Physicochemical Interactions Between Aroma Compounds and Milk Proteins: Effect of Water and Protein Modification

The physicochemical interactions between aroma compounds and sodium caseinate were studied by complementary techniques involving the protein in aqueous solution at 25 or 75g/L (exponential dilution and equilibrium dialysis) or in a solid state (sorption and infrared spectroscopy). No retention of ac...

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Bibliographic Details
Published in:Journal of dairy science 1998-01, Vol.81 (1), p.82-91
Main Authors: Fares, K., Landy, P., Guilard, R., Voilley, A.
Format: Article
Language:English
Subjects:
ACETATE (ESTER)
ACETATES (ESTERS)
ACETATOS (ESTERES)
ACETONA
ACETONE
ADSORCION
ADSORPTION
AGUA DEL SUELO
ALCOHOLES
ALCOHOLS
ALCOOL
ALDEHIDOS
ALDEHYDE
ALDEHYDES
Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts
aroma
BENZALDEHYDE
BINDING
Biological and medical sciences
BOUND WATER
casein
CASEINATE
CASEINATES
CASEINATOS
DIACETILO
DIACETYL
DIACETYLE
EAU DU SOL
ESPECTROSCOPIA INFRARROJA
ETHYL ACETATE
Food industries
Fundamental and applied biological sciences. Psychology
INFRARED SPECTROPHOTOMETRY
interactions
ISOPROPYL ALCOHOL
ODEUR
OLOR
SMELL
SODIUM CASEINATE
SOIL WATER
SOLUCION
SOLUTION
SOLUTIONS
SPECTROSCOPIE INFRAROUGE
water
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Description
Summary:The physicochemical interactions between aroma compounds and sodium caseinate were studied by complementary techniques involving the protein in aqueous solution at 25 or 75g/L (exponential dilution and equilibrium dialysis) or in a solid state (sorption and infrared spectroscopy). No retention of acetone, ethyl acetate, and 2-propanol in aqueous solutions was found by exponential dilution and equilibrium dialysis. Diacetyl and benzaldehyde interacted with sodium caseinate through strong and weak bonds, as found by equilibrium dialysis. The results obtained by sorption differ from those obtained in aqueous solutions. The compounds that sorbed best to sodium caseinate were acetone and ethyl acetate, and their infrared spectra showed a negative shift of the carbonyl peak between the pure and sorbed state of the compounds, demonstrating their involvement in hydrogen bonds with the protein. In addition, 2-propanol and ethyl acetate were strongly bound to sodium caseinate in a dried state. For the other compounds, results from infrared spectroscopy indicated the presence of interactions between sodium caseinate and the ligand.
ISSN:0022-0302
1525-3198
DOI:10.3168/jds.S0022-0302(98)75554-7