Profit-oriented disassembly-line balancing

As product and material recovery has gained importance, disassembly volumes have increased, justifying construction of disassembly lines similar to assembly lines. Recent research on disassembly lines has focused on complete disassembly. Unlike assembly, the current industry practice involves partial disassembly with profit-maximization or cost-minimization objectives. Another difference between assembly and disassembly is that disassembly involves additional precedence relations among tasks due to processing alternatives or physical restrictions. In this study, we define and solve the profit-oriented partial disassembly-line balancing problem. We first characterize different types of precedence relations in disassembly and propose a new representation scheme that encompasses all these types. We then develop the first mixed integer programming formulation for the partial disassembly-line balancing problem, which simultaneously determines (1) the parts whose demand is to be fulfilled to generate revenue, (2) the tasks that will release the selected parts under task and station costs, (3) the number of stations that will be opened, (4) the cycle time, and (5) the balance of the disassembly line, i.e. the feasible assignment of selected tasks to stations such that various types of precedence relations are satisfied. We propose a lower and upper-bounding scheme based on linear programming relaxation of the formulation. Computational results show that our approach provides near optimal solutions for small problems and is capable of solving larger problems with up to 320 disassembly tasks in reasonable time

Calculation of the relative metastabilities of proteins using the CHNOSZ software package

<p>Abstract</p> <p>Background</p> <p>Proteins of various compositions are required by organisms inhabiting different environments. The energetic demands for protein formation are a function of the compositions of proteins as well as geochemical variables including temperature, pressure, oxygen fugacity and pH. The purpose of this study was to explore the dependence of metastable equilibrium states of protein systems on changes in the geochemical variables.</p> <p>Results</p> <p>A software package called CHNOSZ implementing the revised Helgeson-Kirkham-Flowers (HKF) equations of state and group additivity for ionized unfolded aqueous proteins was developed. The program can be used to calculate standard molal Gibbs energies and other thermodynamic properties of reactions and to make chemical speciation and predominance diagrams that represent the metastable equilibrium distributions of proteins. The approach takes account of the chemical affinities of reactions in open systems characterized by the chemical potentials of basis species. The thermodynamic database included with the package permits application of the software to mineral and other inorganic systems as well as systems of proteins or other biomolecules.</p> <p>Conclusion</p> <p>Metastable equilibrium activity diagrams were generated for model cell-surface proteins from archaea and bacteria adapted to growth in environments that differ in temperature and chemical conditions. The predicted metastable equilibrium distributions of the proteins can be compared with the optimal growth temperatures of the organisms and with geochemical variables. The results suggest that a thermodynamic assessment of protein metastability may be useful for integrating bio- and geochemical observations.</p