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.

Animal proteins are essential elements of human and animal feed chain and improving the safety of human and animal feed requires understanding and controlling of the transmission of infectious agents in food chain. Many pathogenic infectious agents, such as prion protein is known to damage the central nervous system in the cattle. Bovine spongiform encephalopathy (BSE) results from infection agent (prion), and affects number of species such as cattle, human, and cats. In addition, Salmonella, pathogenic E. coli O157:H7, and Listeria monocytogenes were found in animal by-products used in the human and animal feed production. Increased interest in controlling microbial risks in human and animal feed is evidenced by a large number of publications, which highlights the need for examining the animal disposal method such as rendering process and provides a broader perspective of rendering process. While existing practices help greatly in controlling microbial contamination, this overview study showed that additional biosafety measures are necessary to ensure microbial safety in animal feed.

The taste of umami peptide H-Lys-Gly-Asp-Glu-Glu-Ser-Leu-Ala-OH (LGAGGSLA) is controversial. One possible reason for this controversy is the use of chemically synthesized LGAGGSLA to confirm its taste. To explore other ways to further confirm the flavor of LGAGGSLA, we developed a new strategy to prepare a bio-source peptide by adopting a gene engineering method to express LGAGGSLA in recombinant Escherichia coli. In our previous work, we structured the LGAGGSLA recombinant expression system and optimized the culturing conditions for preparing a fusion protein. However, the fusion protein was not cleaved by enterokinase to obtain LGAGGSLA. Because the cleavage conditions of commercial enterokinase were not specific and recombinant engineered bacteria had the potential to be used in industrial processes, in this addendum, we calculated the mass and volume yields of key processing steps in the preparation of LGAGGSLA, and established a model of cleavage conditions with the cleavage ratio of LGAGGSLA. When the LGAGGSLA was confirmed to show umami taste, it is considered as a new umami or umami enhancer. The gene information of LGAGGSLA should have a great potential in the development of new flavor product and food product containing high umami flavor.