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- W2480302153 abstract "The role of protein structure on the binding of hexyl acetate with legumin has been studied by a combination of ultrafiltration and gas-liquid chromatography. Molecules of native legumin possess the most binding affinity for hexyl acetate through the unique quaternary structure. Acid denaturation of the protein leads to the complete loss of its binding capacity. On heat denaturation the protein retains its capacity to bind the aroma compounds but has significantly different mechanism and binding parameters from those of the native protein. The effect of molecular structure on binding properties has been studied using a series of homologous, linear alkyl acetates and a series of branched chain esters. The implication of the length of hydrocarbon chain and polarities of molecules of the aroma esters in binding parameters and mechanisms has been shown. The peculiarities of competition and mutual influence between aroma esters, being in equimolar mixtures, in binding with the native protein have been first considered." @default.
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- W2480302153 date "2000-09-07" @default.
- W2480302153 modified "2023-09-25" @default.
- W2480302153 title "Factors Determining Binding of Aroma Esters with Legumin in an Aqueous Medium" @default.
- W2480302153 doi "https://doi.org/10.1021/bk-2000-0763.ch024" @default.
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