Extrusion of food proteins
Protein extrusion has frustrated earlier predictions regarding its impact in the development of food products. The main reason for this disappointing performance has been its failure to yield fabricated food products with textural quality close enough to that of natural products at competitive prices. Texturized soya protein by extrusion is presently the only commercial success in this area, being incorporated into several convenience products, increasing their protein content and quality and conferring them some desirable sensory properties. Technological and scientific gaps in the extrusion texturization are still to be bridged if this technique is to be applied for upgrading unconventional protein. The precise mechanisms responsible for protein texturization through extrusion are still unclear. Proteins show a very wide range of extrusion behavior that is probably related to large differences in their association properties. New peptide bonds, formed by free amino and carboxylic groups of the protein, were postulated as being responsible for the cross-linking that takes place in protein extrusion. However, disulfide bonds and electrostatic and hydrophobic interactions are regarded presently as the texturization mechanism in this process. The recently suggested suspension (or filled "melt") model for biopolymer extrusion offered a new framework for testing extrusion of novel proteins. According to this view, the large differences between the association properties of proteins produce different types of aggregates. Some of them can be insoluble under extrusion conditions and act as a dispersed phase within the melt phase. The extrusion performance of a protein will thus depend on the amount of insoluble aggregate produced inside the extruder and on protein-protein interactions that occur after the superheated molten mass leaves it.
| Medienart: |
Artikel |
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| Erscheinungsjahr: |
1992 |
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| Erschienen: |
1992 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:32 |
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| Enthalten in: |
Critical reviews in food science and nutrition - 32(1992), 4 vom: 15., Seite 365-92 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Arêas, J A [VerfasserIn] |
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| Themen: |
Dietary Proteins |
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| Anmerkungen: |
Date Completed 04.05.1993 Date Revised 16.01.2019 published: Print Citation Status MEDLINE |
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| Förderinstitution / Projekttitel: |
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NLM012782203 |
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| 500 | |a Date Completed 04.05.1993 | ||
| 500 | |a Date Revised 16.01.2019 | ||
| 500 | |a published: Print | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Protein extrusion has frustrated earlier predictions regarding its impact in the development of food products. The main reason for this disappointing performance has been its failure to yield fabricated food products with textural quality close enough to that of natural products at competitive prices. Texturized soya protein by extrusion is presently the only commercial success in this area, being incorporated into several convenience products, increasing their protein content and quality and conferring them some desirable sensory properties. Technological and scientific gaps in the extrusion texturization are still to be bridged if this technique is to be applied for upgrading unconventional protein. The precise mechanisms responsible for protein texturization through extrusion are still unclear. Proteins show a very wide range of extrusion behavior that is probably related to large differences in their association properties. New peptide bonds, formed by free amino and carboxylic groups of the protein, were postulated as being responsible for the cross-linking that takes place in protein extrusion. However, disulfide bonds and electrostatic and hydrophobic interactions are regarded presently as the texturization mechanism in this process. The recently suggested suspension (or filled "melt") model for biopolymer extrusion offered a new framework for testing extrusion of novel proteins. According to this view, the large differences between the association properties of proteins produce different types of aggregates. Some of them can be insoluble under extrusion conditions and act as a dispersed phase within the melt phase. The extrusion performance of a protein will thus depend on the amount of insoluble aggregate produced inside the extruder and on protein-protein interactions that occur after the superheated molten mass leaves it | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 4 | |a Review | |
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| 650 | 7 | |a Plant Proteins |2 NLM | |
| 650 | 7 | |a Proteins |2 NLM | |
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