Optimal dynamic control of laminated adaptive structures using a higher order model and a genetic algorithm

This paper deals with a finite element formulation based on the classical laminated plate theory, for active control of thin plate laminated structures with integrated piezoelectric layers, acting as sensors and actuators. The control is initialized through a previous optimization of the core of the laminated structure, in order to minimize the vibration amplitude. Also the optimization of the patches position is performed to maximize the piezoelectric actuator efficiency. The genetic algorithm is used for these purposes. The finite element model is a single layer triangular plate/shell element with 24 degrees of freedom for the generalized displacements, and one electrical potential degree of freedom for each piezoelectric element layer, which can be surface bonded or embedded on the laminate. To achieve a mechanism of active control of the structure dynamic response, a feedback control algorithm is used, coupling the sensor and active piezoelectric layers. To calculate the dynamic response of the laminated structures the Newmark method is considered. The model is applied in the solution of an illustrative case and the results are presented and discussed

After sales service: key settings for improving profitability and customer satisfaction

This paper presents a performed study to develop and improve the process of after sales of a Latvian company specialized in manufacturing fish processing equipment. The project was developed based on an action- research methodology. During the first stage of the study, the current after sales process was analysed to identify the issues and possible improvement opportunities that could be implemented later on. Data were collected through surveys and analysed, resulting in a series of improvement proposals discussed with the board of the company. At a later stage of the study, improvements were implemented such as the introduction of new services, development of new process diagrams and improvements of the spare parts management strategy. To conclude the study, the new services were offered and presented to customers and the trial period for the new after sales methodology was started.info:eu-repo/semantics/publishedVersio

The mechanism of formate oxidation by metal-dependent formate dehydrogenases

J Biol Inorg Chem (2011) 16:1255–1268 DOI 10.1007/s00775-011-0813-8Metal-dependent formate dehydrogenases (Fdh) from prokaryotic organisms are members of the dimethyl sulfoxide reductase family of mononuclear molybdenum-containing and tungsten-containing enzymes. Fdhs catalyze the oxidation of the formate anion to carbon dioxide in a redox reaction that involves the transfer of two electrons from the substrate to the active site. The active site in the oxidized state comprises a hexacoordinated molybdenum or tungsten ion in a distorted trigonal prismatic geometry. Using this structural model, we calculated the catalytic mechanism of Fdh through density functional theory tools. The simulated mechanism was correlated with the experimental kinetic properties of three different Fdhs isolated from three different Desulfovibrio species. Our studies indicate that the C–H bond break is an event involved in the rate-limiting step of the catalytic cycle. The role in catalysis of conserved amino acid residues involved in metal coordination and near the metal active site is discussed on the basis of experimental and theoretical results

Glucose Gradients Influence Zonal Matrix Deposition in 3D Cartilage Constructs

Reproducing the native collagen structure and glycosaminoglycan (GAG) distribution in tissue-engineered cartilage constructs is still a challenge. Articular cartilage has a specific nutrient supply and mechanical environment due to its location and function in the body. Efforts to simulate this native environment have been reported through the use of bioreactor systems. However, few of these devices take into account the existence of gradients over cartilage as a consequence of the nutrient supply by diffusion. We hypothesized that culturing chondrocytes in an environment, in which gradients of nutrients can be mimicked, would induce zonal differentiation. Indeed, we show that glucose gradients facilitating a concentration distribution as low as physiological glucose levels enhanced a zonal chondrogenic capacity similar to the one found in native cartilage. Furthermore, we found that the glucose consumption rates of cultured chondrocytes were higher under physiological glucose concentrations and that GAG production rates were highest in 5 mM glucose. From these findings, we concluded that this condition is better suited for matrix deposition compared to 20 mM glucose standard used in a chondrocyte culture system. Reconsidering the culture conditions in cartilage tissue engineering strategies can lead to cartilaginous constructs that have better mechanical and structural properties, thus holding the potential of further enhancing integration with the host tissue

Molybdenum Induces the expression of a protein containing a new heterometallic Mo-Fe cluster in desulfoVibrio alaskensis

