Jun. 05, 2021
Benzaldehyde is an aromatic aldehyde used in cosmetics as a denaturant, a flavoring agent, and as a fragrance. Currently used in only seven cosmetic products, its highest reported concentration of use was 0.5% in perfumes. Next, the benzaldehyde supplier will share the following content with you.
The compound is responsible for the odor of natural bitter almond oil and is incorporated directly in perfumes, soaps, foods, drinks, and other products. Substantial amounts are used in the production of derivatives that are also employed in the perfume and flavor industries.
Another application of benzaldehyde is the production of triphenylmethane dyes. In the pharmaceutical industry, benzaldehyde is used as an intermediate in the manufacture of chloramphenicol, ephedrine, ampicillin, diphenylhydantoin, and other products.
Benzoic acid and a wide range of derivatives and related benzenic compounds, such as benzaldehyde is commonly used as antibacterial and antifungal preservatives and as flavoring agents in food, cosmetic, hygiene, and pharmaceutical products.
Chemical intermediate for dyes, flavoring materials, perfumes, and aromatic alcohols; solvent for oils, resins, some cellulose ethers, cellulose acetate, and nitrate; flavoring compounds; synthetic perfumes; manufacturing of cinnamic acid, benzoic acid; pharmaceuticals; photographic chemicals.
Manufacture of dyes, perfumery, cinnamic and mandelic acids, as solvents; in flavors.
The flavor intensity of benzaldehyde, limonene, and citral were determined in the presence of casein and whey protein by quantitative descriptive analysis deviation from reference.
In the presence of whey protein, the benzaldehyde flavour intensity declined, on the other hand, the casein had no effect on benzaldehyde flavour intensity. For limonene, the flavour intensity decreased when the protein concentration (whey protein or casein) increased. For citral, panellists detected no effect on flavour intensity in presence of whey protein or casein.
The authors proposed the following hypothesis: the decrease of benzaldehyde and limonene flavor intensity in the presence of whey protein or casein may be due to non-polar interaction for casein and interaction with non-polar binding sites, cysteine-aldehyde condensation, or Schiff base formation with whey protein. The effect of sodium caseinate or whey concentrate on vanillin flavour intensity was also tested using the same method.
The vanillin flavour intensity was moderately lower than the reference for three concentrations of sodium caseinate tested and for two concentrations of whey protein. The authors supposed that this decrease of vanillin flavour intensity was probably due to the cysteine-aldehyde condensation or Schiff base formation. On the other hand, sensory analysis applying a matching test showed that the addition of β-lactoglobulin had no effect on the odour perception of vanillin, but brought about a significant decrease in the flavour perception of eugenol.
These results are interpreted with the different affinity of the two flavour compounds for β-lactoglobulin: the affinity constant of vanillin is lower than that of eugenol. Moreover, addition of β-lactoglobulin (0.5% and 1%) to aqueous solutions of three methyl ketones (2-heptanone, 2-octanone, 2-nonanone) induces a significant decrease in odour intensity.
Recently, the development of a new technique, APCI-MS (atmospheric pressure chemical ionisation-mass spectrometry), allows the study of the protein–flavour interactions in in vivo conditions. Thus, the interactions between flavour compounds and milk protein under static (headspace analysis) and dynamic (APCI-MS) conditions were described by Le Guen and Vreeker (2003). First, they studied the interactions between 2-alkenals (C3 to C9), methyl ketones (C3 to C9) and whey protein in in vitro conditions by headspace, and after that, in in vivo conditions by APCI-MS, to monitor the release of aroma during eating.
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