数字农科院2.0

Effect of transglutaminase and laccase on the structural changes and texturization behavior of high-moisture extruded pea protein isolate

文献类型： 外文期刊

作者： Li, Tongqing;Hu, Anna;Zhou, Huan;Guo, Feng;Wang, Qiang;Zhang, Jinchuang

作者机构：

关键词： Pea protein isolate;High-moisture extrusion;Enzyme modification

期刊名称： FOOD BIOSCIENCE

ISSN： 2212-4292

年卷期： 2025 年 75 卷

页码：

收录情况： SCIE（2025版） ; ; 农林核心（2024版）

摘要： This study compares the effect of transglutaminase (TG) and laccase (LAC) on the structure and texture of pea protein isolate (PPI) produced by high-moisture extrusion. While high-moisture extrusion is widely used to produce plant-based meat analogues, limited protein cross-linking often leads to weak fibrous structure and poor chewiness. Here, TG and LAC were incorporated during extrusion to investigate their influence on protein structure and textural properties. TG markedly enhanced the textural properties with hardness increasing to 13.53 kg at 0.8 % TG, essentially matching the level observed in bovine semitendinosus, and tensile strength rising from 0.39 kg in the control to 1.51 kg. In contrast, LAC led to a gradual decline in hardness at higher concentrations, reaching 6.12 kg at 0.8 %, and its tensile-enhancing effect peaked at 0.2 %, reached 0.92 kg. Both enzymes promoted protein rearrangement and cross-linking along the extrusion direction, transforming beta-turn and random coil structures into beta-sheet and alpha-helix conformations. TG also induced hydrophobic aggregation, and LAC increased intrinsic fluorescence. The extrudates were benchmarked against real meat samples (chicken, pork, beef) for practical relevance. The results demonstrated that enzymatic cross-linking during extrusion can effectively improve the structure and texture of plant-based meat analogues, offering a practical approach for product development.

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