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Hemocyanins are large multi-subunit copper proteins that transport oxygen in many arthropods and molluscs. Comparison of the amino acid sequence data for seven different subunits of arthropod hemocyanins from crustaceans and chelicerates shows many highly conserved residues and extensive regions of near identity. This correspondence can be matched closely with the three domain structure established by x-ray crystallography for spiny lobster hemocyanin. The degree of identity is particularly striking in the second domain of the subunit that contains the six histidines which ligate the two oxygen-binding copper atoms. The polypeptide architecture of spiny lobster hemocyanin appears to be the same in all arthropods. This structure must therefore be at least as old as the estimated time of divergence of crustaceans and chelicerates, about 540 to 600 million years ago.

There is increasing worldwide demand for proteins of both animal and plant origin. However, animal proteins are expensive in terms of both market price and environmental impact. Among alternative plant proteins, sunflower seeds are particularly interesting in view of their widespread availability in areas where soy is not or only sparsely produced. Compared with other sources of vegetable proteins, sunflower seeds have been reported to have a low content of antinutritional factors. Although the absence of these factors is important, the functionality of the protein preparations will mainly determine their applicability. This review provides detailed information about sunflower seed composition and processing, including processes to remove phenolic compounds from meals. The main part of the review concerns the structure and functionality of the two major protein fractions, helianthinin and 2S albumins. Regarding functionality, emphasis is on solubility, thermal behaviour and surface activity. Protein structure and functionality are discussed as a function of extrinsic factors such as pH, ionic strength, temperature and the presence of other seed components, particularly chlorogenic acid. In addition, sunflower proteins are compared from a structural and functional point of view with other plant proteins, particularly soy proteins.

Long, fibrillar semiflexible aggregates were formed from soy glycinin and soy protein isolate (SPI) when heated at 85 degrees C and pH 2. Transmission electron microscopy analysis showed that the contour length of the fibrils was approximately 1 microm, the persistence length 2.3 microm, and the thickness a few nanometers. Fibrils formed from SPI were more branched than the fibrils of soy glycinin. Binding of the fluorescent dye Thioflavin T to the fibrils showed that beta-sheets were present in the fibrils. The presence of the fibrils resulted in an increase in viscosity and shear thinning behavior. Flow-induced birefringence measurements showed that the behavior of the fibrils under flow can be described by scaling relations derived for rodlike macromolecules. The fibril formation could be influenced by the protein concentration and heating time. Most properties of soy glycinin fibrils are comparable to beta-lactoglobulin fibrils.

Gel network formation of pea legumin (8.4% on a protein basis, pH 7.6) was monitored via dynamic rheological measurements. Gelation was performed in the absence and presence of the thiol-blocking reagent N-ethylmaleimide, at different rates of heating and cooling. Overall, it was shown that pea legumin gel formation was not effected by changes in the heating rate, and the two differently heated samples were unaffected by the addition of 20 mM NEM, which indicated that disulfide bonds were not essential within the network strands of these legumin gels. However, slowly cooling the legumin samples caused disulfide bonds to become involved within the network; this was observed by a large increase in gel strength that was then substantially reduced when repeating the sample in the presence of NEM. These experiments were repeated with soybean glycinin in order to determine whether a common model for gel formation of legumin-like proteins could be built, based upon molecular reasoning. The two proteins were affected in the same way by changes in the conditions used, but when applying a procedure of reheating and recooling the gel networks responded differently. Pea legumin gel networks were susceptible to rearrangements that caused the gels to become stronger after reheating/recooling, yet glycinin gel networks were not. It was concluded that the same physical and chemical forces drove the processes of denaturation, aggregation, and network formation. Each process can therefore be readily targeted for modification based upon molecular reasoning. Pea legumin and soybean glycinin gel networks had structurally different building blocks, however. A model of gelation aimed at texture control therefore requires additional information.

A method for obtaining sunflower protein (SFP) isolate, nondenatured and free of chlorogenic acid (CGA), has been developed. During the isolating procedure, the extent of CGA removal and protein denaturation was monitored. The defatted flour contained 2.5% CGA as the main phenolic compound. Phenolic compounds were removed by aqueous methanol (80%) extraction, before protein extraction at alkaline pH and diafiltration. Differential scanning calorimetry and solubility tests indicated that no denaturation of the proteins had occurred. The resulting protein products were biochemically characterized, and the presence of protein-CGA complexes was investigated. SFPs of the studied variety were found to be composed of two main protein fractions: 2S albumins and 11S globulins. In contrast to what has been previously reported, CGA was found to elute as free CGA, not covalently associated to any protein fraction.

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