The impact of food structure on taste and digestibility.

The modern food chain depends on complex interactions between businesses from farming to retail. Until recently their success depended upon providing consumers with safe, convenient food which was pleasant to eat, at a reasonable value for money. This has required detailed research into how food structures deliver recognisable and preferred types of foods, from hard solids to thick liquids. Fortunately the consumer is able to detect and report sensations of texture and flavour which can be related to the composition, structure and breakdown of food in the mouth. Chemists, physicists and engineers can attempt to build mechanistic models of how structures relate to perception. The state of the art in our understanding and design capabilities are reviewed. In the developed world, the success is self evident as food prices (as a proportion of income) have decreased and there is a surfeit of choice on the supermarket shelf. More recently, the requirement to add a balanced healthy diet to the simple pleasure of eating has become the new target. This is a different type of challenge. The effects of diet on health are long term, and not easily reported by the consumer. Whilst we know something of how the digestive tract works in breaking down foods, we know little of how food structure impacts upon this process, and even less of how the neural and metabolic feedback systems operate to relate food structures to satiety and satiation. Therefore, in the absence of causal models relating structures to eating habits, structures designed to achieve both immediate pleasure and long term healthy eating are much more speculative. What we think we know, and what we need to know are reviewed. There is no doubt that other skills, in nutrition, physiology, neuroscience, and molecular biology etc. will need to be added to the classical approaches of food materials science and engineering if these challenges are to be met.

Fat crystallisation at oil-water interfaces.

This review focuses on recent advances in the understanding of lipid crystallisation at or in the vicinity of an interface in emulsified systems and the consequences regarding stability, structure and thermal behaviour. Amphiphilic molecules such as emulsifiers are preferably adsorbed at the interface. Such molecules are known for their ability to interact with triglycerides under certain conditions. In the same manner that inorganic crystals grown on an organic matrix see their nucleation, morphology and structure controlled by the underlying matrix, recent studies report a templating effect linked to the presence of emulsifiers at the oil/water interface. Emulsifiers affect fat crystallisation and fat crystal behaviour in numerous ways, acting as impurities seeding nucleation and, in some cases, retarding or enhancing polymorphic transitions towards more stable forms. This understanding is of crucial importance for the design of stable structures within emulsions, regardless of whether the system is oil or water continuous. In this paper, crystallisation mechanisms are briefly described, as well as recent technical advances that allow the study of crystallisation and crystal forms. Indeed, the study of the interface and of its effect on lipid crystallisation in emulsions has been limited for a long time by the lack of in-situ investigative techniques. This review also highlights reported interfacial effects in food and pharmaceutical emulsion systems. These effects are strongly linked to the presence of emulsifiers at the interface and their effects on crystallisation kinetics, and crystal morphology and stability.

The physico-chemical characterization of a boiling stable antifreeze protein from a perennial grass (Lolium perenne).

We have characterized a cold-induced, boiling stable antifreeze protein. This highly active ice recrystallization inhibition protein shows a much lower thermal hysteresis effect and displays binding behavior that is uncharacteristic of any AFP from fish or insects. Ice-binding studies show it binds to the (1 0 1 0) plane of ice and FTIR studies reveal that it has an unusual type of highly beta-sheeted secondary structure. Ice-binding studies of both glycosylated and nonglycosylated expressed forms indicate that it adsorbs to ice through the protein backbone. These results are discussed in light of the currently proposed mechanisms of AFP action.

Investigation of bacterial spore structure by high resolution solid-state nuclear magnetic resonance spectroscopy and transmission electron microscopy.

High resolution solid-state nuclear magnetic resonance spectroscopy (NMR) in combination with transmission electron microscopy (TEM) of spores of Bacillus cereus, an outer coatless mutant B. subtilis 322, an inner coatless mutant B. subtilis 325 and of germinated spores of B. subtilis CMCC 604 were carried out. Structural differences in the coats, mainly protein of spores were reflected by NMR spectra which indicated also differences in molecular mobility of carbohydrates which was partially attributed to the cortex. Dipicolinic acid (DPA) of spores of B. cereus displayed a high degree of solid state order and may be crystalline. Heat activation was studied on spores of B. subtilis 357 lux + and revealed a structural change when analysed by TEM but this was not associated with increases in molecular mobility since no effects were measured by NMR.

Understanding the mechanism of ice binding by type III antifreeze proteins.

