Abstract
Alkaline phosphatase from bovine intestinal mucous membrane was immobilized by sorption on Na-sepiolite in order to obtain an enzyme-clay complex for soil application. Optimum conditions for immobilization were: phosphate buffer 0·1 m at pH 7, 2 h of magnetic stirring at 4°C, 0·25 mg ml −1 for the concentration of enzyme and an enzyme/clay ratio of 10 ml g −1. The adsorption isotherm obeyed the Langmuir equation (r 2 0·996 at P < 0·001), reaching a maximum amount of enzyme retention. Apparent K m values were 18·32 m m for the immobilized enzyme and 2·36 m m for the enzyme in aqueous solution; optimum pH (10·5) did not change as a consequence of immobilization; a first-order kinetic was obtained for incubation times of less than 1 h for both enzymes and the immobilized enzyme showed a lower incubation temperature optimum. The immobilized phosphatase showed less stability than the soluble enzyme in terms of storage at 30°C, thermal stability and resistance to proteolytic attack.
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