作者: C. Dinnella , G. Lanzarini , P. Ercolessi
DOI: 10.1016/0032-9592(95)80006-9
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摘要: Abstract An endo-pectinlyase present in a commercial mixture was immobilized on EUDRAGIT L100-55, polymer which is reversibly soluble-insoluble depending the pH of medium. The enzymic activities biocatalytic matrices, obtained by pre-activating either with water-soluble carbodiimide or simple adsorption, were compared. biocatalyst adsorption showed an activity higher (500 E.U. g −1 ) than that using activated (50 ). Moreover, activating agent did not seem to be necessary order stabilize interaction between carrier and protein. In fact about 80% initial detectable both matrices after repeated washings NaCl 0.2 m . immobilization procedure alter main biochemical parameters enzyme respect its native form appreciably enhanced stability temperature range 25-45°C.