A study has been made of the characteristics of α-chymotrypsin and β-galactosidase trapped in polyacrylamide gels. Two methods were used to produce the gels: γ-irradiation and chemical polymerization, ammonium persulfate being used as catalyst in the latter case. The enzyme activities passed through maxima as the acrylamide concentration was increased. The supported β-galactosidase produced by chemical polymerization was approximately as active as that produced by γ-irradiation; the γ-irradiated preparation was more active in the case of α-chymotrypsin. The supported enzymes were somewhat less stable than the free enzyme.
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Bunting et al. (1973) studied this question.
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