The potential of wastewater-source heat pump in decarbonising buildings sector of China.

As China's economy and society continue to advance, there has been a notable enhancement in the quality of life for its people. However, the escalating energy consumption in buildings, particularly for heating and cooling purposes, has emerged as a pressing concern, accounting for nearly 60% of the overall energy consumption. In response to this challenge, heat pumps have emerged as a promising solution by efficiently meeting the demand for heating and cooling. Among these options, wastewater-source heat pumps (WWSHP) have garnered attention as an innovative choice, harnessing the waste heat in available wastewater resources in China to provide efficient heating and cooling services. The objective of this study was to comprehensively investigate the decarbonisation potential associated with sewage source heat pumps in China. By employing both techno-economic analysis and life cycle assessment methods, we conducted a thorough comparison between conventional heating and cooling systems and various heat pump systems. The results of our analysis demonstrate that WWSHPs not only exhibit the lowest greenhouse gas (GHG) emissions but also yield the lowest production costs. Our findings reveal that the potential capacity of WWSHPs amounted to a total of 2.4 EJ in 2020, with the capability to mitigate 99 Mt CO2-eq emissions and achieve cost savings of 24 billion RMB. Importantly, WWSHPs' maximum potential cannot be fully realised by replacing heating alone. However, by replacing both heating and cooling options, WWSHPs unlock substantial decarbonisation potential and cost savings.

Effective asymmetric bioreduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate by recombinant E. coli CCZU-A13 in [Bmim]PF6-hydrolyzate media.

It was the first report that the concentrated hydrolyzates from the enzymatic hydrolysis of dilute NaOH (3wt%)-soaking rice straw at 30°C was used to form [Bmim]PF6-hydrolyzate (50:50, v/v) media for bioconverting ethyl 4-chloro-3-oxobutanoate (COBE) into ethyl (R)-4-chloro-3-hydroxybutanoate [(R)-CHBE] (>99% e.e.) with recombinant E. coli CCZU-A13. Compared with pure glucose, the hydrolyzates could promote both initial reaction rate and the intracellular NADH content. Furthermore, emulsifier OP-10 (20mM) was employed to improve the reductase activity. Moreover, Hp-ß-cyclodextrin (0.01mol Hp-ß-cyclodextrin/mol COBE) was also added into this bioreaction system for enhancing the biosynthesis of (R)-CHBE from COBE by E. coli CCZU-A13 whole-cells. The yield of (R)-CHBE (>99% e.e.) from 800mM COBE was obtained at 100% in the [Bmim]PF6-hydrolyzate (50:50, v/v) media by supplementation of OP-10 (20mM) and Hp-ß-CD (8mM). In conclusion, an effective strategy for the biosynthesis of (R)-CHBE was successfully demonstrated.

MTERF2 contributes to MPP(+)-induced mitochondrial dysfunction and cell damage.

Parkinson's disease (PD) is a common neurodegenerative disorder whose pathogenesis is under intense investigation. Substantial evidence indicates that mitochondrial dysfunction plays a central role in the pathophysiology of PD. Several mitochondrial internal regulating factors act to maintain the mitochondrial function. However, how these internal regulating factors contribute to mitochondrial dysfunction in PD remains elusive. One of these factors, mitochondrial transcription termination factor 2 (MTERF2), has been implicated in the regulation of oxidative phosphorylation by modulating mitochondrial DNA transcription. Here, we discovered a new role of MTERF2 in regulating mitochondrial dysfunction and cell damage induced by MPP(+) in SH-SY5Y cells. We found that MPP(+) treatment elevated MTERF2 expression, induced mitochondrial dysfunction and cell damage, which was alleviated by MTERF2 knockdown. These findings demonstrate that MTERF2 contributes to MPP(+)-induced mitochondrial disruption and cell damage. This study indicates that MTERF2 is a potential therapeutic target for environmentally induced Parkinson's disease.

MTERF4 regulates the mitochondrial dysfunction induced by MPP(+) in SH-SY5Y cells.

Mitochondrial transcription termination factor 4, MTERF4, a member of the MTERF family, has been implicated in the regulation of mitochondrial translation by targeting NSUN4 to the large mitochondrial ribosome. Here, we found a novel role for MTERF4 in regulating mitochondrial dysfunction induced by MPP(+). We observed that knockdown of MTERF4 in SH-SY5Y cells resulted in increased mitochondrial DNA transcription levels and decreased mitochondrial DNA translation levels. In addition, after treatment with 2 mM MPP(+) for 24 h, the expression levels of MTERF4 were decreased compared to wide-type SH-SY5Y cells. Moreover, after exposure to 2 mM MPP(+) for 24 h, knockdown of MTERF4 in SH-SY5Y cells worsened the mitochondrial dysfunction induced by MPP(+), including increased reactive oxygen species, accumulated cleaved PARP-1, decreased mitochondrial membrane potential and depressed mitochondrial complexes. Furthermore, overexpression of MTERF4 in SH-SY5Y cells partially alleviated the mitochondrial dysfunction induced by MPP(+). Based on these findings, we suggest that the main function of MTERF4 is regulating mtDNA expression, and it is the crucial factor in the mechanism of mitochondrial dysfunction in SH-SY5Y cells induced by MPP(+). MTERF4 probably is the triggering of the pathogenesis of Parkinson's disease induced by environmental toxin.

Phylogenetic analysis and prokaryotic expression of NMAAP1 derived from BCG-activated murine macrophages.

BCG-activated macrophages exerted anti-tumor activities. Cell surface molecules play an important role in mediating endocytosis by macrophages. In the previous study, we identified a group of 454 membrane proteins specifically expressed on BCG-activated mouse macrophages, including a protein named NMAAP1 (novel macrophage activated associated protein). In this study, we aligned the full-length nucleotide sequences of NMAAP1 and its homologous sequences to construct its phylogenetic tree, and cloned the NMAAP1 cDNA from BCG-activated macrophages to generated NMAAP1 fusion protein in Escherichia coli. Purified the fusion protein were applied for generation of polyclonal antibodies. Western-blotting detection showed that the polyclonal antibodies have high specificities to recognize target protein.