Mechanical and rheological effects of transglutaminase treatment on dense plant protein blends
Pea protein isolate (PPI) and mung bean protein isolate (MBPI) are rising alternatives for soy protein isolate in producing meat analogues. Transforming these isolates into full products is challenging due to their differences in functional properties compared with soy. Here, we report on the use of transglutaminase to improve the mechanical and rheological properties of dense MBPI and PPI dispersions. Gels from PPI and MBPI (40 wt% dry matter) were produced with 0, 0.1, 0.3, 0.5, and 0.7 wt% transglutaminase and incubation temperatures of 30, 40, 50, and 60 °C. Their mechanical and rheological properties were determined by tensile and closed cavity rheometer tests. The degree of crosslinking was determined by the OPA assay. Transglutaminase significantly increased fracture stress and strain of PPI gels, and to a lesser extent those of MBPI gels. The degree of free amino confirmed that this increase in PPI was due to formation of additional crosslinks. Amplitude sweeps identified that the rheological properties of PPI gels and MBPI gels were affected by the addition of transglutaminase, but in an opposite manner. Stress relaxation experiments showed that transglutaminase increased the elasticity of PPI gels and formed mainly small aggregates in MBPI gels. This work showed that the fibrous structure diminished when >0.1 wt% transglutaminase was added to PPI/MBPI - wheat gluten blends. To conclude, transglutaminase can be used to create intermolecular crosslinks in PPI gels, creating a full network, while mostly intramolecular crosslinks are formed in MBPI gels, leading to a cluster structure.
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| Format: | Article/Letter to editor biblioteca |
| Language: | English |
| Subjects: | Mechanical properties, Mung bean protein isolate, Pea protein isolate, Rheological properties, Transglutaminase, |
| Online Access: | https://research.wur.nl/en/publications/mechanical-and-rheological-effects-of-transglutaminase-treatment- |
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dig-wur-nl-wurpubs-6051112024-12-04 Schlangen, Miek Ribberink, Marieke A. Taghian Dinani, Somayeh Sagis, Leonard M.C. van der Goot, Atze Jan Article/Letter to editor Food Hydrocolloids 136 (2023) Part A ISSN: 0268-005X Mechanical and rheological effects of transglutaminase treatment on dense plant protein blends 2023 Pea protein isolate (PPI) and mung bean protein isolate (MBPI) are rising alternatives for soy protein isolate in producing meat analogues. Transforming these isolates into full products is challenging due to their differences in functional properties compared with soy. Here, we report on the use of transglutaminase to improve the mechanical and rheological properties of dense MBPI and PPI dispersions. Gels from PPI and MBPI (40 wt% dry matter) were produced with 0, 0.1, 0.3, 0.5, and 0.7 wt% transglutaminase and incubation temperatures of 30, 40, 50, and 60 °C. Their mechanical and rheological properties were determined by tensile and closed cavity rheometer tests. The degree of crosslinking was determined by the OPA assay. Transglutaminase significantly increased fracture stress and strain of PPI gels, and to a lesser extent those of MBPI gels. The degree of free amino confirmed that this increase in PPI was due to formation of additional crosslinks. Amplitude sweeps identified that the rheological properties of PPI gels and MBPI gels were affected by the addition of transglutaminase, but in an opposite manner. Stress relaxation experiments showed that transglutaminase increased the elasticity of PPI gels and formed mainly small aggregates in MBPI gels. This work showed that the fibrous structure diminished when >0.1 wt% transglutaminase was added to PPI/MBPI - wheat gluten blends. To conclude, transglutaminase can be used to create intermolecular crosslinks in PPI gels, creating a full network, while mostly intramolecular crosslinks are formed in MBPI gels, leading to a cluster structure. en application/pdf https://research.wur.nl/en/publications/mechanical-and-rheological-effects-of-transglutaminase-treatment- 10.1016/j.foodhyd.2022.108261 https://edepot.wur.nl/581645 Mechanical properties Mung bean protein isolate Pea protein isolate Rheological properties Transglutaminase https://creativecommons.org/licenses/by/4.0/ https://creativecommons.org/licenses/by/4.0/ Wageningen University & Research |
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Mechanical properties Mung bean protein isolate Pea protein isolate Rheological properties Transglutaminase Mechanical properties Mung bean protein isolate Pea protein isolate Rheological properties Transglutaminase |
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Mechanical properties Mung bean protein isolate Pea protein isolate Rheological properties Transglutaminase Mechanical properties Mung bean protein isolate Pea protein isolate Rheological properties Transglutaminase Schlangen, Miek Ribberink, Marieke A. Taghian Dinani, Somayeh Sagis, Leonard M.C. van der Goot, Atze Jan Mechanical and rheological effects of transglutaminase treatment on dense plant protein blends |
| description |
Pea protein isolate (PPI) and mung bean protein isolate (MBPI) are rising alternatives for soy protein isolate in producing meat analogues. Transforming these isolates into full products is challenging due to their differences in functional properties compared with soy. Here, we report on the use of transglutaminase to improve the mechanical and rheological properties of dense MBPI and PPI dispersions. Gels from PPI and MBPI (40 wt% dry matter) were produced with 0, 0.1, 0.3, 0.5, and 0.7 wt% transglutaminase and incubation temperatures of 30, 40, 50, and 60 °C. Their mechanical and rheological properties were determined by tensile and closed cavity rheometer tests. The degree of crosslinking was determined by the OPA assay. Transglutaminase significantly increased fracture stress and strain of PPI gels, and to a lesser extent those of MBPI gels. The degree of free amino confirmed that this increase in PPI was due to formation of additional crosslinks. Amplitude sweeps identified that the rheological properties of PPI gels and MBPI gels were affected by the addition of transglutaminase, but in an opposite manner. Stress relaxation experiments showed that transglutaminase increased the elasticity of PPI gels and formed mainly small aggregates in MBPI gels. This work showed that the fibrous structure diminished when >0.1 wt% transglutaminase was added to PPI/MBPI - wheat gluten blends. To conclude, transglutaminase can be used to create intermolecular crosslinks in PPI gels, creating a full network, while mostly intramolecular crosslinks are formed in MBPI gels, leading to a cluster structure. |
| format |
Article/Letter to editor |
| topic_facet |
Mechanical properties Mung bean protein isolate Pea protein isolate Rheological properties Transglutaminase |
| author |
Schlangen, Miek Ribberink, Marieke A. Taghian Dinani, Somayeh Sagis, Leonard M.C. van der Goot, Atze Jan |
| author_facet |
Schlangen, Miek Ribberink, Marieke A. Taghian Dinani, Somayeh Sagis, Leonard M.C. van der Goot, Atze Jan |
| author_sort |
Schlangen, Miek |
| title |
Mechanical and rheological effects of transglutaminase treatment on dense plant protein blends |
| title_short |
Mechanical and rheological effects of transglutaminase treatment on dense plant protein blends |
| title_full |
Mechanical and rheological effects of transglutaminase treatment on dense plant protein blends |
| title_fullStr |
Mechanical and rheological effects of transglutaminase treatment on dense plant protein blends |
| title_full_unstemmed |
Mechanical and rheological effects of transglutaminase treatment on dense plant protein blends |
| title_sort |
mechanical and rheological effects of transglutaminase treatment on dense plant protein blends |
| url |
https://research.wur.nl/en/publications/mechanical-and-rheological-effects-of-transglutaminase-treatment- |
| work_keys_str_mv |
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| _version_ |
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