Mung bean is an inexpensive yet sustainable protein source. Current work compared the effects of freeze (FD), spray (SD) and oven drying (OD), on mung bean protein isolate (MBPI) produced on pilot scale. All samples showed no dissociation of protein subunits and were thermally stable (Td = 157.90-158.07 °C). According to morphological studies, FD formed a porous protein while SD and OD formed wrinkled and compact crystals, respectively. FD and SD formed elastic gels with better gelling capacity than OD (aggregated gel). FD showed exceptional protein solubility, water and oil absorption capacity (4.23 g/g and 8.38 g/g, respectively). SD demonstrated the smallest particle size, excellent emulsion activity index (29.21 m2/g) and stability (351.90 min) and the highest β-sheet amount (37.61%). FTIR spectra for all samples showed characteristic peaks which corresponded well to the secondary structure of legume proteins. Rheological analysis revealed that gelation temperature for all MBPI lied around 90 °C. Current work described the different final properties achieved for MBPI produced under different drying techniques that allowed tailoring for different food systems, whereby FD is ideal for meat extender, SD is suitable for meat emulsion while OD is suitable in general protein-based application.
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).
Rice bran protein concentrates (RBPC) were extracted using mild alkaline solvents (pH: 8, 9, 10). The physicochemical, thermal, functional, and structural aspects of freeze-drying (FD) and spray-drying (SD) were compared. FD and SD of RBPC had porous and grooved surfaces, with FD having non-collapsed plates and SD being spherical. Alkaline extraction increases FD's protein concentration and browning, whereas SD inhibits browning. According to amino acid profiling, RBPC-FD9's extraction optimizes and preserves amino acids. A tremendous particle size difference was prominent in FD, thermally stable at a minimal maximum of 92 °C. Increased pH extraction gives FD greater exposal surface hydrophobicity and positively relates to denaturation enthalpy. Mild pH extraction and drying significantly impacted solubility, improved emulsion properties, and foaming properties of RBPC as observed in acidic, neutral, and alkaline environments. RBPC-FD9 and RBPC-SD10 extracts exhibit outstanding foaming and emulsion activity in all pH conditions, respectively. Appropriate drying selection, RBPC-FD or SD potentially employed as foaming/emulsifier agent or meat analog.