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Mechanisms by which maltol and talin potentiate flavourBingham, Alison F. January 1990 (has links)
No description available.
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Modelling, NMR and synthesis of food peptidesCutts, Rosalind Jennifer January 1996 (has links)
The work in this thesis can be divided into two sections, namely the study of delicious peptide, a food flavour and the antimicrobial peptide lactofenicin B. The main interest in these compounds is in terms of structure and conformation adopted in solution and how this relates to their mode of action. Delicious peptide was studied initially by 1H NMR spectroscopy for evidence of a specific solution structure. Results show that delicious peptide does not adopt a regular conformation in solution. Molecular dynamics simulations of this peptide show the flexibility of the peptide structure in solution. Quenched molecular dynamics simulations were used to search for low energy conformers of the peptide. The results suggest that the flavour of the peptide is produced by interaction of basic and acidic regions in the peptide. The work was extended to examine delicious peptide analogues with similar flavour characteristics. The results obtained suggest that similar interactions of basic and acidic regions occur for these peptides to produce a savoury flavour. The antimicrobial peptide Lactofemcin B was synthesised by Fmoc poly-amide synthesis. Problems with the synthesis occurred due to the protecting groups used for the five arginine residues present in the sequence. Predictive modelling studies on Lactofenicin B peptide, derived from bovine lactofenicin protein suggest that the peptide adopts a region of alpha-helical conformation in solution. The flexibility of the peptide was studied by molecular dynamics in solution and simulations of other environmental conditions were carried out by variation of electrostatic interactions using dielectric constants for membrane, TFE and water environments. The results suggest the beta-helical conformation is most stable in an environment such as trifluoroethanol, the peptide showing more flexibility in aqueous solution. Experimental results for the peptide confirm the flexibility of the peptide in solution. CD results show that lactofenicin B has no specific conformation in solution, although an beta-helical conformation is adopted in trifluoroethanol. The peptide also adopts a beta-sheet conformation in low concentrations of SDS micelle and therefore its conformation is dependant on environmental conditions. NMR studies show that the peptide, although flexible in solution, shows short-range NOE interactions that suggest a local beta-helical conformation may be present. However the overall conformation for the peptide is a flexible one.
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Studies on interactions of milk proteins with flavour compounds : a thesis presented in partial fulfilment of the requirements for the degree of Doctor of Philosophy in Food Technology at Massey University, Palmerston North, New ZealandKühn, Janina January 2007 (has links)
Milk proteins are known to bind volatile flavour compounds to varying extents, depending on the nature of the protein and flavour compound. Processing conditions, such as temperature and pH, are also known to have an influence on the interactions between milk proteins and flavour compounds. These interactions cause a great challenge for flavour scientists because they influence the perceived aroma profile of food products significantly, in particular in low-fat food products. The objectives of this research were to develop a headspace solid-phase microextraction (SPME) method followed by gas chromatography with flame ionisation detection (GC-FID) for the investigation of protein-flavour interactions, and to determine binding parameters of the hydrophobic flavour compound, 2-nonanone, to individual milk proteins - namely, β-lactoglobulin (β-lg), α-lactalbumin (α-la), bovine serum albumin (BSA), αs1-casein, and β-casein -, whey protein isolate (WPI), and sodium caseinate. Secondly, it was the aim to compare the binding of the structurally similar flavour compounds - 2-nonanone, 1-nonanal, and trans-2-nonenal – to WPI in aqueous solution, and to investigate the effect of heat and high pressure treatment, and pH on the extent of protein-flavour binding. The final objective was to investigate the in vivo release of the reversibly bound flavour compound, 2-nonanone, from WPI and sodium caseinate using proton transfer-reaction mass spectrometry (PTR-MS), and to understand the effect of viscosity on flavour release in vivo. The binding of the model flavour compound 2-nonanone to individual milk proteins, WPI, and sodium caseinate in aqueous solutions was investigated, using headspace SPME followed by GC-FID. The 2-nonanone binding capacities decreased in the order: BSA > β-lg > α-la > αs1-casein > β-casein, and the binding to WPI was stronger than the binding to sodium caseinate. All proteins appeared to have one binding site for 2-nonanone, except for BSA which possessed two classes of binding sites. The influence of heat treatment, high pressure processing and pH of the protein solutions on the binding of 2-nonanone, 1-nonanal, and trans-2-nonenal to WPI was determined. The binding of these compounds to WPI decreased in the order: trans-2-nonenal > 1-nonanal > 2-nonanone. The binding of 2-nonanone appears to involve hydrophobic interactions only, whereas the aldehydes, in particular trans-2-nonenal, also react through covalent binding. Upon both heat and high pressure denaturation, the binding of 2-nonanone to WPI decreased, the binding of 1-nonanal remained unchanged, while the binding of trans-2-nonenal increased. The binding affinity of the flavour compounds and WPI increased with increasing pH, which is likely to result from pH dependent conformational changes of whey proteins. The in vivo flavour (2-nonanone) release from solutions of WPI and sodium caseinate was investigated using proton-transfer-reaction mass spectrometry. During consumption, 2-nonanone was partly released from WPI, whereas there was no significant release from sodium caseinate. Even after swallowing of the samples, a substantial amount of flavour was detected in the breath, suggesting that the milk proteins interact with the mucosa in the mouth and throat, resulting in a further release of flavour from mucosa-bound proteins. An increase in viscosity of the protein solutions by the addition of carboxymethylcellulose enhanced the release of 2-nonanone from WPI, and resulted in 2-nonanone release from sodium caseinate. This may be due to a thicker coating of the mucosa with the sample solution after swallowing due to the higher viscosity, resulting in additional release of protein-bound flavour. These findings contribute to the knowledge of the interactions that occur between flavour compounds and proteins, which is required to improve food flavouring and to make protein based foods, e.g., low-fat dairy products, sensorily more acceptable to the consumer. The results also emphasize a careful choice of food processing conditions, such as temperature, high pressure or pH to obtain a desirable flavour profile.
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