Structuring camellia seed-derived oleosomes for the fabrication of meat analogs using transglutaminase: Structural, functional, and rheological properties
Shahzad Farooq , Muhammad Ijaz Ahmad , Shijie Zheng , Usman Ali , Yipeng Zhang , Jiawen Xue , Yang Li , Cui Shixiu , Hui Zhang
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引用次数: 0
Abstract
Presently, protein-based meat analogs fabricated via the extrusion process still cannot fully meet consumers' requirements, particularly in terms of replicating the real meat fiber that contains solid fat. This study introduced a facile approach to fabricating real meat analogs using plant-derived oleosomes (0–40 wt%) as lipid droplets, which were crosslinked with texturized soy-wheat gluten proteins (50 wt%) through a transglutaminase-induced reaction (0–50 U/g). FTIR and SDS-PAGE analyses confirmed that transglutaminase induction enabled oleosome-associated proteins to crosslink with texturized proteins through covalent bonds rather than non-covalent interactions. Microstructural analyses indicated that uncross-linked meat analogs contained an evenly distributed array of isolated oleosomes, whereas those with higher transglutaminase contents exhibited a compact and homogeneous 3D network of aggregated oleosomes and proteins. Analysis of appearance and colorimetry showed that color changes in meat analogs depended on oleosomes, which increased lightness and decreased redness, effectively changing the rough and uneven appearance of meat analogs into a smoother and more homogeneous one. Compared to control sample, elevated concentrations of oleosomes (0–40 wt%) and transglutaminase (0–50 U/g) led to increased critical strain (1.02–100.4 %), storage modulus (310–820 kPa), and structure-recovery ability (56.62–89.38 %), while decreased activation energy (16.16–7.12 kJ/mol). This indicated that oleosomes, which are integrated and assembled with proteins by enzymatic action, acted as “active fillers”, effectively strengthening the gel matrices. Additionally, Lissajous-Bowditch analysis best described the influence of filler/protein interactions on the gel matrices, showing a transition of meat analogs from viscoelastic to strongly elastic gels, resisting structural breakdown due to intensified covalent interactions and interconnected networks.
期刊介绍:
Food Hydrocolloids publishes original and innovative research focused on the characterization, functional properties, and applications of hydrocolloid materials used in food products. These hydrocolloids, defined as polysaccharides and proteins of commercial importance, are added to control aspects such as texture, stability, rheology, and sensory properties. The research's primary emphasis should be on the hydrocolloids themselves, with thorough descriptions of their source, nature, and physicochemical characteristics. Manuscripts are expected to clearly outline specific aims and objectives, include a fundamental discussion of research findings at the molecular level, and address the significance of the results. Studies on hydrocolloids in complex formulations should concentrate on their overall properties and mechanisms of action, while simple formulation development studies may not be considered for publication.
The main areas of interest are:
-Chemical and physicochemical characterisation
Thermal properties including glass transitions and conformational changes-
Rheological properties including viscosity, viscoelastic properties and gelation behaviour-
The influence on organoleptic properties-
Interfacial properties including stabilisation of dispersions, emulsions and foams-
Film forming properties with application to edible films and active packaging-
Encapsulation and controlled release of active compounds-
The influence on health including their role as dietary fibre-
Manipulation of hydrocolloid structure and functionality through chemical, biochemical and physical processes-
New hydrocolloids and hydrocolloid sources of commercial potential.
The Journal also publishes Review articles that provide an overview of the latest developments in topics of specific interest to researchers in this field of activity.