Insight into the solubilization mechanism of wheat gluten by protease modification from conformational change and molecular interaction perspective.

The low solubility limits the utilization of other functional characteristics of wheat gluten (WG). This study effectively improved the solubility of WG through protease modification and explored the potential mechanism of protease modification to enhance the solubility of WG, further stimulating the potential application of WG in the food industry. Solubility of WG modified with alkaline protease, complex protease, and neutral protease was enhanced by 98.99%, 54.59%, and 51.68%, respectively. Notably, the content of ß-sheet was reduced while the combined effect of hydrogen bond and ionic bond were increased after protease modification. Meanwhile, the reduced molecular size and viscoelasticity as well as the elevated surface hydrophobicity, thermostability, water absorption capacity, and crystallinity were observed in modified WG. Moreover, molecular docking indicated that protease was specifically bound to the amino acid residues of WG through hydrogen bonding, hydrophobic interaction, and salt bridge.

Remodeling mechanism of gel network structure of soy protein isolate amyloid fibrils mediated by cellulose nanocrystals.

The differences in the gelling properties of soy protein isolate (SPI) and soy protein isolate amyloid fibrils (SAFs) as well as the role of cellulose nanocrystals (CNC) in regulating their gel behaviors were investigated in this study. The binding of CNC to ß-conglycinin (7S), glycinin (11S), and SAFs was predominantly driven by non-covalent interactions. CNC addition reduced the particle size, turbidity, subunit segments, and crystallinity of SPI and SAFs, promoted the conversion of α-helix to ß-sheet, improved the thermal stability, exposed more tyrosine and tryptophan residues, and enhanced the intermolecular interactions. A more regular and ordered lamellar network structure was formed in the SAFs-CNC composite gel, which could be conducive to the improvement of gel quality. This study would provide theoretical reference for the understanding of the regulatory mechanism of protein amyloid fibrils gelation as well as the high-value utilization of SAFs-CNC complex as a functional protein-based material or food ingredient in food field.

Roles of the PH, coiled-coil and SAM domains of the yeast polarity protein Boi2 in polarity-site localization and function in polarized growth.

Boi1 and Boi2 are paralogous proteins essential for bud formation in budding yeast. So far, the domains that target Boi1/Boi2 to the polarity sites and function in bud formation are not well understood. Here, we report that a coiled-coil domain of Boi2 cooperates with the adjacent PH domain to confer Boi2's bud-cortex localization and major function in cell growth. The PH domain portion of the PH-CC bi-domain interacts with the Rho GTPases Cdc42 and Rho3 and both interactions are independent of the GTP/GDP-bound state of each GTPase. Interestingly, high-copy RHO3 and BOI2 but not CDC42 suppressed the growth defect of RGA1-C538 overexpression and the sec15-1 mutant and this BOI2 function depends on RHO3, suggesting that Boi2 may function in the Rho3 pathway. The SAM domain of Boi2 plays an essential role in high-copy suppression of the two mutants as well as in the early bud-neck localization of Boi2. The SAM domain and the CC domain also interact homotypically. They are likely involved in the formation of Boi2-containing protein complex. Our results provide new insights in the localization and function of Boi2 and highlight the importance of the PH-CC bi-domain and the SAM domain in Boi2's localization and function.