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Review
. 2019 Jun;56(6):2787-2798.
doi: 10.1007/s13197-019-03723-8. Epub 2019 Mar 19.

Pulse proteins: secondary structure, functionality and applications

Khetan Shevkani  1 , Narpinder Singh  2 , Ying Chen  3 , Amritpal Kaur  2 , Long Yu  3
Affiliations
Review

Pulse proteins: secondary structure, functionality and applications

Khetan Shevkani et al. J Food Sci Technol. 2019 Jun.

Abstract

Pulses are the second most important source of food for humans after cereals. They hold an important position in human nutrition. They are rich source of proteins, complex carbohydrates, essential vitamins, minerals and phytochemicals and are low in lipids. Pulses are also considered the most suitable for preparing protein ingredients (concentrates and isolates) because of their high protein content, wide acceptability and low cost. In addition, pulse proteins exhibit functional properties (foaming and emulsification, water and fat absorption and gelation) as well as nutraceutical/health benefiting-properties which makes them healthier and low cost alternative to conventional protein sources like soy, wheat and animals. Proteins from different pulses (beans, peas, lentils, cowpeas, chickpeas, pigeon peas, etc.) differ in their composition and structure hence for finished product suitability. Therefore, this article aimed to review composition, structure-function relationship and current applications of different pulse proteins in the food industry.

Keywords: Application; Functional properties; Nutraceutical properties; Pulses; Secondary structure.

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Figures

Fig. 1
Fig. 1
Relative proportion of different secondary structural components of protein isolates from different kidney bean and field pea lines. EC 572723, Pi 244719, Pi 312296, Pi 249554, and PLB 10 1 are kidney bean lines while IC 394027, IC 342028, IC 291541, IC 381453 and IC 299013 are field pea lines (Source: Shevkani et al. 2015b)
Fig. 2
Fig. 2
Typical U shaped protein solubility-pH profiles of proteins isolated from three different pulses
Fig. 3
Fig. 3
Foaming (FC foaming capacity and FS foam stability) and emulsifying properties (EAI emulsifying activity index and ESI emulsion stability index) of protein isolates from kidney bean (Pi 312296) and field pea (IC 291541) at different pH (Source: Shevkani et al. 2015b)
Fig. 4
Fig. 4
Changes in the dynamic rheological moduli (G′ and G″) of protein isolates from kidney bean and field pea during heating and cooling. Arrow showing gelation temperature of protein as crossover temperature between moduli (Source: Shevkani et al. 2015b)
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