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...

Full description

Bibliographic Details
Published in:Food Chemistry
Main Author: 2-s2.0-85096823419
Format: Article
Language:English
Published: Elsevier Ltd 2021
Online Access:https://www.scopus.com/inward/record.uri?eid=2-s2.0-85096823419&doi=10.1016%2fj.foodchem.2020.128643&partnerID=40&md5=256662415c28757af2197d55465de79f
Description
Summary: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
ISSN:3088146
DOI:10.1016/j.foodchem.2020.128643