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The excessive water sensitivity of hydroxypropyl methylcellulose (HPMC) films prevent them from being used extensively. In order to overcome this limitation, superhydrophobic HPMC films were meticulously crafted through the utilization of a composite of polydimethylsiloxane (PDMS) and ball-milled rice starch, corn starch, or potato starch (RS/CS/PS) for the coating process. Initially possessing hydrophilic properties, the HPMC Film (CA = 49.3 ± 1.8°) underwent a transformative hydrophobic conversion upon the application of PDMS, resulting in a static contact angle measuring up to 103.4 ± 2.0°. Notably, the synergistic combination of PDMS-coated HPMC with ball-milled starch demonstrated exceptional superhydrophobic attributes. Particularly, the treated HPMC-based film, specifically the HP-CS-2 h film, showcased an impressive contact angle of 170.5° alongside a minimal sliding angle of 5.2°. The impact of diverse starch types and the ball milling treatment on the PDMS/starch coatings and HPMC film was thoroughly examined using scanning electron microscopy (SEM), wide-angle X-ray diffraction (WAXS), and particle size analysis. These studies demonstrated that the low surface energy and roughness required for the creation of superhydrophobic HPMC-based films were imparted by the hierarchical structure formed by the application of PDMS/ball-milled starch. Polydimethylsiloxane (PubChem CID: 24764); Hydroxypropyl methylcellulose (PubChem CID: 671); Ethyl acetate (PubChem CID: 8857). [Display omitted] [ABSTRACT FROM AUTHOR]

In this study, rice starch (RS) was mixed with varying amounts of rice protein (RP; 0 % to 16 %) to explore the effects of protein on the gelatinization and retrogradation of starch during storage. The increased RP addition decreased the viscosity and gelatinization enthalpy of the mixtures but caused an upward trend in the gelatinization temperature, indicating that protein hampers the process of starch gelatinization. Furthermore, RP addition reduced gel hardness, decreased retrogradation enthalpy and crystallization rate constant, but increased Avrami exponent upon RS retrogradation. RP addition also facilitated the mobility of water molecules, weakened the conversion from bound water to free water in the gels, and moderately increased the uniformity and thickness of gel shape. In summary, RP had a dose-dependent effect on the gelatinization and retrogradation behavior of RS, although the anti-retrogradation concentration effect strongly weakened at protein levels exceeding 12 %. It is noteworthy, that excessive RP addition resulted in disulfide bond formation, which increased gel strength and network structure but reduced the ability of RP to facilitate water molecule mobility and restrict water migration, ultimately reducing its anti-retrogradation capability. This phenomenon can be partially attributed to spontaneous protein-protein interaction caused by excessive protein addition, replacing the starch-protein interaction. [ABSTRACT FROM AUTHOR]

In this study, rice starch (RS) was mixed with varying amounts of rice protein (RP; 0 % to 16 %) to explore the effects of protein on the gelatinization and retrogradation of starch during storage. The increased RP addition decreased the viscosity and gelatinization enthalpy of the mixtures but caused an upward trend in the gelatinization temperature, indicating that protein hampers the process of starch gelatinization. Furthermore, RP addition reduced gel hardness, decreased retrogradation enthalpy and crystallization rate constant, but increased Avrami exponent upon RS retrogradation. RP addition also facilitated the mobility of water molecules, weakened the conversion from bound water to free water in the gels, and moderately increased the uniformity and thickness of gel shape. In summary, RP had a dose-dependent effect on the gelatinization and retrogradation behavior of RS, although the anti-retrogradation concentration effect strongly weakened at protein levels exceeding 12 %. It is noteworthy, that excessive RP addition resulted in disulfide bond formation, which increased gel strength and network structure but reduced the ability of RP to facilitate water molecule mobility and restrict water migration, ultimately reducing its anti-retrogradation capability. This phenomenon can be partially attributed to spontaneous protein-protein interaction caused by excessive protein addition, replacing the starch-protein interaction. [ABSTRACT FROM AUTHOR]