Abstract: Allantoinases (ALNase) in the water extracts distilled from seeds and leaves of soybean (Glycine max L. cv. Keyu 10) were. remarkably heat stable. However the enzyme and non-enzyme protein in the seed extract, but not leaf extract, lost their activity and were denaturated at 75℃ for 5 min in the presence of Ca2+, Mg2+. or Mn2+ions respecitively. At room temperature over 40%～50% of the non-enzyme proteins in the seed extract could be removed by the bivalent cations without affecting the enzyme activity. This effect was weakend by the increase of concentration. Both extracts had different responses to all sorts of insoluble Ca2. salts. For the seed extract about 50 % of the non-enzyme proteins were removed by 5 % CaSO4 (W/V), without effecting the enzyme activity, while the leaf extract was sensible to Ca3 (PO4) 2. After treatment with 5 % Ca3 (PO4) 2 about 50 % of the enzyme activities and about 70% of proteins were lost. Mn2+ ions could enhance the enzyme activity in crude seed extract, but had no effect on partially purified enzyme from seeds and enzyme in crude extract from leaves. Further, EDTA had no effect on enzyme activity in both extracts.

Key words: Soybean:Allantoinases, Heat lability, Allantoinase bivalent cations