Structural and Thermal Characterization of Protein Isolates from Australian Lupin Varieties as Affected by Processing Conditions.

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 ß-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 ß-sheet and α-helical structure being the dominant structure, respectively. Thermal characterization showed two denaturation peaks corresponding to ß-conglutin (Td = 85-89 °C) and α-conglutin (Td = 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.