ethanol (2)

It is very difficult to verify, by testing honey, whether bees have been fed with C3-derived sugar syrups during the foraging season.  Sugar-feeding is not permitted unless over winter to keep the bees alive.

 In this study (open access), the researchers set out to show the potential for discrimination of sugar-fed hives using the non-exchangeable hydrogen isotope ratios on ethanol derived from honey, measured using mass spectrometry (ethanol isotope ratios are the same discriminator that underpin the proprietary SNIF-NMR databases that have been accepted for many years for fruit juice authenticity testing and have also been applied to honey)

 To generate reference samples, 36 genetically similar bee colonies, at a single geographical location and time point, were subject to different controlled sugar feeding regimes.  Four different sugar syrup types were used to represent distinct adulteration scenarios: fructose and glucose syrups derived from C4 plants, invert sugar derived from C3 plants (sugar beet), and sucrose syrup of unknown botanical origin.  Controls were in place to stop the colonies cross-feeding.

 The authors report that Ethanol δDn values for adulterated samples differed significantly from controls, enabling clear discrimination.  This discrimination could form the basis of a potential classification database.

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12633554080?profile=RESIZE_400xDifferentiating gelatin species is an analytical challenge because of a lack of intact DNA.  Most speciation methods therefore target the profile of proteins.  Proteins are difficult to analyse - they are too large to measure directly by techniques such as LC-MS, without  prior breaking down, and their folded structure is also an important diagnostic parameter.  This structure is disrupted by many of the sampling and extraction procedures used in analytical method. Analysis of mixed gelatins is particularly difficult.

This method (open access) used a new approach based on the interaction of ethanol with amino acids inside a protein. Ethanol can denature globular proteins by disrupting intraprotein hydrogen bonds due to hydrophobic interactions. However, when added to solutions having proteins with considerable number of α-helices, ethanol can stabilize the protein structure and prevent aggregation. The specific effects of ethanol on protein structure and function can vary depending on the protein's composition and environment.

Attenuated Total Reflectance-Fourier Transform Infrared (ATR-FTIR) spectroscopy was used to leverage ethanol's differential effects on gelatin's amide bands for quantifying pork gelatin contamination in bovine gelatin.

The authors report that the method showed a strong linear correlation between contamination levels and amide band transmission, with detection and quantification limits of 0.85 and 2.85 mg/100 mg (pork in bovine), respectively. It effectively identified pork gelatin in halal candy, with recovery rates from 50.05 % to 103.69 %.

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