Abstract:

One endo-β-1,4-glucanase (EG-1) was purified to electrophoretical homogeneity from the gut extract of Apriona germari larvae by acetone precipitating, gel filtrating, ion exchange chromatography and preparative PAGE, and its enzymatic properties were investigated. The enzyme component showed high activity on sodium carboxymethylcellulose (CMC). The molecular weight of EG-1 was 26ku and the isoelectric point (pI) was about 4.0 It had an optimal temperature of 45℃ and optimal pH of 5.2 The enzyme activity was stable at 37℃ for at least 2h, but decreased rapidly when kept at 50℃ and almost no activity was left after incubated at 70℃ for 2h. All these showed that EG-1component was suit for the insect intestinal environment, and should be a endogenous enzyme.

Key words: Apriona germari, Endo-&beta, -1, 4-glucanase, Purification, Properties