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Considering the efficiency and environmental issue in balloon inflating and sealing up work,an innovate design scheme cooperated by a variety of transmission structure which is ingenuity and meets the green design concept is put forward. Taking the core component cylindrical cam as an example and the parametric design analysis in its process is expounded and the mechanism is controlled to achieve precise movement by using function expression. On this basis,the optimization design based on the parameter- driven is further studied,by using the genetic algorithm in Matlab optimization toolbox and taking the resistance moment of inverse cam mechanism as objective,the model is modified and the parameter is reset by using the optimization result. The verification is carried out through the functional prototype testing and motion simulation analysis in Recur Dyn solver in UG software,and the optimized design in all the parameter driving is perfected.

Collagenolytic proteases are widely used in the food, medical, pharmaceutical, cosmetic, and textile industries. Mesophilic collagenases exhibit collagenolytic activity under physiological conditions, but have limitations in efficiently degrading collagen-rich wastes, such as collagen from fish scales, at high temperatures due to their poor thermostability. Bacterial collagenolytic proteases are members of various proteinase families, including the bacterial collagenolytic metalloproteinase M9 and the bacterial collagenolytic serine proteinase families S1, S8, and S53. Notably, the C-terminal domains of collagenolytic proteases, such as the pre-peptidase C-terminal domain, the polycystic kidney disease-like domain, the collagen-binding domain, the proprotein convertase domain, and the β-jelly roll domain, exhibit collagen-binding or -swelling activity. These activities can induce conformational changes in collagen or the enzyme active sites, thereby enhancing the collagen-degrading efficiency. In addition, thermostable bacterial collagenolytic proteases can function at high temperatures, which increases their degradation efficiency since heat-denatured collagen is more susceptible to proteolysis and minimizes the risk of microbial contamination. To date, only a few thermophile-derived collagenolytic proteases have been characterized. TSS, a thermostable and halotolerant subtilisin-like serine collagenolytic protease, exhibits high collagenolytic activity at 60°C. In this review, we present and summarize the current research on A) the classification and nomenclature of thermostable and mesophilic collagenolytic proteases derived from diverse microorganisms, and B) the functional roles of their C-terminal domains. Furthermore, we analyze the cleavage specificity of the thermostable collagenolytic proteases within each family and comprehensively discuss the thermostable collagenolytic protease TSS.

Silver nanoparticles (AgNPs), revered for their antimicrobial prowess, have become ubiquitous in a range of products, from biomedical equipment to food packaging. However, amidst their rising popularity, concerns loom over their possible detrimental effects on fetal development and subsequent adult life. This review delves into the developmental toxicity of AgNPs across diverse models, from aquatic species like zebrafish and catfish to mammalian rodents and in vitro embryonic stem cells. Our focus encompasses the fate of AgNPs in different contexts, elucidating associated hazardous results such as embryotoxicity and adverse pregnancy outcomes. Furthermore, we scrutinize the enduring adverse impacts on offspring, spanning impaired neurobehavior function, reproductive disorders, cardiopulmonary lesions, and hepatotoxicity. Key hallmarks of developmental harm are identified, encompassing redox imbalances, inflammatory cascades, DNA damage, and mitochondrial stress. Notably, we explore potential explanations, linking immunoregulatory dysfunction and disrupted epigenetic modifications to AgNPs-induced developmental failures. Despite substantial progress, our understanding of the developmental risks posed by AgNPs remains incomplete, underscoring the urgency of further research in this critical area., Competing Interests: The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (© 2023 The Authors.)

Meiotic recombination contributes to the maintenance of the association between homologous chromosomes (homologs) and ensures the accurate segregation of homologs during anaphase I, thus facilitating the redistribution of alleles among progeny. Meiotic recombination is initiated by the programmed formation of DNA double strand breaks, the repair of which requires DNA synthesis, but the role of DNA synthesis proteins during meiosis is largely unknown. Here, we hypothesized that the lagging strand-specific DNA Polymerase δ (POL δ) might be required for meiotic recombination, based on a previous analysis of DNA Replication Factor1 that suggested a role for lagging strand synthesis in meiotic recombination. In Arabidopsis ( Arabidopsis thaliana ), complete mutation of the catalytic subunit of POL δ, encoded by AtPOLD1 , leads to embryo lethality. Therefore, we used a meiocyte-specific knockdown strategy to test this hypothesis. Reduced expression of AtPOLD1 in meiocytes caused decreased fertility and meiotic defects, including incomplete synapsis, the formation of multivalents, chromosome fragmentation, and improper segregation. Analysis of meiotic crossover (CO) frequencies showed that AtPOLD1 RNAi plants had significantly fewer interference-sensitive COs than the wild type, indicating that AtPOL δ participates in type I CO formation. AtPOLD1 RNAi atpol2a double mutant meiocytes displayed more severe meiotic phenotypes than those of either single mutant, suggesting that the function of AtPOLD1 and AtPOL2A is not identical in meiotic recombination. Given that POL δ is highly conserved among eukaryotes, we hypothesize that the described role of POL δ here in meiotic recombination likely exists widely in eukaryotes., (© 2019 American Society of Plant Biologists. All Rights Reserved.)