Chitosan was linked to cellulase (EC 3.2.1.4) from Trichoderma viride by covalent conjugation to periodate-activated carbohydrate moieties of the enzyme. The modi®ed enzyme contained about 1.5 mol of polymer per mol of protein. The speci®c activity of the conjugate prepared was 39.8% of the native cellulase. The optimum pH and temperature for cellulase remained unaltered after modi®cation. The thermostability was increased by 8.9°C for the cellulase±chitosan complex. Thermal inactivation at different temperatures ranging from 65°C to 80°C was markedly increased for the polymer-modi®ed enzyme. The stability within the pH range 1.0±3.2 was also improved for the modi®ed enzyme.

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