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This research aims to investigate the solubility, structural properties, and immunomodulatory of rice dreg protein (RDP) modified with sodium alginate. The modification was done by wet heating assisted with microwave treatment. The solubility, emulsifying properties at pH 2–12, amino acid composition, molecular weight distribution, circular dichroism (CD) spectroscopy, and FTIR spectra of modified RDP were analyzed and discussed. Results showed that Maillard reaction could significantly enhance the solubility and emulsifying capacity of RDP. Further, an animal model for cyclophosphamide‐induced immunodeficiency was designed to evaluate the immunomodulatory effect of modified RDP. It is therefore suggested that modified RDP could improve the immunomodulatory effect of immunosuppressed mice, and the immunomodulation was concentration dependent, being generally enhanced by increased concentrations. This research revealed that glycosylation modification of RDP through Maillard reaction by wet heating assisted with microwave treatment may be successfully applied to improve the physicochemical properties and bioactive benefits of the final product.

Mannooligosaccharides are released by mannan-degrading endo-β-1,4-mannanase and are known as functional additives in human and animal diets. To satisfy demands for biocatalysis and bioprocessing in crowed environments, in this study, we employed a recently developed enzyme-engineering system, isopeptide bond-mediated molecular cyclization, to modify a mesophilic mannanase from Bacillus subtilis. The results revealed that the cyclized enzymes showed enhanced thermostability and ion stability and resilience to aggregation and freeze–thaw treatment by maintaining their conformational structures. Additionally, by using the SpyTag/SpyCatcher system, we generated a mannanase-xylanase bifunctional enzyme that exhibited a synergistic activity in substrate deconstruction without compromising substrate affinity. Interestingly, the dual-enzyme ring conformation was observed to be more robust than the linear enzyme but inferior to the single-enzyme ring conformation. Taken together, these findings provided new insights into the mechanisms of molecular cyclization on stability improvement and will be useful in the production of new functional oligosaccharides and feed additives.

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