Poly(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 and KM values. The possible industrial application of DEAE‐cellulose‐Ti‐PMGL is discussed.
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Hanisch et al. (1978) studied this question.
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