albumin Protein Based on 3D Printing.

Recently, personalized meals and customized food design by means of 3D printing technology have been considered over traditional food manufacturing methods. This study examined the effects of different proteins (soy, cricket, and egg albumin protein) in two concentrations (3% and 5%) on rheological, textural, and 3D printing characteristics. The textural and microstructural properties of different formulations were evaluated and compared.

The effect of borage, ginger and fennel extracts on acrylamide formation in French fries in deep and electric air frying.

The aim of this study was to evaluate the effect of three Lebanese wild plant extracts on acrylamide (AA) content in French fries, and to investigate the impact of air frying (AF) and deep frying (DF) techniques against AA formation. HPLC showed higher level of AA in DF (1384.79 ng/g) than in AF (163.

Assessing Mechanical and Rheological Properties of Potato Puree: Effect of Different Ingredient Combinations and Cooking Methods on the Feasibility of 3D Printing.

The effects of agar, alginate, butter, olive oil, and carrots on the mechanical and rheological properties of potato puree prepared by two different cooking methods (microwave heating (MP) and boiling (BP)) were investigated and interpreted in terms of starch microstructural changes. Microscopic observations revealed more aggregated and densely concentrated starch granules in MP samples. This consequently led to a significant increase ( < 0.

The Membrane Proximal Domain of TRPV1 and TRPV2 Channels Mediates Protein⁻Protein Interactions and Lipid Binding In Vitro.

Constitutive or regulated membrane protein trafficking is a key cell biology process. Transient receptor potential channels are somatosensory proteins in charge of detecting several physical and chemical stimuli, thus requiring fine vesicular trafficking. The membrane proximal or pre-S1 domain (MPD) is a highly conserved domain in transient receptor potential channels from the vanilloid (TRPV) subfamily.

Characterization of food additive-potato starch complexes by FTIR and X-ray diffraction.

Fourier-transform infrared spectroscopy (FTIR) and X-ray diffraction (XRD) techniques were used to study the effect of four food additives, agar, alginate, lecithin and glycerol, at three different concentrations, 0.5, 1 and 1.5%, on the molecular structure of potato puree prepared from commercial potato powder.

Assessing the microstructural and rheological changes induced by food additives on potato puree.

The effects of agar, alginate, lecithin and glycerol on the rheological properties of commercial potato puree were investigated and interpreted in terms of starch microstructural changes, and the applicability of the Cox-Merz rule was evaluated. Each additive was applied separately at two concentrations (0.5 and 1%).

Combination of extended X-ray absorption fine structure spectroscopy with lipidic cubic phases for the study of cation binding in bacteriorhodopsin.

We have performed a quantitative X-ray absorption fine structure analysis of bacteriorhodopsin in purple membrane patches and in lipidic cubic phases regenerated with Mn(2+). Lipidic cubic phases and purple membrane results have been compared, demonstrating that the lipidic cubic phase process does not introduce relevant distortions in the local geometry of the cation binding sites. For both samples, we have observed similarities for Mn(2+) coordination in terms of type, number, and average distances of surrounding atoms, indicating a first coordination shell composed by 6 O atoms, and 3/4 C atoms located in the second coordination shell.

Structural characterization of a zinc high-affinity binding site in rhodopsin.

For the first time to our knowledge, X-ray absorption spectroscopy (XAS) has been used to investigate the environment of putative Zn(2+) binding sites in rhodopsin. We studied native purified nondeionized rhodopsin without any further addition of Zn(2+), as well as with 1.5 mol of Zn(2+)-as zinc chloride-per mole of protein.

X-ray absorption and molecular dynamics study of cation binding sites in the purple membrane.

The present work describes the results of a study aimed at identifying candidate cation binding sites on the extracellular region of bacteriorhodopsin, including a site near the retinal pocket. The approach used is a combined effort involving computational chemistry methods (computation of cation affinity maps and molecular dynamics) together with the Extended X-Ray Absorption Fine Structure (EXAFS) technique to obtain relevant information about the local structure of the protein in the neighborhood of Mn(2+) ions in different affinity binding sites. The results permit the identification of a high-affinity binding site where the ion is coordinated simultaneously to Asp212(-) and Asp85(-).

A quantitative XANES analysis of the calcium high-affinity binding site of the purple membrane.

In this article we report x-ray absorption measurements of Ca(2+)-substituted bacteriorhodopsin. We present a detailed study of the absorption spectrum close to the absorption edge that is very sensitive to the site geometry. We combined ab initio calculations of the x-ray absorption cross section based on a full multiple scattering approach, with a best fit of the experimental data performed by changing the cluster geometry.

Specific effects of chloride on the photocycle of E194Q and E204Q mutants of bacteriorhodopsin as measured by FTIR spectroscopy.

Low-temperature Fourier transform infrared spectroscopy has been used to study mutants of Glu194 and Glu204, two amino acids that are involved in proton release to the extracellular side of bacteriorhodopsin. Difference spectra of films of E194Q, E204Q, E194Q/E204Q, E9Q/E194Q/E204Q, and E9Q/E74Q/E194Q/E204Q at 243, 277, and 293 K and several pH values were obtained by continuous illumination. A specific effect of Cl(-) ions was found for the mutants, promoting a N-like intermediate at alkaline pH and an O' intermediate at neutral or acid pH.