Rare earth elements (REEs) have become increasingly important materials owing to their use in the high-tech and clean-energy industries. However, the unpredictable supply, possible health risks, and environmentally unsustainable extraction practices associated with REEs have encouraged the development of green technologies for the selective extraction and recovery of metals. This study presents a simple and innovative approach for the selective extraction and recovery of total REEs. Elastin-like polypeptide (ELP) and the REE-binding domain (lanmodulin) are fused to form REEs-sensitive and thermo-responsive genetically encoded ELP called RELP, where ELP offered a reversible, inverse phase transition for repeated uses. The RELP are purified and used for the selective extraction of total REEs from competing non-REEs metals by controlling the solution temperature (4 and 37 °C) and pH. RELP exhibit high REE specificity, even in the presence of non-REE metal ions. The bound REEs are readily recovered during at least six repeated cycles, and the efficiency is maintained. Moreover, REEs are selectively recovered by RELP from steel slag leachate, a potential industrial source of REEs. RELP offers a rapid, selective, and scalable method for REE extraction and recovery. This technology can be adapted to recover other precious metals and commodities.
Enzyme
immobilization is very important for diverse enzyme applications.
Particularly, there is a growing need for coimmobilization of multiple
enzymes for biosensing and synthetic applications. However, it is
still challenging to coimmobilize two enzymes with desirable features,
including high immobilization yield, retention of enzymatic activity,
and low leaching. In this study, we demonstrated that a pluronic-based
nanocarrier (PNC) can be an encapsulation platform for immobilization
of various single enzymes. Since the PNC is temperature-sensitive,
a simple temperature change from 4 to 37 °C led to a substantial
size reduction and enzyme encapsulation. All six enzymes tested were
encapsulated by the PNC in high yield (∼90%) with the retained
enzymatic activity (>95%). The leaching of encapsulated enzymes
was
very minimal (<0.13% for 2 weeks). Then, we demonstrated that the
PNC can efficiently coencapsulate two enzymes, formate dehydrogenase
(FDH) and mannitol dehydrogenase (MDH), for a cascade reaction producing d-mannitol. Coencapsulation of FDH and MDH resulted in an over
10-fold increase in d-mannitol production compared to the
free mix of FDH and MDH, likely due to the enhanced local concentrations
of FDH and MDH inside the PNC.
An
inverse-electron-demand Diels–Alder (IEDDA) reaction
using genetically encoded tetrazine variants enables rapid bioconjugation
for diverse applications in vitro and in
cellulo. However, in vivo bioconjugation
using genetically encoded tetrazine variants is challenging, because
the IEDDA coupling reaction competes with rapid elimination of reaction
partners in vivo. Here, we tested the hypothesis
that a genetically encoded phenylalanine analogue containing a hydrogen-substituted
tetrazine (frTet) would increase the IEDDA reaction rate, thereby
allowing for successful bioconjugation in vivo. We
found that the in vitro IEDDA reaction rate of superfolder
green fluorescent protein (sfGFP) containing frTet (sfGFP-frTet) was
12-fold greater than that of sfGFP containing methyl-substituted tetrazine
(sfGFP-Tet_v2.0). Additionally, sfGFP variants encapsulated with chitosan-modified,
pluronic-based nanocarriers were delivered into nude mice or tumor-bearing
mice for in vivo imaging. The in vivo-delivered sfGFP-frTet exhibited almost complete fluorescence recovery
upon addition of trans-cyclooctene via the IEDDA reaction within 2
h, whereas sfGFP-Tet_v2.0 did not show substantial fluorescence recovery.
These results demonstrated that the genetically encoded frTet allows
an almost complete IEDDA reaction in vivo upon addition
of trans-cyclooctene, enabling temporal control of in vivo bioconjugation in a very high yield.
Charge Booster Tags
In article number 2209874, Jaeyun Kim, Inchan Kwon, and co‐workers show cars with a booster that deliver the loaded drugs to the goal (blood vessel). The roads are made of many bricks, representing the polymeric hydrogel composed of many monomeric units.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.