The -isoleucine-4-dioxygenase converts -isoleucine (Ile) into(2S,3R,4S)-4-(OH)-isoleucine (4-HIL), a naturally occurring hydroxyl amino acid, which is a promising compound for drug and functional food development. Here, a novel -isoleucine-4-dioxygenase (RaIDO) from Rahnella aquatilis was cloned, expressed and characterized, as one of only a few reported -isoleucine-4-dioxygenases. RaIDO showed high catalytic efficiency with Ile as the substrate, as well as good stability.
View Article and Find Full Text PDFSheng Wu Gong Cheng Xue Bao
May 2023
The discovery of new enzymes for poly(ethylene terephthalate) (PET) degradation has been a hot topic of research globally. Bis-(2-hydroxyethyl) terephthalate (BHET) is an intermediate compound in the degradation of PET and competes with PET for the substrate binding site of the PET-degrading enzyme, thereby inhibiting further degradation of PET. Discovery of new BHET degradation enzymes may contribute to improving the degradation efficiency of PET.
View Article and Find Full Text PDFJ Colloid Interface Sci
September 2023
Polyethylene terephthalate (PET), the most abundant polyester plastic, has become a global concern due to its refractoriness and accumulation in the environment. In this study, inspired by the structure and catalytic mechanism of the native enzyme, peptides, based on supramolecular self-assembly, were developed to construct enzyme mimics for PET degradation, which were achieved by combining the enzymatic active sites of serine, histidine and aspartate with the self-assembling polypeptide MAX. The two designed peptides with differences in hydrophobic residues at two positions exhibited a conformational transition from random coil to β-sheet by changing the pH and temperature, and the catalytic activity followed the self-assembly "switch" with the fibrils formed β-sheet, which could catalyze PET efficiently.
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