AbstractPoly(methoxygalacturonide) lyase (PMGL) (E.C. 4.2.2.10) was purified from a commercial preparation and immobilized by the metal link method. The properties of DEAE‐cellulose‐Ti‐PMGL and of porous glass‐Ti‐PMGL were compared with those of the native enzyme; despite the presence of the metal and the heterogeneity of the substrate, pectin, typical substrate–enzyme‐support interactions were demonstrated by shifts in pH optima andKMvalues. The possible industrial application of DEAE‐cellulose‐Ti