https://www.selleckchem.com/products/Streptozotocin.html Low colloidal stability of myofibrillar protein (MP) during heating is a technofunctional constraint encountered in its beverage application. Gallic acid (GA), a natural polyphenol, was applied to fabricate MP soluble aggregates for an enhanced thermal stability. Upon pH shifting, GA was grafted into MP with the cysteine and tryptophan residues being the binding sites. As a result, the antioxidant activity of MP was enhanced. Additionally, GA modification decreased the α-helix structure of MP and converted MP into cross-linked aggregates. At low dosages (10 and 25 μmol/g GA), disulfide-dominant covalent bonds were formed to generate myosin and actin aggregates, while MP aggregates were mostly bridged through GA-thiols or GA-tryptophan adducts when the dosages exceeded 50 μmol/g. Such aggregates prevented MP from thermal gelation, leading to a stable and tunable colloidal state. This work can foster technological advances in the tailor manufacture of muscle protein-based beverages for special dietary uses.Zearalenone (ZEA), a nonsteroidal estrogenic mycotoxin produced by Fusarium graminearum, induces hyperestrogenic responses in mammals and can cause reproductive disorders in farm animals. In this study, a transcriptome analysis of Bacillus amyloliquefaciens H6, which was previously identified as a ZEA-degrading bacterium, was conducted with high-throughput sequencing technology, and the differentially expressed genes were subjected to gene ontology (GO) and kyoto encyclopedia of genes and genomes (KEGG) enrichment analyses. Among the 16 upregulated genes, BAMF_RS30125 was predicted to be the key gene responsible for ZEA degradation. The protein encoded by BAMF_RS30125 was then expressed in Escherichia coli, and this recombinant protein (named ZTE138) significantly reduced the ZEA content, as determined by the enzyme-linked immunosorbent assay (ELISA) and high-performance liquid chromatography (HPLC), and decre