RESUMEN
Life cycle assessment (LCA) has been used in waste management for the last two decades and hundreds of journal papers have been published. The use of LCA in waste management has provided a much-improved holistic view of waste management including waste flows and potential environmental impacts. Although much knowledge has been obtained from LCA studies, there is still a need to use LCA models in integrated waste management. This paper describes six areas where LCA is expected to play a role in waste management in the future: 1) understanding an existing waste management system; 2) improving existing waste management systems; 3) comparing alternative technologies/ technology performance; 4) technology development/prospective technologies; 5) policy development/strategic development; and 6) reporting. Illustrative examples are provided for each application area.
Asunto(s)
Eliminación de Residuos , Administración de Residuos , Ambiente , Formulación de Políticas , Estudios ProspectivosRESUMEN
From gurza poison phosphodiesterase covalently bound with DEAE-cellulose via triazine dye was isolated. Immobilized phosphodiesterase retained 100% activity of the initial enzyme. The effect of pH, temperature. Mg++ concentration on the immobilized enzyme activity was studied. Preparations of the immobilized enzyme did not lose their activity upon hydrolysis of oligodeoxy- and ribonucleotides during a month and remained suitable for prolonged hydrolysis of preparative quantities of oligonucleotides.
Asunto(s)
Enzimas Inmovilizadas/aislamiento & purificación , Hidrolasas Diéster Fosfóricas/aislamiento & purificación , Venenos de Víboras/enzimología , Cromatografía DEAE-Celulosa , Estabilidad de Enzimas , Enzimas Inmovilizadas/metabolismo , Concentración de Iones de Hidrógeno , Hidrólisis , Magnesio , Oligodesoxirribonucleótidos/metabolismo , Hidrolasas Diéster Fosfóricas/metabolismo , Ribonucleótidos/metabolismo , TemperaturaRESUMEN
Glucoamylase from Endomycopsis species 20-9 was immobilized on AE-cellulose by covalent binding with the use of glutaraldehyde. The activity of immobilized preparations was measured as a function of pH, buffer concentration, temperature and immobilization time. The most active preparations of immobilized glucoamylase were obtained in 0.2 M Na-phosphate buffer, pH 5.0--7.0 at 4--20 degrees C for 4--24 hrs. In the presence of substrate--starch the activity of immobilized glucoamylase increased almost two-fold whereas glucose had no effect of this kind.