[Economic analysis of health promotion conducted in an enterprise].

OBJECTIVE: To take intervention measures for health promotion after investigation of occupational health needs among employees, to analyze the economic input and output of the intervention measures, and to analyze the feasibility of health promotion through cost-effectiveness analysis and cost-benefit analysis. METHODS: A survey was conducted in an enterprise using a self-designed questionnaire to investigate the general information on enterprise, occupational history of each employee, awareness of occupational health knowledge, awareness of general health knowledge, awareness of hypertension, acquired immune deficiency syndrome, etc., lifestyle, and needs for health knowledge. Intervention measures were taken in the enterprise according to the investigation results, and then investigation and economic analysis of investment in health promotion, economic benefit, and absence of employees were performed using the questionnaire. RESULTS: After intervention, the awareness rate of the Code of Occupational Disease Prevention increased from 4.5% to 15.3%, the awareness rate of the definition of occupational diseases increased from 4.5% to 73.5%, and the awareness rate of the prevention and control measures for occupational diseases increased from 38.4% to 85.8%. Before intervention, 25.4%of all employees thought salt intake needed to be reduced, and this proportion increased to 92.5% after intervention. After the control strategy for health promotion, the benefit of health promotion that results from avoiding absence of employees and preventing occupational diseases was more than ten times the investment in health promotion, suggesting a significant benefit of health promotion conducted in the enterprise. CONCLUSION: The return on health promotion's investment for enterprise is worth. Health promotion really not just contribute to improve hygienic knowledge but increase the economic benefit.

Identification and characterization of a novel fumarase gene by metagenome expression cloning from marine microorganisms.

BACKGROUND: Fumarase catalyzes the reversible hydration of fumarate to L-malate and is a key enzyme in the tricarboxylic acid (TCA) cycle and in amino acid metabolism. Fumarase is also used for the industrial production of L-malate from the substrate fumarate. Thermostable and high-activity fumarases from organisms that inhabit extreme environments may have great potential in industry, biotechnology, and basic research. The marine environment is highly complex and considered one of the main reservoirs of microbial diversity on the planet. However, most of the microorganisms are inaccessible in nature and are not easily cultivated in the laboratory. Metagenomic approaches provide a powerful tool to isolate and identify enzymes with novel biocatalytic activities for various biotechnological applications. RESULTS: A plasmid metagenomic library was constructed from uncultivated marine microorganisms within marine water samples. Through sequence-based screening of the DNA library, a gene encoding a novel fumarase (named FumF) was isolated. Amino acid sequence analysis revealed that the FumF protein shared the greatest homology with Class II fumarate hydratases from Bacteroides sp. 2_1_33B and Parabacteroides distasonis ATCC 8503 (26% identical and 43% similar). The putative fumarase gene was subcloned into pETBlue-2 vector and expressed in E. coli BL21(DE3)pLysS. The recombinant protein was purified to homogeneity. Functional characterization by high performance liquid chromatography confirmed that the recombinant FumF protein catalyzed the hydration of fumarate to form L-malate. The maximum activity for FumF protein occurred at pH 8.5 and 55°C in 5 mM Mg(2+). The enzyme showed higher affinity and catalytic efficiency under optimal reaction conditions: K(m) = 0.48 mM, V(max) = 827 µM/min/mg, and k(cat)/K(m) = 1900 mM/s. CONCLUSIONS: We isolated a novel fumarase gene, fumF, from a sequence-based screen of a plasmid metagenomic library from uncultivated marine microorganisms. The properties of FumF protein may be ideal for the industrial production of L-malate under higher temperature conditions. The identification of FumF underscores the potential of marine metagenome screening for novel biomolecules.