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Plant protein films are a research hotpot in the current food packaging field for their renewable and bio-compatibility, and further improving the physicochemical properties of plant protein films in combination with biodegradable materials is of great significance. In this study, we selected cellulose nanocrystals (CNC) to modify the protein films with soybean protein isolate (SPI), wheat gluten protein (WGP), and Zein, and the physicochemical properties were studied. The results showed that the hardness and opacity of Zein-based films decreased by 16.61% and 54.12% with the incorporation of CNC, respectively. The SPI-based films performed with lower hardness and higher tensile strength. The thickness and opacity of WGP-based films increased by 39.76% and 214.38% after combination with CNC, respectively. Accordingly, this study showed that CNC could largely modify the physicochemical properties of the plant protein films, which provided a reference for the preparation of modified plant protein films using biodegradable materials.

BackgroundWheat gluten protein (WGP) has poor solubility and does not easily form fibrous structures, the meat analogues, prepared from it, have unsatisfactory texture properties and poor water holding capacity. Our previous work indicated that pH‐shifting combined with heat treatment can significantly improve the solubility and emulsibility of WGP. Therefore, in this work, WGP was treated by pH‐cycling (m‐WGP) to improve the solubility and then applied in the preparation of meat analogues by high moisture extrusion.ResultsThe results indicated that the addition of m‐WGP significantly improved the texture characteristics and water holding capacity (282.4%) of the extrudates and made the extrudates show a tighter organizational structure according to the SEM images. Additionally, MRI analysis showed that the addition of m‐WGP resulted in a more uniform moisture distribution in the extrudate. And the free sulfhydryl group result showed that the addition of m‐WGP significantly increased the free sulfhydryl group content, which was beneficial to the formation of disulfide bonds to enhance the tissue structure.ConclusionWhen the addition content of m‐WGP was 10%, the gluten extrudate exhibited good water holding capacity and uniform moisture distribution, but the excessive hardness and chewiness were not suitable for simulating meat. When the addition content of m‐WGP reached 50%, the gluten extrudate has the closest textural characteristics to commercial plant‐based meat and real meat, with the potential to be used as a raw material to simulate meat. Accordingly, this work improves the processing properties of WGP and explores plant‐based ingredients for meat analogues.This article is protected by copyright. All rights reserved.

Wheat gluten protein (WGP) is a high-quality plant-based protein resource. However, due to its unique reticulation structure, the processing properties of WGP are extremely poor, limiting its application. To overcome these drawbacks, the aim of this study was to modify wheat gluten protein by three relatively novel and mainstream chemical modifications. The results showed that the pH-shifting treatment changed the apparent morphology of the protein, showing a uniform flocculent structure, leading to significant improvements in foaming capacity and emulsification property. After deamidation by acetic acid, the solubility of WGP was greatly improved (60.1%), which was nearly four times that of the control group (15.8%), and its foam stability was also significantly improved. The WGP had the highest thermal stability (deformation temperature up to 148 ℃) after TGase deamidation. These results indicate that the three modification methods improve the functional properties of WGP in different aspects and expand its application potential.

Wheat gluten protein (WGP) is a high-quality plant-based protein resource. However, due to its unique reticulation structure, the processing properties of WGP are extremely poor, limiting its application. To overcome these drawbacks, the aim of this study was to modify wheat gluten protein by three relatively novel and mainstream chemical modi cations. The results showed that the pH-shifting treatment changed the apparent morphology of the protein, showing a uniform occulent structure, leading to signi cant improvements in foaming capacity and emulsi cation property. After deamidation by acetic acid, the solubility of WGP was greatly improved (60.1%), which was nearly four times that of the control group (15.8%), and its foam stability was also signi cantly improved. The WGP had the highest thermal stability (deformation temperature up to 148 ℃) after TGase deamidation. These results indicate that the three modi cation methods improve the functional properties of WGP in different aspects and expand its application potential.