Mung bean is gaining attention as a sustainable and economic source of plant protein. The current study evaluates the techno-functionality, anti-nutrient properties, in vivo protein quality and toxicity of texturized mung bean protein (TMBP) produced under optimized conditions. Our work successfully produces TMBP with improved techno-functionalities that are crucial for meat-based food applications, credited to retained juiciness and fat-binding ability. Alkaline extraction and extrusion significantly reduce trypsin inhibitor, phytic acid and tannin content in TMBP. An in vivo study using Sprague-Dawley rats reveals the good protein quality of TMBP, with a true protein digestibility of 99.26% resembling casein (99.36%, control protein), a net protein utilization of 63.99% and a biological value of 64.46%. The good protein quality, increased lean muscle mass along with reduced cholesterol and triglyceride secures TMBP's potential as a Protein meal replacer and dietary suplement. Non-toxicity of TMBP is confirmed by normal serum biochemical parameters and healthy organs, ascertaining the safety of alkaline extraction. The current study elucidates the production of TMBP with improved techno-functionalities (for meat-based food applications), reduced anti-nutritional factors and high quality (for weight-watchers and malnourished individuals).
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.
The mangosteen pericarp contains unstable non-acylated ACNs, rendering it prone to degradation. Therefore, intermolecular copigmentation of semi-purified ACNs (SPA) with tartaric acid (SPA-TA), sinapic acid (SPA-SA), catechin (SPA-CE), and sucrose (SPA-SU) in 1:5 and 1:10 M ratios were used to increase their stability during storage for 77 days at 25 ± 1 °C in pH 3 buffer solution. The SPA-TA1:5 complex showed the significant highest stability of total monomeric ACN content (TMAC) with a half-life (t1/2) = 56.9 days, cyanidin-3-O-sophoroside (C3S) with t1/2 = 48.1 days and color retention (69.80 %) compare to SPA with TMAC (t1/2 = 37.4), C3S (t1/2 = 13.3) and color retention (57.2 %) after 49 days (p