Ping Wang

A green and sustainable strategy was used to prepare curli nanomaterialsin situas an alternative to enzyme immobilization.

Herein we report the use of Pseudomonas putida F1 biofilms grown on carbonized cellulosic fibers to achieve biodegradation of airborne volatile organic compounds (VOCs) in the absence of any bulk aqueous‐phase media. It is believed that direct exposure of gaseous VOC substrates to biomass may eliminate aqueous‐phase mass transfer resistance and facilitate VOC capture and degradation. When tested with toluene vapor as a model VOC, the supported biofilm could grow optimally at 300 p.p.m. toluene and 80% relative humidity, with a specific growth rate of 0.425 day⁻¹. During long‐term VOC biodegradation tests in a tubular packed bed reactor, biofilms achieved a toluene degradation rate of 2.5 mg g_DCW⁻¹ h⁻¹ during the initial growth phase. Interestingly, the P. putida F1 film kept biodegrading activity even at the stationary nongrowth phase. The supported biofilms with a biomass loading of 20% (wt) could degrade toluene at a rate of 1.9 mg g_DCW⁻¹ h⁻¹ during the stationary phase, releasing CO₂ at a rate of 6.4 mg g_DCW⁻¹ h⁻¹ at the same time (indicating 100% conversion of substrate carbon to CO₂). All of these observations promised a new type of “dry” biofilm reactors for efficient degradation of toxic VOCs without involving a large amount of water.

Biofilms are promising candidates for sustainable bioprocessing applications. This work presents a rational design of biofilm catalysts by integrating extra‐ and intracellular catalysis systems with optimized substrate channeling to realize efficient multistep biosynthesis. An assembly of four enzymes in a “three‐in‐one” structure was achieved by rationally placing the enzymes on curli nanofibers, the cell surface, and inside cells. The catalytic efficiency of the biofilm catalysts was over 2.8 folds higher than that of the control whole‐cell catalysis when the substrate benzaldehyde was fed at 100 mm. The highest yield of d‐phenyllactic acid catalyzed by biofilm catalysts under optimized conditions was 102.19 mm, also much higher than that of the control catalysis test (52.29 mm). The results demonstrate that engineered biofilms are greatly promising in integrating extra‐ and intracellular catalysis, illustrating great potentials of rational design in constructing biofilm catalysts as sustainable supports for whole‐cell catalysis.

A programmable biofilm-cellulose platform is constructed to facilitate the clustering of two Escherichia coli catalysts, which is promising to achieve an efficient transformation by bringing cells into close proximity. This study also provides a unique bacteria-based method for endowing traditional materials with multiple functions via genetic engineering.

New advances in nanotechnology are driving a wave of technology revolution impacting a broad range of areas in agricultural production. The current work reviews nanopesticides, nano-fabricated fertilizers, and nano activity-based growth promoters reported in the last several years, focusing on mechanisms revealed for preparation and functioning. It appears to us that with many fundamental concepts have been demonstrated over last two decades, new advances in this area continue to expand mainly in three directions, i.e., efficiency improvement, material sustainability and environment-specific stimulation functionalities. It is also evident that environmental and health concerns associated with nano agrochemicals are the primary motivation and focus for most recent work. Challenges and perspectives for future development of nano agrochemicals are also discussed.

NADPH provides the reducing power for decomposition of reactive oxygen species (ROS), making it an indispensable part during ROS defense. It remains uncertain, however, if living cells respond to the ROS challenge with an elevated intracellular NADPH level or a more complex NADPH-mediated manner. Herein, we employed a model fungus Aspergillus nidulans to probe this issue. A conditional expression of glucose-6-phosphate dehydrogenase (G6PD)-strain was constructed to manipulate intracellular NADPH levels. As expected, turning down the cellular NADPH concentration drastically lowered the ROS response of the strain; it was interesting to note that increasing NADPH levels also impaired fungal H₂O₂ resistance. Further analysis showed that excess NADPH promoted the assembly of the CCAAT-binding factor AnCF, which in turn suppressed NapA, a transcriptional activator of PrxA (the key NADPH-dependent ROS scavenger), leading to low antioxidant ability. In natural cell response to oxidative stress, we noticed that the intracellular NADPH level fluctuated “down then up” in the presence of H₂O₂. This might be the result of a co-action of the PrxA-dependent NADPH consumption and NADPH-dependent feedback of G6PD. The fluctuation of NADPH is well correlated to the formation of AnCF assembly and expression of NapA, thus modulating the ROS defense. Our research elucidated how A. nidulans precisely controls NADPH levels for ROS defense. Graphical Abstract

In this paper, a fluorescence resonance energy transfer (FRET)-based sensor for ultra-sensitive detection of H₂O₂ was developed by utilizing the unique enzymatic properties of peroxiredoxin (Prx) to H₂O₂. Cyan and yellow fluorescent protein (CFP and YFP) were fused to Prx and mutant thioredoxin (mTrx), respectively. In the presence of H₂O₂, Prx was oxidized into covalent homodimer through disulfide bonds, which were further reduced by mTrx to form a stable mixed disulfide bond intermediate between CFP-Prx and mTrx-YFP, inducing FRET. A linear quantification range of 10–320 nM was obtained according to the applied protein concentrations and the detection limit (LOD) was determined to be as low as 4 nM. By the assistance of glucose oxidase to transform glucose into H₂O₂, the CFP-Prx/mTrx-YFP system (CPmTY) was further exploited for the detection of glucose in real sample with good performance, suggesting this CPmTY protein sensor is highly practical.