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This study aimed to demonstrate the feasibility of improving the properties of pea protein isolate (PPI) related to food applications via deamidation with glutaminase. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Fourier transform infrared (FT-IR) profiling revealed that the current glutaminase treatment did not change the basic protein subunit composition. However, it allowed a certain extent of protein unfolding and conformational reorganization to generate more flexible and extended proteins with reduced average particle size and more hydrophobic groups exposed. The underlying mechanisms might include the reduction of β-sheets and antiparallel β-sheets and the increase of the β-turn structure. Moreover, the treatment time was of importance. A 12 h treatment was generally better than a 24 h treatment, and PPI treated with glutaminase at 50 °C for 12 h to a degree of deamidation of 56.1% exhibited significantly improved solubility, homogeneity, dispersibility, and suspendability with reduced beany flavor, grittiness, and lumpiness (compared to those of the untreated PPI). Thus, the glutaminase treatment offers a promising approach for enhancing the usability and applicability of pea proteins.

In order to investigate the effect of glutaraldehyde (GTA) on the structure, mechanical properties and thermal stability of gelatin films, gelatin films modified by GTA at various pH (4.5, 6.5, and 11), were prepared. According to FTIR analysis, the reaction mechanism between GTA and gelatin was different at various pH. With the addition of GTA, the intermolecular forces (hydrogen bonds and ionic bonds) and triple helix structure of gelatin film were significantly disrupted. At pH 4.5, gelatin films modified by GTA showed the highest mechanical properties and thermal stability among all films, which tensile strength and residues in TGA up to 16.13 MPa and 15.05%, respectively. Therefore, an optimum pH was around 4.5 in gelatin films cross‐linked by GTA.

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