Summary
The study of the molecular location of acid and alkaline phosphatases in a compost of urban refuse was initiated after their extraction using 0,05 M pyrophosphate at pH 9 and in the presence of 1 M KCl to modify its ionic strength. The extract was divided by ultrafiltration in cell-bound (UF3 fraction with ϕ>0,45 μm) and exocellular enzymes: UF23 with ϕ<0,45 μm and mol. wt.> 100 kD; UF22 with 100<moi. wt.<30 kD; UF21, with 30 <mol. wt.>l0 kD and UF1, with mol. wt.<l0 kD. Thereafter UF3 was divided by sonication in their intracellular (Ei) and membranebound components (Em) and after solubilization with Triton X-100 in enzymes located outside (Emp) and inside the membrane (Ems)
The highest activity of acid phosphatase appeared in the UF3 fraction, its extraction being unaffected by the introduction of KCl in the extractant. The UF3 fractionation located the acid PA in the membrane-protein fractions (Em). Alkaline phosphatase was predominant in the fraction UF23 showing 86% of the activity displayed by all the fractions; the increase in the ionic strength reduced this activity in UF23 (-68%) increasing the activity in UF22 (5,2% to 24,2%). In UF3, the alkaline phosphatase had an intracellular localization (Ei fraction) showing 90% of the activity displayed by UF3
Different mechanisms of stabilization for compost enzymes were postulated: acid phosphatases may be associated to membranous components of living or dead microbial cells with low solubility in the pyrophosphate extractant and alkaline phosphatase may form a soluble complex enzyme-organic matter of high mol. wt. dissociable at high ionic strength.
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Rad Moradillo, J.C., González Carcedo, S. (1996). Different Location of Acid and Alkaline Phosphatases Extracted From a Compost of Urban Refuse. In: de Bertoldi, M., Sequi, P., Lemmes, B., Papi, T. (eds) The Science of Composting. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-1569-5_28
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DOI: https://doi.org/10.1007/978-94-009-1569-5_28
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