High-performance electrochemiluminescence of self-assembled multi-resonance thermally activated delayed fluorescence nanoparticles

In this paper, the synthesis of thermally activated delayed fluorescence nanoparticles (TADF NPs) is reported using a micelle-confined soft template self-assembly. With vaporing organic solvent in this system, TADF NPs with a diameter of about 500 nm were obtained. The main advantage is to nanoencapsulate these TADF molecules with an amphiphilic polymer. As demonstrated, air-stable nanoparticles with efficient TADF properties are realized in water. The application of these as-prepared TADF NPs as a kind of alternative electrochemiluminescent (ECL) material has also been investigated. The triplet-harvesting ability combined with excellent redox properties endows as-prepared TADF NPs with a high ECL efficiency of 10.82%, which is a marked enhancement over previous results. Therefore, ECL materials with similar behavior to reported TADF materials in this article are desirable in applications such as ECL sensing, imaging, and light-emitting devices.</p

Programming a Biofilm-Mediated Multienzyme-Assembly-Cascade System for the Biocatalytic Production of Glucosamine from Chitin

Chitin is used as an essential raw material for the production of glucosamine (GlcN). In this study, we adopted three key enzymes, isolated from <i>Thermococcus kodakaraensis</i> KOD1, that catalyze the sequential conversion of α-chitin into GlcN and developed a multienzyme-assembly-cascade (MAC) system immobilized in a bacterial biofilm, which enabled a multistep one-pot reaction. Specifically, the SpyTag–SpyCatcher and SnoopTag–SnoopCatcher pairs provided covalent and specific binding force to fix enzymes to the biofilm one by one and assemble close enzyme cascades. The MAC system showed great catalytic activity, converting 79.02 ± 3.61% of α-chitin into GlcN with little byproducts, which was 2.09 times that of GlcN catalyzed by a mixture of pure enzymes. The system also exhibited good temperature and pH stability. Notably, 90% of enzyme activity was retained after 6 rounds of reuse, and appreciable activity remained after 17 rounds