Система управления повышением квалификации управленческого персонала организации

Выпускная квалификационная работа посвящена анализу путей повышения эффективности использования человеческих ресурсов. В ходе работы был произведен обзор теоретического материала по управлению человеческими ресурсами; проанализированы размер и структура организации; изучены методы мотивации рассматриваемой организации; проведена оценка удовлетворенности персонала; проанализированы методы, влияющие на эффективность работы персонала; предложены рекомендации по повышению эффективности использования людских ресурсов.The final qualifying work is devoted to the analysis of ways to improve the efficiency of the use of human resources. In the course of the work, a review was made of theoretical material on human resource management; analyzed the size and structure of the organization; the methods of motivation of the organization in question have been studied; staff satisfaction was assessed; analyzed the methods that affect the efficiency of the personnel; recommendations for improving the efficiency of the use of human resources are proposed

Solution Behavior and Activity of a Halophilic Esterase under High Salt Concentration

Background: Halophiles are extremophiles that thrive in environments with very high concentrations of salt. Although the salt reliance and physiology of these extremophiles have been widely investigated, the molecular working mechanisms of their enzymes under salty conditions have been little explored. Methodology/Principal Findings: A halophilic esterolytic enzyme LipC derived from archeaon Haloarcula marismortui was overexpressed from Escherichia coli BL21. The purified enzyme showed a range of hydrolytic activity towards the substrates of p-nitrophenyl esters with different alkyl chains (n = 2−16), with the highest activity being observed for p-nitrophenyl acetate, consistent with the basic character of an esterase. The optimal esterase activities were found to be at pH 9.5 and [NaCl] = 3.4 M or [KCl] = 3.0 M and at around 45°C. Interestingly, the hydrolysis activity showed a clear reversibility against changes in salt concentration. At the ambient temperature of 22°C, enzyme systems working under the optimal salt concentrations were very stable against time. Increase in temperature increased the activity but reduced its stability. Circular dichroism (CD), dynamic light scattering (DLS) and small angle neutron scattering (SANS) were deployed to determine the physical states of LipC in solution. As the salt concentration increased, DLS revealed substantial increase in aggregate sizes, but CD measurements revealed the maximal retention of the α-helical structure at the salt concentration matching the optimal activity. These observations were supported by SANS analysis that revealed the highest proportion of unimers and dimers around the optimal salt concentration, although the coexistent larger aggregates showed a trend of increasing size with salt concentration, consistent with the DLS data. Conclusions/Significance: The solution α-helical structure and activity relation also matched the highest proportion of enzyme unimers and dimers. Given that all the solutions studied were structurally inhomogeneous, it is important for future work to understand how the LipC's solution aggregation affected its activity