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Even after decades of research, the preparation of mesoporous silica still depends on the sol–gel method. The major problem of sol–gel method is its infeasibility in industrial manufacturing. A large-scale preparation method is desired to meet the growing demand of mesoporous silica in multiple applications. A cost-effective and industrially feasible method was proposed to prepare mesoporous silica. The well-developed acid leaching technology was used as a novel pore forming method for treating coal fly ash. And mesoporous silica with specific surface area as high as 585.02 m 2 /g and pore volume of 0.54 cm 3 /g was successfully prepared under a control of reaction parameters. Reaction intensity was introduced as a new parameter to describe reaction conditions and help explain the variation of pore structure and shape prepared under different reaction conditions. This method is feasible in large-scale manufacturing of mesoporous silica and will satisfy the great demand for its wide applications. [ABSTRACT FROM AUTHOR]

• SPC can be a good feed ingredient as swimming crab can tolerate up to 75% replacement. • Replacement of dietary fish meal with SPC will inhibit TOR pathway in hepatopancreas. • 51.49% replacement level with SPC is recommended for better PER. A 56-day feeding trial was conducted to evaluate the potential use of soy protein concentrate (SPC) as a partial replacement of fish meal in swimming crab Portunus trituberculatus. Four isonitrogenous and isolipidic diets (450 g/kg protein and 80 g/kg lipid) were formulated to contain graded levels of SPC, and fish meal was replaced with SPC at 25%, 50% and 75% level (SPC25, SPC50 and SPC75, respectively). The control diet (SPC0) contained fish meal, soybean meal and krill meal as the main protein sources. Lysine and methionine were added into SPC replacement diets to maintain the same concentrations as the control diet. Each diet was randomly assigned to triplicate groups of 45 juvenile swimming crabs (5.00 ± 0.23 g / crab) that were stocked in the rectangle plastic baskets. The results indicated that the weight gain (WG), special growth rate (SGR), feed efficiency (FE) and daily feed intake (DFI) were not significantly influenced by the dietary replacement of fish meal with SPC (P > 0.05). Crabs fed the SPC75 diet had lower protein efficiency ratio (PER) and molting frequencey (MF) than those fed the SPC50 diet(P < 0.05). The proximate compositions in whole body and muscle were not significantly influenced by the replacement of fish meal with SPC (P > 0.05), however, there was significant difference in the hepatopancreas moisture content (P < 0.05), and crabs fed the SPC0 diet had the highest lipid in hepatopancreas among all treatments (P < 0.05). Moreover, the essential amino acid (EAA), non-essential amino acid (NEAA) and total amino acid (TAA) contents of muscle significantly increased with the dietary replacement of fish meal with SPC levels increasing from 0 to 75% (P < 0.05). No significant differences in hemolymph enzyme activities and characteristics were observed among all treatments (P > 0.05). Crabs fed the SPC0 diet had higher amylase and lipase activities in hepatopancreas than those fed other diets. The hepatopancreas trypsin activity was not significantly influenced by the replacement of fish meal with SPC (P > 0.05). The hepatopancreas alanine aminotransferase (ALT) and aspartate aminotransferase (AST) activities increased when the dietary SPC levels increased from 0 to 25%, and then decreased significantly with the further increase of SPC replacement levels (P < 0.05). The relative expression of genes in target of rapamycin (TOR) pathway, crabs fed the SPC0 diet had higher relative expressions of tor, akt, s6k1, s6, 4ebp1, eif4e1a, eif4e2 and eif4e3 genes in hepatopancreas than those fed other diets (P < 0.05), moreover, there were no significant differences in gene expressions of TOR pathway among crabs fed the SPC25, SPC50 and SPC75 diets (P > 0.05). Based on the two slope broken-line regression analysis of PER against the dietary fish meal replacement with SPC levels, the optimum dietary replacement of fish meal with SPC was determined to be 51.49% for juvenile swimming crab. [ABSTRACT FROM AUTHOR]

Introduction Myocardial ischemia-reperfusion (I/R) injury affects millions of people worldwide and has a very high mortality rate. Since microRNA-497 (miR-497) has been found to be related with cardiomyocyte apoptosis, this study aimed to explore the effect of miR-497 by targeting Mfn2 in a mouse model of myocardial ischemia-reperfusion (I/R) injury. Materials BALB/c mice were modeled with I/R and some were injected with miR-497 agomir before I/R to observe whether miR-497 alleviates the injury that occurs as a result of I/R. Bioinformatics website and dual-luciferase reporter gene assay were employed in order to detect the relations between miR-497 and Mfn2 gene. Next, cells were extracted to be transfected with different mimic, inhibitor and siRNAs to further explore how miR-497 acts to I/R. Western blot analysis and reverse transcription quantitative polymerase chain reaction (RT-qPCR) were conducted to measure expressions of miR-497, Mfn2, Fas, Bcl-2, Bax and Caspase-3 in myocardial tissues and cardiomyocytes after transfection. CCK-8 assay and flow cytometry were used to determine proliferation, cell cycle distribution and apoptosis of cardiomyocytes in each group after transfection. Results Mice with I/R had myocardial dysfunction but before the injection with miR-497 agomir, the impairment was alleviated. Mfn2 was verified as the target gene of miR-497. The inhibition of miR-497 in turn inhibits Mfn2 expressione and cardiomyocyte apoptosis. The overexpression of miR-497 and Mfn2 gene silencing can lead to the promotion of proliferation capability of mice cardiomyocytes in vitro. Overexpressed miR-497 and Mfn2 gene silencing can also facilitate cell cycle entry and inhibit the apoptosis cardiomyocytes of mice in vitro. Conclusion The present study provided strong evidence that miR-497 promotes proliferation and inhibits apoptosis of cardiomyocytes by downregulating the expression of Mfn2 in a mouse model of myocardial I/R injury. [ABSTRACT FROM AUTHOR]