Physicochemical modulation of soy-hemp-wheat protein meat analogues prepared by high-moisture extrusion using transglutaminase
文献类型： 外文期刊
作者： Sun, Zhouliang 2 ; Zhang, Wanhui 2 ; Zhang, Fengkai 2 ; Chiu, Ivy 4 ; Li, Dan 1 ; Wu, Xinghui 2 ; Yang, Tianxi 4 ; Gao, Yang 3 ; Zheng, Huanyu 1 ;
作者机构： 1.Heilongjiang Green Food Sci Res Inst, Harbin 150028, Peoples R China
2.Northeast Agr Univ, Coll Food Sci, Harbin 150030, Peoples R China
3.Heilongjiang Acad Agr Sci, Inst Food Proc, Harbin 150086, Peoples R China
4.Univ British Columbia, Fac Land & Food Syst, Food Nutr & Hlth, Vancouver, BC V6T1Z4, Canada
关键词： Soy protein; Hemp protein; Wheat gluten; Meat analogues; Physicochemical properties; Transglutaminase; Textural properties; Protein structure
期刊名称：FOOD RESEARCH INTERNATIONAL （ 影响因子：8.0； 五年影响因子：8.5 ）
ISSN： 0963-9969
年卷期： 2025 年 208 卷
页码：
收录情况： SCI
摘要： Transglutaminase (TGase) is widely used in the production of high-moisture extruded meat analogues (HMEMA) to enhance fiber structure by promoting protein cross-linking. However, its impact on the structure, quality, and protein configuration across different extrusion zones during the preparation of meat analogues (MA) from various proteins remains unclear. This study aimed to investigate the effects of TGase on the physicochemical properties and texture of HMEMA made from soy protein (SP), hemp protein (HP), and wheat gluten (WG). A "dead stop" experiment was conducted to analyze the microstructure, protein structure, and intermolecular interaction forces of MA at different extrusion zones. The results showed that the addition of 0.18 % TGase increased the degree of texturization by 15.4 % and improved the water holding capacity (WHC) by 42.5 %. MA prepared with TGase exhibited a more distinct fiber structure, whereas those without TGase displayed a layered morphology. Furthermore, TGase significantly enhanced hydrogen bonding and hydrophobic interactions between proteins. Notably, the presence of 0.18 % TGase reduced the proportion of protein alpha-helix and beta-sheet structures in the melting zone from 60.4 % to 46.0 %, while in the extrusion zone, these structures increased from 58.2 % to 69.2 %. These findings suggest that TGase facilitates protein expansion and recombination during extrusion, thereby promoting superior fiber formation. This study underscores the crucial role of TGase in improving the textural properties of MA derived from various plant proteins, offering valuable insights for the development of MA from diverse plant protein sources.
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