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311.
Increasing growth and productivity of food crops via safe biostimulants is a very important issue in the current years. This study aimed to investigate the potential of moringa leaf extract (MLE) in improving the performance of snap bean (Phaseolus vulgaris L.) cv. ‘Paulista’ under field conditions. Hormonal analysis of MLE revealed its richness of various classes of phytohormones particularly salicylates. The results revealed that all MLE concentrations had a positive effect on growth, biochemical, yield, and yield related traits as well as yield quality of snap bean compared to control, and the effect was dose-dependent. Moreover, increasing pods yield of snap bean may be related to gibberellins (GA7) content than other plant hormones. In conclusion, the leaf extract of moringa provides a good source of phytohormones that have a positive role to stimulate growth and productivity of snap bean plants.  相似文献   
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α-Amylase inhibitors (aAIs) have been applied for the efficient management of type 2 diabetes. The aim of this study was to search for potential aAIs produced by microbial fermentation. Among various bacterial strains, Pseudomonas aeruginosa TUN03 was found to be a potential aAI-producing strain, and shrimp heads powder (SHP) was screened as the most suitable C/N source for fermentation. P. aeruginosa TUN03 exhibited the highest aAIs productivity (3100 U/mL) in the medium containing 1.5% SHP with an initial pH of 7–7.5, and fermentation was performed at 27.5 °C for two days. Further, aAI compounds were investigated for scaled-up production in a 14 L-bioreactor system. The results revealed a high yield (4200 U/mL) in a much shorter fermentation time (12 h) compared to fermentation in flasks. Bioactivity-guided purification resulted in the isolation of one major target compound, identified as hemi-pyocyanin (HPC) via gas chromatography-mass spectrometry and nuclear magnetic resonance. Its purity was analyzed by high-performance liquid chromatography. HPC demonstrated potent α-amylase inhibitory activity comparable to that of acarbose, a commercial antidiabetic drug. Notably, HPC was determined as a new aAI. The docking study indicated that HPC inhibits α-amylase by binding to amino acid Arg421 at the biding site on enzyme α-amylase with good binding energy (−9.3 kcal/mol) and creating two linkages of H-acceptors.  相似文献   
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