Comparison of recombinant protein Z with natural protein Z derived from malt: From structure to functional properties

Protein Z (PZ) is a prominent albumin found in the endosperm of barley seeds with a molecular weight of approximately 40 kDa. Its multifaceted functional attributes, including trypsin- and thrombin-inhibiting bioactivities and superior foaming properties, have garnered significant attention in research. Considering the post-translational modifications of PZ natural in barley malt, we tried to express recombinant protein Z (rPZ) in E. coli. The present study aims to undertake a comparative analysis between natural PZ and rPZ in order to elucidate their respective characteristics. After spectral analysis, there are significant differences in their secondary and tertiary structures. In addition, rPZ showed superior foamability and foam stability. As for the serpin-like activity, the inhibition rate of rPZ is much higher than that of PZ. In contrast with the inhibition activity, the digestability of rPZ is much lower than that of PZ. As for the cargo carrier properties, rPZ showed an excellent ability to stabilize astaxanthin at 37 °C. These results suggest that rPZ is more suitable as protein carrier, due to the high foamability, serpin-like activity and low digestive stability, which not only give a brief view of recombinant protein, but also give a direction for PZ in cargo delivery.