Structural and rheological changes of texturized mung bean protein induced by feed moisture during extrusion
Mung bean protein isolate was texturized at different feed moisture contents (30.0, 49.3, and 60.0%) at a constant temperature (144.57 °C) to evaluate the changes in protein profile, solubility, thermal, structural (at secondary and tertiary levels) and rheological properties. SDS-PAGE, surface hydr...
| 發表在: | Food Chemistry |
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| 格式: | Article |
| 語言: | English |
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Elsevier Ltd
2021
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| 在線閱讀: | https://www.scopus.com/inward/record.uri?eid=2-s2.0-85096823419&doi=10.1016%2fj.foodchem.2020.128643&partnerID=40&md5=256662415c28757af2197d55465de79f |
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Hossain Brishti F.; Chay S.Y.; Muhammad K.; Rashedi Ismail-Fitry M.; Zarei M.; Karthikeyan S.; Caballero-Briones F.; Saari N. |
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Hossain Brishti F.; Chay S.Y.; Muhammad K.; Rashedi Ismail-Fitry M.; Zarei M.; Karthikeyan S.; Caballero-Briones F.; Saari N. 2-s2.0-85096823419 Structural and rheological changes of texturized mung bean protein induced by feed moisture during extrusion 2021 Food Chemistry 344 10.1016/j.foodchem.2020.128643 https://www.scopus.com/inward/record.uri?eid=2-s2.0-85096823419&doi=10.1016%2fj.foodchem.2020.128643&partnerID=40&md5=256662415c28757af2197d55465de79f Mung bean protein isolate was texturized at different feed moisture contents (30.0, 49.3, and 60.0%) at a constant temperature (144.57 °C) to evaluate the changes in protein profile, solubility, thermal, structural (at secondary and tertiary levels) and rheological properties. SDS-PAGE, surface hydrophobicity, circular dichroism, FTIR spectroscopy, and fluorescence analyses revealed protein unfolding, aggregation, and structural rearrangement as a function of feed moisture content. Extrusion at 49.3% feed moisture produced texturized mung bean protein (TMBP) with favourable partial denaturation, the formation of small aggregates, improved solubility, and digestibility with strong gel forming behaviour, whereas 30.0 and 60.0% moisture content resulted in complete protein denaturation, the undesirable formation of large aggregates and weak gels. In conclusion, protein denaturation and formation of aggregates can be controlled by manipulating feed moisture content during extrusion, with 49.3% feed moisture prompting favourable partial denaturation to produce TMBP with desirable qualities for use as a vegetarian-based meat extender. © 2020 Elsevier Ltd Elsevier Ltd 3088146 English Article |
| author |
2-s2.0-85096823419 |
| spellingShingle |
2-s2.0-85096823419 Structural and rheological changes of texturized mung bean protein induced by feed moisture during extrusion |
| author_facet |
2-s2.0-85096823419 |
| author_sort |
2-s2.0-85096823419 |
| title |
Structural and rheological changes of texturized mung bean protein induced by feed moisture during extrusion |
| title_short |
Structural and rheological changes of texturized mung bean protein induced by feed moisture during extrusion |
| title_full |
Structural and rheological changes of texturized mung bean protein induced by feed moisture during extrusion |
| title_fullStr |
Structural and rheological changes of texturized mung bean protein induced by feed moisture during extrusion |
| title_full_unstemmed |
Structural and rheological changes of texturized mung bean protein induced by feed moisture during extrusion |
| title_sort |
Structural and rheological changes of texturized mung bean protein induced by feed moisture during extrusion |
| publishDate |
2021 |
| container_title |
Food Chemistry |
| container_volume |
344 |
| container_issue |
|
| doi_str_mv |
10.1016/j.foodchem.2020.128643 |
| url |
https://www.scopus.com/inward/record.uri?eid=2-s2.0-85096823419&doi=10.1016%2fj.foodchem.2020.128643&partnerID=40&md5=256662415c28757af2197d55465de79f |
| description |
Mung bean protein isolate was texturized at different feed moisture contents (30.0, 49.3, and 60.0%) at a constant temperature (144.57 °C) to evaluate the changes in protein profile, solubility, thermal, structural (at secondary and tertiary levels) and rheological properties. SDS-PAGE, surface hydrophobicity, circular dichroism, FTIR spectroscopy, and fluorescence analyses revealed protein unfolding, aggregation, and structural rearrangement as a function of feed moisture content. Extrusion at 49.3% feed moisture produced texturized mung bean protein (TMBP) with favourable partial denaturation, the formation of small aggregates, improved solubility, and digestibility with strong gel forming behaviour, whereas 30.0 and 60.0% moisture content resulted in complete protein denaturation, the undesirable formation of large aggregates and weak gels. In conclusion, protein denaturation and formation of aggregates can be controlled by manipulating feed moisture content during extrusion, with 49.3% feed moisture prompting favourable partial denaturation to produce TMBP with desirable qualities for use as a vegetarian-based meat extender. © 2020 Elsevier Ltd |
| publisher |
Elsevier Ltd |
| issn |
3088146 |
| language |
English |
| format |
Article |
| accesstype |
|
| record_format |
scopus |
| collection |
Scopus |
| _version_ |
1828987870481743872 |