TY - JOUR
T1 - Structural and rheological changes of texturized mung bean protein induced by feed moisture during extrusion
AU - Hossain Brishti, Fatema
AU - Chay, Shyan Yea
AU - Muhammad, Kharidah
AU - Rashedi Ismail-Fitry, Mohammad
AU - Zarei, Mohammad
AU - Karthikeyan, Sivakumaran
AU - Caballero-Briones, F.
AU - Saari, Nazamid
N1 - Publisher Copyright:
© 2020 Elsevier Ltd
PY - 2021/5/15
Y1 - 2021/5/15
N2 - 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.
AB - 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.
KW - Extrusion
KW - Mung bean
KW - Secondary structure
KW - Structural properties
KW - Sustainable food
KW - Texturized vegetable protein
UR - http://www.scopus.com/inward/record.url?scp=85096823419&partnerID=8YFLogxK
U2 - 10.1016/j.foodchem.2020.128643
DO - 10.1016/j.foodchem.2020.128643
M3 - Artículo
C2 - 33246681
AN - SCOPUS:85096823419
SN - 0308-8146
VL - 344
JO - Food Chemistry
JF - Food Chemistry
M1 - 128643
ER -