Interfacial and foam-stabilizing properties of Mung bean and Pigeon pea proteins obtained from wet conventional extraction

IntroductionThe structuring of plant-based meat alternatives is a complex process which is highly dependent on qualitative and quantitative proportion of different ingredients. In the present study, starch, protein, and oil concentrations were optimized for the formulation of meat alternative (MA) using response surface methodology (RSM).MethodsProtein isolates of mung bean and pea protein, & corn starch were used along with sunflower oil to formulate meat alternatives using heat-induced gelation. The protein functionality of mungbean protein isolate (MBPI) and pea protein isolate (PPI) were analyzed. In addition, the effects of constituent composition on the physicochemical properties of meat alternatives were studied using RSM.ResultsThe protein content exhibited an elevation with increased levels of MBPI and PPI in 15:15 ratio. Moisture and hardness were chiefly influenced by oil content, as they displayed a decline with increasing oil levels. The color (L*) was principally affected by starch and oil, where the L* reduced with increasing levels of both variables. Springiness was influenced by the interaction of protein ratio (MBPI:PPI) and starch, as it showed a lowest value at the lowest level of protein and the highest level of starch. Chewiness was influenced by the interaction of hardness and springiness. The microstructure analysis showed dense protein matrix in the meat alternative.DiscussionOverall, the study shows that starch facilitated the structuring of meat alternative formulated using MBPI and PPI which could be utilized as potential materials for enhanced textural properties of the meat alternatives.

Deciphering the gastrointestinal fate of four heat-treated legume proteins: Focus on digestive characteristics and peptide profiles.

Structural and rheological properties of mung bean protein emulsion as a liquid egg substitute: The effect of pH shifting and calcium

Characterization of mung bean endogenous proteases and globulins and their effects on the production of mung bean protein

Fat crystallization and physical characteristics of mung bean protein-based frozen whipped emulsions: Effect of lipophilic surfactants and quinoa hydrolysate

B.J.F. Hudson Developments in food proteins — 7 1991 Elsevier £65.00 (ix + 278 pages) ISBN 1 85166 535 8

Optimizing whey isolate protein/mung bean protein ratios in emulsion gels for enhanced dihydroquercetin delivery: Gel properties, stability, and bioaccessibility insights.

High internal-phase pickering emulsions stabilized by mung bean protein-glycyrrhizin complexes for β-carotene delivery.

The aim of this study was to isolate, purify, and characterize a novel peptide with zinc-binding ability from mung bean protein hydrolysates obtained by alcalase. The peptide purification process was performed using ultrafiltration, TSK-GEL size-exclusion chromatography, and reversed-phase high-performance liquid chromatography (RP-HPLC). The molecular weight of the isolated peptide was determined by liquid chromatography–electrospray ionization mass spectrometry (LC–ESI/MS) and found to be 1192.56 Da with amino acid sequence SSEDQPFNLR. The identified peptide showed zinc-binding capacity of 80.82 mg/g, which is 55.09% higher than that of the original mung bean protein hydrolyzate. Moreover, UV–vis and FTIR spectra indicated that the zinc-binding sites on the peptide were nitrogen atoms of amide, terminal amino group, and oxygen atoms on the carboxyl group. Moreover, zinc-releasing experiments showed that the peptide–zinc chelate is highly soluble under both acidic and alkaline conditions. Furthermore, the identified peptide significantly promoted the transportation and absorption of zinc ions in Caco-2 cell model. These findings indicate a potential for production of zinc-binding peptide from mung bean protein for the utilization as ingredient in functional foods.

Enhancing whipped cream anti-freeze properties: A dual plant system with aquafaba and mung bean protein

Mung bean (Vigna radiata) as probiotic food through fermentation with Lactobacillus plantarum B1-6

Mung bean (Vigna radiata L.) is a protein-rich pulse mainly cultivated in Asia, where its consumption has been associated with positive health outcomes. Mung bean protein is especially rich in leucine, lysine, phenylalanine, and tyrosine amino acids and it contains the 8S α-globulin as the major seed storage protein. Protein derived products from pulses, such as protein concentrates, hydrolysates, and purified peptide fractions are becoming popular functional foods. Mung bean peptides are enzymatically generated using gastrointestinal and non-gastrointestinal proteases. Protein hydrolysates generated by one or a combination of enzymes have been demonstrated to exert different biological potentials, including antioxidant, antihypertensive, anticancer, and hypocholesterolemic effects. These properties are attributed to the amino acid sequences, the type of enzyme used for hydrolysis, and the purification method. More robust experimental designs must be performed to understand the role and mechanisms of these bioactive peptides with in vivo studies and clinical trials. Furthermore, there is a lack of information related to the incorporation of bioactive peptides into a food matrix while preserving their bioactivity. This chapter provides an overview of the central aspects of mung bean physical structure and chemical composition, protein characteristics, enzymatic production, and the biological potential of mung bean protein hydrolysates and peptides.

Influence of pH-shifting and transglutaminase on the freeze-thaw stability and thermal gel properties of mung bean protein-based liquid egg substitute prepared with two different oil phases

Protein isolates deliver functionalities such as gelling, emulsifying, and foaming, and many recent publications are reporting the functionality of new protein isolates produced in the laboratory. Laboratory protein isolation processes are quite different to industrial processes, and therefore isolate functionalities are likely to be different. We examined some of the differences between laboratory isolates and commercial isolates of mung bean and chickpea protein (MPBI and CPPI). We tested solubility as a function of pH, dispersibility by static light scattering, and viscosity enhancement in a rapid visco analyzer (RVA). Thermal transitions were evaluated with differential scanning calorimetry (DSC), and powder morphology was examined by scanning electron microscopy (SEM). Laboratory isolates were more soluble (e.g. 54%–57% vs. 5%–45% at pH 8) and dispersible than commercial isolates, with the largest DSC endotherms, indicating the least denaturation. Among commercial isolates, we found large differences in solubility, thermal properties, and viscosity enhancement, and minor differences in dispersibility and powder morphology. The hydration protocol had a strong effect on solubility and DSC results, and a moderate effect on RVA results. Comparisons between isolates produced in different laboratories are currently hampered by the use of nonstandard empirical methods for certain functionalities, and we highlight standardized methods for measuring dispersibility and viscosity enhancement. Protein isolation processes affect isolate functionality via effects on protein denaturation and aggregation, and via the morphology and surface chemistry of isolate powders. This means that findings with laboratory isolates cannot necessarily be extrapolated to commercial counterparts but also indicates the power of process design to modulate isolate functionality.

Fabrication, molecular mechanism, and property characterization of chicken 3D-analogs using protein-protein multiple-ligand interactions.