抄録
Bacterial α-amylase was inacti ethylenediamine tetraacetate and, reactivated by the addition of salts alkaline earth metals, respectively, p the reactivated amylase were investi
1) The enzyme activities of the amylase in relation to the associk decreased in the following order: Ba and Be.
2) The stability of the reactivate at alkaline side was not so significant according to the kind of metals, w ception of beryllium-reactivated amy as well as the EDTA-inactivated ar sensitive to alkaline condition.
3) The stability of the reactivat to heat remarkably varied with the metals decreasing in the following 4 Sr, Ba, Mg and Be. Though the amylase was stable at temperatures l:it easily lost its competence of rea, temperatures above 40°C.
4) Only the calcium-amylase ex. solute resistance to proteinase. The d by proteinase occurred gradually in amylase while it proceeded rapidly ii lases reactivated by other metals.
5) All the reactivated amylases to be almost equal in their degree of on starch, in spite of the remarkable in activity and stability.
