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Bean proteins, known for their sustainability, versatility, and high nutritional value, represent a valuable yet underutilized resource, receiving less industrial attention compared to soy and pea proteins. This review examines the structural and molecular characteristics, functional properties, amino acid composition, nutritional value, antinutritional factors, and digestibility of bean proteins. Their applications in various food systems, including baked goods, juice and milk substitutes, meat alternatives, edible coatings, and 3D printing inks, are discussed. The physiological benefits of bean proteins, such as antidiabetic, cardioprotective, antioxidant, and neuroprotective effects, are also presented, highlighting their potential for promoting well-being. Our review emphasizes the diversity of bean proteins and highlights ultrasound as the most effective extraction method among available techniques. Beyond their physiological benefits, bean proteins significantly enhance the structural, technological, and nutritional properties of food systems. The functionality can be further improved through various modification techniques, thereby expanding their applicability in the food industry. While studies have explored the impact of bean protein structure on their nutritional and functional properties, further research is needed to investigate advanced modification techniques and the structure-function relationship. This will enhance the utilization of bean proteins in innovative and sustainable food applications., Competing Interests: Declaration of competing interest The authors declare no conflict of interest in submitting this manuscript., (Copyright © 2025 Elsevier B.V. All rights reserved.)

Peanut protein concentrates (PPCs) were subjected to hydrolysis by crude protease extract (CPE) obtained from three fungi viz; Rhizopus oligosporus, Trichoderma reesei, and Aspergillus oryzae and the effect on structural, functional and in-vitro protein digestibility (IVPD) properties were studied. Particle size was found significantly ( p  ≤ 0.05) lower in hydrolyzed samples than un-treated samples. Fourier transform infrared spectroscopy (FTIR) spectrum of hydrolyzed samples displayed intense absorbance peaks in the wavelength ranging from 1500 to 2600 cm -1 . Peanut protein concentrates hydrolyzed by CPE from R. oligosporus showed higher surface hydrophobicity (564.18). Total sulfhydryl content was found lower in all the hydrolyzed samples whereas, reverse trend was observed for exposed sulfhydryl content. The structural changes simultaneously affected the functional and IVPD attributes of hydrolyzed PPCs. In comparison to the PPCs hydrolysed using crude extracts from T. reesei and R. oligosporus, PPCs hydrolysed by A, oryzae showed higher solubility, water and oil binding capacity, foaming capacity and foam stability. Higher IVPD values of 86.70% was also found in PPCs hydrolyzed with CPE of A. oryzae . The study established that CPE hydrolysis of PPCs has potential for scale-up studies and may serve as a cost effective alternative to protein hydrolysis with pure enzymes., Competing Interests: Conflict of interestThe authors declare that there is no conflict of interest in the present study., (© Association of Food Scientists & Technologists (India) 2021.)

The synthesis of β-(C3)-functionalized pyrroles is a challenging task and requires a multistep protocol. An operationally simple direct catalytic synthesis of β-substituted pyrroles has been developed. This one-pot multicomponent method combined aqueous succinaldehyde as 1,4-dicarbonyl, primary amines, and isatins to access hydroxyl-oxindole β-tethered pyrroles. Direct synthesis of the β-substituted free NH-pyrrole is the central intensity of this work. DFT-calculations and preliminary mechanism investigation support the possible reaction pathway.