High moisture extrusion cooking of pea protein isolates: Raw material characteristics, extruder responses, and texture properties

2014 ◽  
Vol 127 ◽  
pp. 67-74 ◽  
Author(s):  
Raffael Osen ◽  
Simone Toelstede ◽  
Florian Wild ◽  
Peter Eisner ◽  
Ute Schweiggert-Weisz
Keyword(s):  
Raw Material ◽  
Extrusion Cooking ◽  
High Moisture ◽  
Protein Isolates ◽  
Pea Protein ◽  
Texture Properties ◽  
Material Characteristics ◽  
High Moisture Extrusion

scholarly journals High-Moisture Meat Analogues Produced from Yellow Pea and Faba Bean Protein Isolates/Concentrate: Effect of Raw Material Composition and Extrusion Parameters on Texture Properties

Foods ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 843
Author(s):  
Ferawati Ferawati ◽  
Izalin Zahari ◽  
Malin Barman ◽  
Mohammed Hefni ◽  
Cecilia Ahlström ◽  
...  
Keyword(s):  
Faba Bean ◽  
Genetically Modified Organisms ◽  
Extrusion Process ◽  
Raw Material ◽  
High Moisture ◽  
Protein Isolates ◽  
Factors Affecting ◽  
Texture Properties ◽  
Meat Analogue ◽  
Bean Protein

Yellow pea and faba bean are potential candidates to replace soybean-based ingredients due to their suitability for cultivation in the northern hemisphere, non-genetically modified organisms cultivation practice and low risk of allergenicity. This study examined the functionality of local yellow pea and faba bean protein isolates/concentrate as meat analogue products. The most critical factors affecting the texture properties of meat analogue were also determined. Extrusion was used to produce high-moisture meat analogues (HMMAs) from yellow pea and faba bean protein isolates/concentrates and HMMAs with fibrous layered structures was successfully produced from both imported commercial and local sources. The texture properties of the HMMA produced were mainly affected by the ash, fiber and protein content and water-holding capacity of the source protein. Three extrusion process parameters (target moisture content, extrusion temperature, screw speed), also significantly affected HMMA texture. In conclusion, functional HMMA can be produced using protein isolates derived from locally grown pulses.

scholarly journals Comparison of Whole and Gutted Baltic Herring as a Raw Material for Restructured Fish Product Produced by High-Moisture Extrusion Cooking

Foods ◽  
2020 ◽  
Vol 9 (11) ◽  
pp. 1541
Author(s):  
Anni Nisov ◽  
Heikki Aisala ◽  
Ulla Holopainen-Mantila ◽  
Hanna-Leena Alakomi ◽  
Emilia Nordlund ◽  
...  
Keyword(s):  
Hybrid Plant ◽  
Environmental Benefits ◽  
Raw Material ◽  
Human Consumption ◽  
Extrusion Cooking ◽  
High Moisture ◽  
Baltic Herring ◽  
Fish Product ◽  
Sensory Profiles ◽  
High Moisture Extrusion

Interest in using undervalued forage fish for human consumption has recently increased due to its environmental benefits. However, feasible strategies to process the undervalued fish species to food use are limited. Therefore, this study investigated the possibility to utilise whole (ungutted) Baltic herring as a raw material for hybrid plant-fish meat analogues produced by high-moisture extrusion cooking. The sample properties were compared with ungutted Baltic herring. Produced meat analogues showed sufficiently high microbial quality, with spoilage microbes showing growth levels of under 1.4 log CFU/g. Whole fish and gutted fish extrudates showed uniform flavour- and odour-related sensory profiles. Colour values of the whole fish (L* 57.8) extrudates were similar to the values of gutted fish extrudates (L* 62.0). The whole and gutted fish extrudates had tensile strength in a cross-cut direction of 25.5 and 46.3 kPa, respectively. This correlated with the tearing force of the extrudates analysed by a trained sensory panel. Furthermore, a more explicit protein network was microscopically observed in gutted fish than in whole fish extrudates. The present study showed that high-moisture extrusion cooking enables the use of whole small-sized fish for human consumption.

scholarly journals Thermo-mechanical processing of plant proteins using shear cell and high-moisture extrusion cooking

2021 ◽  
pp. 1-18
Author(s):  
Steven H. V. Cornet ◽  
Silvia J. E. Snel ◽  
Floor K. G. Schreuders ◽  
Ruud G. M. van der Sman ◽  
Michael Beyrer ◽  
...  
Keyword(s):  
Extrusion Cooking ◽  
Mechanical Processing ◽  
Plant Proteins ◽  
High Moisture ◽  
Shear Cell ◽  
High Moisture Extrusion

scholarly journals Texturization of a Blend of Pea and Destarched Oat Protein Using High-Moisture Extrusion

Foods ◽  
2021 ◽  
Vol 10 (7) ◽  
pp. 1517
Author(s):  
Mika Immonen ◽  
Angga Chandrakusuma ◽  
Juhani Sibakov ◽  
Minna Poikelispää ◽  
Tuula Sontag-Strohm
Keyword(s):  
Protein Interactions ◽  
Protein Complexes ◽  
Protein Isolate ◽  
Protein Protein Interactions ◽  
High Moisture ◽  
Covalent Bonds ◽  
Closed Cavity ◽  
Pea Protein ◽  
Extractable Protein ◽  
High Moisture Extrusion

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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