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Microcrystalline cellulose (MCC) is one of the essential functional excipients in the formulation of tablets. The need for cheaper MCC sources has drawn significant attention to exploring renewable sources. In this study, MCC was produced from soybean hull (SBH), the primary by-product of the soy industry, using a novel, simplified, and cost-effective approach. Various characterization techniques were used to study the physicochemical properties and micromeritics of the SBH-based MCC powders and compare them to those of the commercial Avicel PH-101. SBH MCCs had a larger particle size, a broader particle size distribution, a higher degree of polymerization, a higher degree of crystallinity, better thermal stability, and slightly superior flowability and compressibility than Avicel PH-101. The tableting blends (containing 60 % MCC) were prepared, and the post-compression out-of-die Heckel analysis showed that formulations with aggregated SBH MCCs were less ductile than those made with Avicel PH-101, resulting in a lower porosity (better compressibility) of the latter at higher compression pressures. The hardness values for all formulations were above 6 kg, with higher values for those made with Avicel PH-101. The lubricant sensitivity was lower for SBH MCCs. All tablets made using developed formulations showed very low friability (<0.1 %) and short disintegration times (<90 s), making them well-suited candidates for manufacturing orally disintegrating tablets (ODTs)., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier B.V. All rights reserved.)

The complexation between soy soluble polysaccharide (SSPS) and curcumin at pH 7.0 and 4.0, as well as some physicochemical characteristics of the resultant complexes, was investigated. The encapsulation efficiency and loading amount of curcumin in the complexes at pH 4.0 reached 67.3% and 4.49 μg/mg SSPS, respectively. Ethanol-induced denaturation and structural unfolding of the protein fraction in SSPS was essential for complex formation. The complexation with curcumin resulted in aggregation of SSPS and the subsequent formation of compacted nanoparticles with curcumin as the core. The complexation greatly improved the heat stability and in vitro bioaccessibility of curcumin. In general, the encapsulation efficiency, heat stability, and bioaccessibility of curcumin in the complexes at pH 4.0 were better than those at pH 7.0. The findings are of importance for the development of food grade nanovehicles for enhanced water solubility, stability, and bioaccessibility of hydrophobic bioactives.

An alkaline isoform of the PR-5 protein (designated GmOLPc) has been purified from soybean hulls and identified by MALDI-TOF/TOF-MS. GmOLPc effectively inhibited in vitro the growth of Phytophthora soja spore and Pseudomonas syringae pv glycinea. The antimicrobial activity of GmOLPc should be mainly ascribed to its high binding affinity with vesicles composed of DPPG, (1,3)-β-D-glucans, and weak endo-(1,3)-β-D-glucanase activity. From the 3D models, predicted by the homology modeling, GmOLPc contains an extended negatively charged cleft. The cleft was proved to be a prerequisite for endo-(1,3)-β-D-glucanase activity. Molecular docking revealed that the positioning of linear (1,3)-β-D-glucans in the cleft of GmOLPc allowed an interaction with Glu83 and Asp101 that were responsible for the hydrolytic cleavage of glucans. Interactions of GmOLPc with model membranes indicated that GmOLPc possesses good surface activity which could contribute to its antimicrobial activity, as proved by the behavior of perturbing the integrity of membranes through surface hydrophobic amino acid residues (Phe89 and Phe94).

In this study, we examined the possibility of preparing stable soy protein nanogels by simply heating homogeneous soy protein dispersion. The protein nanogels formed were characterized by z-average hydrodynamic diameter, polydispersity index, turbidity, ζ-potential, morphology, and their stability to pH and ionic strength change. Soy protein dispersion (1% w/v) was homogeneous around pH 5.9 where it had the lowest polydispersity index (∼0.1). Stable and spherical nanogels were formed by heating soy protein dispersion at pH 5.9 under 95 °C. They sustained constantly low polydispersity index (∼0.1) in the investigated pH range of 6.06-7.0 and 2.6-3.0. The nanogels were pH-sensitive and would swell with pH change. They were stable at 0-200 mM NaCl concentration. Denaturation of soy glycinin was the prerequisite for the formation of stable nanogels. Soy protein nanogels had a core-shell structure with basic polypeptides and β subunits interacting together as the hydrophobic core; and acid polypeptides, α', and α subunits locating outside the core as hydrophilic shell. The inner structure of soy protein nanogels was mainly stabilized by disulfide bonds cross-linked network and hydrophobic interaction. Soy protein nanogels made in this study would be useful as functional ingredients in biotechnological, pharmaceutical, and food industries.

Plant proteins are used - for the first time - in this work as bulk binders for cellulosic fibers in paper composites. Soy bean protein and wheat gluten were denatured by two methods, namely by: urea+NaOH and by urea+NaOH+acrylamide. Addition of increased amounts of the denatured proteins resulted in a significant increase in all paper strength properties. Soy protein led, in addition, to a remarkable enhancement in opacity. The use of proteins increased kaolin retention in the paper composites, while keeping the paper strength higher than the blank protein-free paper. The results show that plant proteins are favorable than synthetic adhesives; because they are biodegradable and do not cause troubles in paper recycling i.e. they are environmentally friendly., ((c) 2010 Elsevier B.V. All rights reserved.)

A stilbene dye (Direct Yellow 11) and a methine dye, Basazol 46L, recalcitrant to common chemical bleaches, were treated with horseradish and soybean peroxidases. Both enzymes were effective at chromophore removal. When compared to laccase in combination with a mediator (ABTS), soybean peroxidase was more effective at oxidative dye removal, especially for the methine dye.