Protein–Protein Interactions in High Moisture-Extruded Meat Analogs and Heat-Induced Soy Protein Gels

2007 ◽  
Vol 84 (8) ◽  
pp. 741-748 ◽  
Author(s):  
Ke Shun Liu ◽  
Fu-Hung Hsieh
Foods ◽  
2021 ◽  
Vol 10 (1) ◽  
pp. 102
Author(s):  
Patrick Wittek ◽  
Nicole Zeiler ◽  
Heike P. Karbstein ◽  
M. Azad Emin

The high moisture extrusion of plant proteins is well suited for the production of protein-rich products that imitate meat in their structure and texture. The desired anisotropic product structure of these meat analogues is achieved by extrusion at high moisture content (>40%) and elevated temperatures (>100 °C); a cooling die prevents expansion of the matrix and facilitates the formation of the anisotropic structure. Although there are many studies focusing on this process, the mechanisms behind the structure formation still remain largely unknown. Ongoing discussions are based on two very different hypotheses: structure formation due to alignment and stabilization of proteins at the molecular level vs. structure formation due to morphology development in multiphase systems. The aim of this paper is, therefore, to investigate the mechanism responsible for the formation of anisotropic structures during the high moisture extrusion of plant proteins. A model protein, soy protein isolate, is extruded at high moisture content and the changes in protein–protein interactions and microstructure are investigated. Anisotropic structures are achieved under the given conditions and are influenced by the material temperature (between 124 and 135 °C). Extrusion processing has a negligible effect on protein–protein interactions, suggesting that an alignment of protein molecules is not required for the structure formation. Instead, the extrudates show a distinct multiphase system. This system consists of a water-rich, dispersed phase surrounded by a water-poor, i.e., protein-rich, continuous phase. These findings could be helpful in the future process and product design of novel plant-based meat analogues.


MethodsX ◽  
2021 ◽  
Vol 8 ◽  
pp. 101243
Author(s):  
Caren Tanger ◽  
David J. Andlinger ◽  
Annette Brümmer-Rolf ◽  
Julia Engel ◽  
Ulrich Kulozik

1995 ◽  
Vol 62 (3) ◽  
pp. 479-489 ◽  
Author(s):  
Sylvie Marchesseau ◽  
Jean-Louis Cuq

SummaryIn order to predict the oozing susceptibility of heat-induced milk protein gels such as processed cheeses during storage, ultracentrifugation forces are required to accelerate the expulsion of water from the gel structure. Two predictive methods have been tested. Direct ultracentrifugation of processed cheese was used to study effects of centrifugal compression on the water-holding ability. The water release with optimal parameters (time, temperature and ultracentrifugation force) from a freshly manufactured processed cheese was correlated with visual assessment of oozing after 6 months storage. A second method was based on the susceptibility of gelled proteins to resist the dissociating action of solutions of chemical agents such as SDS, urea, EDTA and 2-mercaptoethanol. Most of the protein sedimented by ultracentrifugation in the presence of SDS represented that still in complexed form. This correlated with optimal water binding by the processed cheese. Response-surface methods, used to optimize the ultracentrifugation variables and the composition of the dissociation solutions, showed that the dissociation test was best with a dispersion of processed cheese in SDS solution (10 g/l) at a ratio of 1:6 (w/v) at 20°C, ultracentrifuged at 86000 g and 20°C for 25 min. Analysis of processed cheese cooked at 115°C and then dissociated in different solutions showed various protein–protein interactions in the gel network, whereas hydrophobic interactions were the most important stabilizers of the protein matrix of cheese cooked at higher temperature.


Foods ◽  
2021 ◽  
Vol 10 (7) ◽  
pp. 1517
Author(s):  
Mika Immonen ◽  
Angga Chandrakusuma ◽  
Juhani Sibakov ◽  
Minna Poikelispää ◽  
Tuula Sontag-Strohm

Grain protein fractions have great potential as ingredients that contain high amounts of valuable nutritional components. The aim of this study was to study the rheological behavior of destarched oat and pea proteins and their blends in extrusion-like conditions with a closed cavity rheometer. Additionally, the possibility of producing fibrous structures with high-moisture extrusion from a blend of destarched oat and pea protein was investigated. In the temperature sweep measurement (60–160 °C) of the destarched oat protein concentrate and pea protein isolate blend, three denaturation and polymerization sections were observed. In addition, polymerization as a function of time was recorded in the time sweep measurements. The melting temperature of grain proteins was an important factor when producing texturized structures with a high-moisture extrusion. The formation of fibrillar structures was investigated with high-moisture extrusion from the destarched oat and pea protein blend at temperatures ranging from 140 to 170 °C. The protein–protein interactions were significantly influenced in the extruded samples. This was due to a decrease in the amount of extractable protein in selective buffers. In particular, there was a decrease in non-covalent and covalent bonds due to the formation of insoluble protein complexes.


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