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

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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,transformingβ-turn and random coil structures into β-sheet and α-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.
出处 《Food Bioscience》 2026年第1期935-943,共9页 食品生物科学(英文)
基金 supported by the National Key Research and Development Plan of China(2023YFD2100800) the Beijing Natural Science Foundation(6242027) the Agricultural Science and Technology Innovation Program by CAAS(ASTIP-Y2025QC30) the YOUNG ELITE SCIENTIST SPONSORSHIP PROGRAM BY CAST(2022QNRC001).

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