Breaking the temperature limitation of zein-rice starch dough by microwave pre-gelatinization: Morphological, structural and rheological properties of the dough.

Zein has gluten-like viscoelasticity, but its use is limited due to high glass transition temperature (Tg). To break the temperature limitation of zein-starch dough, microwave heating was used to pre-gelatinize a partial of the starch with zein, and then the remaining was added and kneaded to form a dough. Pre-gelatinized doughs formed by rice starch (PRS), zein-starch (PUZS), and extruded zein-starch (PEZS) were included in this study. The thermal, morphological, rheological, and secondary structural properties of the dough were investigated. The results showed that zein and starch formed a composite gel network and firmly bound starch granules, which improved the dough properties with a smooth surface and compact internal structure, increased strain tolerance, and decreased stiffness. Unextruded zein was distributed uniformly and had strong interactions with the starch. Extruded zein tended to form large particles and had limited interaction with starch but improved dough extensibility. Microwave pre-gelatinization increased the stability of the secondary structure of zein and maintained the viscoelasticity of dough below zein's Tg, which provided a safe and effective way to break the temperature limitation of zein as a structural protein used in foods.

Film-forming properties and mechanisms of soy protein: Insights from ß-conglycinin and glycinin.

Extensive research has been conducted on soy protein films; however, limited information is available regarding the influence of the major components, ß-conglycinin (7S) and glycinin (11S), on the film-forming properties of soy protein. This study aimed to isolate the 7S and 11S fractions in order to prepare films and investigate the impact of varying 7S/11S ratios on the film-forming solutions (FFS) and film properties. The findings revealed that higher 11S ratios led to increased protein aggregation, consequently elevating the storage modulus (G') of the FFS. Notably, an optimal 7S/11S ratio of 7S1:11S2 (CF3) significantly enhanced the film's water resistance. Specifically, it enhanced the water contact angle by an impressive 17.44 % and reduced the water vapor transmission rate by 27.56 %. These improvements were attributed to intermolecular interactions, involving hydrogen bonds and salt bridges, between the amino acid residues of 7S and 11S. As a result, a more uniform and dense microstructure was achieved. Interestingly, the mechanical and optical properties of the film were maintained by the different protein fractions examined. In summary, this study contributes to the understanding of the film-forming properties of soy protein, particularly the role of 7S and 11S.