Biochemistry. 2009 Feb 10;48(5):873-82. doi: 10.1021/bi801773t.The characterization of a novel Mo-Fe protein (MorP) associated with a system that responds to Mo in Desulfovibrio alaskensis is reported. Biochemical characterization shows that MorP is a periplasmic homomultimer of high molecular weight (260 +/- 13 kDa) consisting of 16-18 monomers of 15321.1 +/- 0.5 Da. The UV/visible absorption spectrum of the as-isolated protein shows absorption peaks around 280, 320, and 570 nm with extinction coefficients of 18700, 12800, and 5000 M(-1) cm(-1), respectively. Metal content, EXAFS data and DFT calculations support the presence of a Mo-2S-[2Fe-2S]-2S-Mo cluster never reported before. Analysis of the available genomes from Desulfovibrio species shows that the MorP encoding gene is located downstream of a sensor and a regulator gene. This type of gene arrangement, called two component system, is used by the cell to regulate diverse physiological processes in response to changes in environmental conditions. Increase of both gene expression and protein production was observed when cells were cultured in the presence of 45 microM molybdenum. Involvement of this system in Mo tolerance of sulfate reducing bacteria is proposed

Endothelial C-type natriuretic peptide maintains vascular homeostasis

PMCID: PMC4151218Wellcome Trust (084449/Z/07/Z and 078496/Z/05/Z

Production of thermostable β-glucosidase and CMCase by Penicillium sp. LMI01 isolated from the Amazon region

Background: Cellulolytic enzymes of microbial origin have great industrial importance because of their wide application in various industrial sectors. Fungi are considered the most efficient producers of these enzymes. Bioprospecting survey to identify fungal sources of biomass-hydrolyzing enzymes from a high-diversity environment is an important approach to discover interesting strains for bioprocess uses. In this study, we evaluated the production of endoglucanase (CMCase) and β-glucosidase, enzymes from the lignocellulolytic complex, produced by a native fungus. Penicillium sp. LMI01 was isolated from decaying plant material in the Amazon region, and its performance was compared with that of the standard isolate Trichoderma reesei QM9414 under submerged fermentation conditions. Results: The effectiveness of LMI01 was similar to that of QM9414 in volumetric enzyme activity (U/mL); however, the specific enzyme activity (U/mg) of the former was higher, corresponding to 24.170 U/mg of CMCase and 1.345 U/mg of β-glucosidase. The enzymes produced by LMI01 had the following physicochemical properties: CMCase activity was optimal at pH 4.2 and the β-glucosidase activity was optimal at pH 6.0. Both CMCase and β-glucosidase had an optimum temperature at 60°C and were thermostable between 50 and 60°C. The electrophoretic profile of the proteins secreted by LMI01 indicated that this isolate produced at least two enzymes with CMCase activity, with approximate molecular masses of 50 and 35 kDa, and β-glucosidases with molecular masses between 70 and 100 kDa. Conclusions: The effectiveness and characteristics of these enzymes indicate that LMI01 can be an alternative for the hydrolysis of lignocellulosic materials and should be tested in commercial formulations

Production of thermostable \u3b2-glucosidase and CMCase by Penicillium sp. LMI01 isolated from the Amazon region

Background: Cellulolytic enzymes of microbial origin have great industrial importance because of their wide application in various industrial sectors. Fungi are considered the most efficient producers of these enzymes. Bioprospecting survey to identify fungal sources of biomass-hydrolyzing enzymes from a high-diversity environment is an important approach to discover interesting strains for bioprocess uses. In this study, we evaluated the production of endoglucanase (CMCase) and \u3b2-glucosidase, enzymes from the lignocellulolytic complex, produced by a native fungus. Penicillium sp. LMI01 was isolated from decaying plant material in the Amazon region, and its performance was compared with that of the standard isolate Trichoderma reesei QM9414 under submerged fermentation conditions. Results: The effectiveness of LMI01was similar to that of QM9414 in volumetric enzymeactivity (U/mL); however, the specific enzyme activity (U/mg) of the former was higher, corresponding to 24.170 U/mg of CMCase and 1.345 U/mg of \u3b2-glucosidase. The enzymes produced by LMI01 had the following physicochemical properties: CMCase activity was optimal at pH 4.2 and the \u3b2-glucosidase activity was optimal at pH 6.0. Both CMCase and \u3b2-glucosidase had an optimum temperature at 60\ub0C and were thermostable between 50 and 60\ub0C. The electrophoretic profile of the proteins secreted by LMI01 indicated that this isolate produced at least two enzymes with CMCase activity, with approximate molecular masses of 50 and 35 kDa, and \u3b2-glucosidases with molecular masses between 70 and 100 kDa. Conclusions: The effectiveness and characteristics of these enzymes indicate that LMI01 can be an alternative for the hydrolysis of lignocellulosic materials and should be tested in commercial formulations