Type III antifreeze proteins (AFPs) are present in the body fluids of some polar fishes where they inhibit ice growth at subzero temperatures. Previous studies of the structure of type III AFP by NMR and X-ray identified a remarkably flat surface on the protein containing amino acids that were demonstrated to be important for interaction with ice by mutational studies. It was proposed that this protein surface binds onto the (1 0 [\bar 1] 0) plane of ice with the key amino acids interacting directly with the water molecules in the ice crystal. Here, we show that the mechanism of type III AFP interaction with ice crystals is more complex than that proposed previously. We report a high-resolution X-ray structure of type III AFP refined at 1.15 A resolution with individual anisotropic temperature factors. We report the results of ice-etching experiments that show a broad surface coverage, suggesting that type III AFP binds to a set of planes that are parallel with or inclined at a small angle to the crystallographic c-axis of the ice crystal. Our modelling studies, performed with the refined structure, confirm that type III AFP can make energetically favourable interactions with several ice surfaces.

Isolation and characterization of a novel antifreeze protein from carrot (Daucus carota).

A modified assay for inhibition of ice recrystallization which allows unequivocal identification of activity in plant extracts is described. Using this assay a novel, cold-induced, 36 kDa antifreeze protein has been isolated from the tap root of cold-acclimated carrot (Daucus carota) plants. This protein inhibits the recrystallization of ice and exhibits thermal-hysteresis activity. The polypeptide behaves as monomer in solution and is N-glycosylated. The corresponding gene is unique in the carrot genome and induced by cold. The antifreeze protein appears to be localized within the apoplast.

A carrot leucine-rich-repeat protein that inhibits ice recrystallization.

Many organisms adapted to live at subzero temperatures express antifreeze proteins that improve their tolerance to freezing. Although structurally diverse, all antifreeze proteins interact with ice surfaces, depress the freezing temperature of aqueous solutions, and inhibit ice crystal growth. A protein purified from carrot shares these functional features with antifreeze proteins of fish. Expression of the carrot complementary DNA in tobacco resulted in the accumulation of antifreeze activity in the apoplast of plants grown at greenhouse temperatures. The sequence of carrot antifreeze protein is similar to that of polygalacturonase inhibitor proteins and contains leucine-rich repeats.

Structure and solution properties of tamarind-seed polysaccharide.

The major polysaccharide in tamarind seed is a galactoxyloglucan for which the ratios galactose:xylose:glucose are 1:2:25:2.8. A minor polysaccharide (2-3%) contains branched (1----5)-alpha-L-arabinofuranan and unbranched (1----4)-beta-D-galactopyranan features. Small-angle X-ray scattering experiments gave values for the cross-sectional radius of the polymer in aqueous solution that were typical of single-stranded molecules. Marked stiffness of the chain (C infinity 110) was deduced from static light-scattering studies and is ascribed partially to the restriction of the motion of the (1----4)-beta-D-glucan backbone by its extensive (approximately 80%) glycosylation. The rigidity of the polymer caused significant draining effects which heavily influenced the hydrodynamic behaviour. The dependence of "zero-shear" viscosity on concentration was used to characterise "dilute" and "semi-dilute" concentration regimes. The marked dependence on concentration in the "semi-dilute" region was similar to that for other stiff neutral polysaccharide systems, ascribed to "hyper-entanglements", and it is suggested that these may have arisen through a tenuous alignment of stiffened chains.

The effect of mechanical deformation on the movement of water in foods.

This study has shown the importance of relating NMR spectroscopic information on the water in model food structures to the mechanical properties of those structures. Analysis of the NMR relaxation data can be used to examine the distribution of water domain sizes, and this has been related to the mechanical properties of the samples. A novel NMR probe-head has been designed, which allows both the NMR and the mechanical data to be simultaneously measured during compression of the sample. This probe-head allows compressive stress/strain data to be obtained directly from the NMR sample, allowing changes in the distribution of the water to be directly correlated to changes in mechanical properties.

Salt-induced swelling of meat: The effect of storage time, pH, ion-type and concentration.

The effect of hypertonic salt solutions on meat fibres has been studied as a function of post-mortem storage. Rabbit longissimus dorsi fibres (after about 20 h post-mortem storage at 4°C), were found to swell in hypertonic salt solutions, such as 0·25m KI or 0·6m KCl, to two to three times their original diameter. This swelling occurred in the fibre transverse plane only. X-ray diffraction shows swelling occurs by a combination of an increase in the myofilament lattice spacing and a loss of myofilament order. Fibre swelling is highly co-operative. At pHs below the isoelectric point of the myofibrillar proteins, hypertonic salt solutions induce fibre shrinkage. The post-mortem time course of response shows a peak at 18-35 h bounded by periods of minimal or zero response. We propose that the collagenous endomysial sheath acts as a restraint to myofibril swelling and that the characteristics of post-mortem swelling are a balance of the myofibrillar propensity to swell and the constraint of the endomysium.