Pulse proteins: Processing, characterization, functional properties and applications in food and feed

Physicochemical and textural properties of heat-induced pea protein isolate gels

These studies have demonstrated that peas and lentils can be used as protein sources for flours, concentrates and isolates Less research attention has been devoted to lentil protein extraction, probably because of the greater cost of lentils as compared to peas Pin-milling and air classification is well adapted to extracting pea flours to produce pea protein concentrates Apparently, air-classification can be applied successfully to starch rich legumes, but will not give satisfactory results with lipid rich legumes Wet processes, including alkaline and salt and acid solubilization, together with isoelectric precipitation or ultrafiltration, have been developed The pea and lentil protein extracts of these processes exhibit comparable and complementary functionality to homologous soybean products Air-classified pea protein concentrates are different from soy protein concentrates because of residual starch which can be useful for particular functional applications Pea isolates appear to exhibit better foaming properties and more solubility than soy isolates, but pea isolates have to be more concentrated than soy isolates to produce viscous dispersions The economic feasibility of pea and lentil protein extracts is related directly to protein content of the flour, unique functionality of the extracts, marketability of the by-products of extraction and the cost of peas or lentils

Pea and lentil protein extraction and functionality

Thermal properties of Phaseolus angularis (red bean) globulin

Smooth and wrinkled pea cultivars were studied to evaluate the protein content of the seeds, the proportion of albumins to globulins and the variability of the vicilin/legumin ratio. Principal components analysis showed a strong negative correlation between albumin and globulin contents. Stepwise discriminant analysis demonstrated that two variables, protein content and vicilin/legumin ratio, divided the samples into smooth and wrinkled cultivars with a percentage of success of 95%. In addition, the vicilin/legumin ratio tended to increase, the lower the protein content is.

Quantitative and qualitative variability of pea (Pisum sativum L.) protein composition

Pea globulins, vicilin and legumin were isolated by chromatography on DEAE Sepharose and Ultrogel ACA 34. The procedure was carried out on a preparative scale and used to purify about 5 g of each globulin for a separation cycle. The purity of the vicilin and legumin was verified by immunoelectrophoretic and ultracentrifuge analysis.

François Schaeffer

Papers

Large-scale purification and characterisation of pea globulins