Future dietary protein demand will focus more on plant-based sources than animal-based products. In this scenario, legumes and pulses (lentils, beans, chickpeas, etc.) can play a crucial role as they are one of the richest sources of plant proteins with many health benefits. However, legume consumption is undermined due to the hard-to-cook (HTC) phenomenon, which refers to legumes that have high resistance to softening during cooking. This review provides mechanistic insight into the development of the HTC phenomenon in legumes with a special focus on common beans and their nutrition, health benefits, and hydration behaviour. Furthermore, detailed elucidation of HTC mechanisms, mainly pectin-cation-phytate hypothesis and compositional changes of macronutrients like starch, protein, lipids and micronutrients like minerals, phytochemicals and cell wall polysaccharides during HTC development are critically reviewed based on the current research findings. Finally, strategies to improve the hydration and cooking quality of beans are proposed, and a perspective is provided.

Proteins from the full and defatted flours of L. angustifolius cv Jurien and L. albus cv Murringo were prepared using alkaline extraction and iso-electric precipitation. Isolates were either freeze dried or spray dried or pasteurized at 75 ± 3 °C/5 min before freeze-drying. Various structural properties were investigated to elucidate the varietal and processing-induced effect on molecular and secondary structure. Irrespective of processing, isolated proteins had a similar molecular size, with α-conglutin (412 kDa) and β-conglutin (210 kDa) being principal fractions for the albus and angustifolius variety, respectively. Smaller peptide fragments were observed for the pasteurized and spray dried samples, indicating some degree of processing-induced changes. Furthermore, secondary structure characterization by Fourier-transform-infrared and circular dichroism spectroscopy showed β-sheet and α-helical structure being the dominant structure, respectively. Thermal characterization showed two denaturation peaks corresponding to β-conglutin (T_d = 85–89 °C) and α-conglutin (T_d = 102–105 °C) fractions. However, the enthalpy values for α-conglutin denaturation were significantly higher for albus species, which corroborates well with higher amounts of heat stable α-conglutin present. Amino acid profile was similar for all samples with limiting sulphur amino acid. In summary, commercial processing conditions did not have a profound effect on the various structural properties of lupin protein isolates, and properties were mainly determined by varietal differences.