Immobilization of S-Methyltransferase

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Abstract
S-methyltransferase was solubilized from pig liver microsomes by treatment with N-dodecyl-N,N-dimethyl-3-ammonio-l-sulfonate (Zwittergent®). The soluble enzyme was immobilized by covalent binding to agarose and by copolymerization with acrylamide. The specific activity for the agarose-bound enzyme towards the substrate ethane thiol was 0.87 nmol/min/mg and for the acrylamide-bound enzyme 0.55 nmol/min/mg. The specific activity of the soluble enzyme was found to vary with increasing chain length of the substrate molecules from 0.5 nmol/min/mg for methane thiol (C(1)) to 6.3 nmol/min/mg for n-heptane thiol (C(7)). After binding of the enzyme to agarose beads, the increase in specific activity towards substrates with increasing chain length was no longer detectable. Instead, a relatively constant specific activity of 1.1 nmol/min/mg was observed for the whole range of substrates tested from C(1) to C(7). The stability of the agarose immobilized enzyme at -20 °C is twice as good as the soluble enzyme. The acrylamide immobilized enzyme is less stabile than the soluble enzyme.

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