Arylamidase activity in soils: effect of trace elements and relationships to soil properties and activities of amidohydrolases

The enzyme arylamidase (ol-aminoacyl-peptide hydrolase, EC 3.4.11.2) cataly zes the hydrolysis of an N-terminal amino acid from peptides, amides or ary lamides in soils. Recently, the activity of this enzyme was detected in soi ls, and a method was developed for its assay. The method was used in studie s of the effects of salts of 25 trace elements on the activity of arylamida se in field-moist soils and their air-dried counterparts. At 5 mu mol g-l s oil, the activity of arylamidase was inhibited in both air-dried and field- moist samples by 18 of the 25 trace elements used, and Ag(I), Hg(II) and Cd (II) were the most effective inhibitors (>55%). At this concentration, Co(I I), Mg(II), Mn(II), B(III) and As(V) activated this enzyme in field-moist s oils and their air-dried counterparts (1-49%), and W(VI) and Mo(VI) activat ed this enzyme in air-dried soils (4-21%), but inhibited it in the field-mo ist soils (7-46%). Arylamidase activity was significantly correlated with t he content of organic C (r = 0.80(***), P < 0.001), total N (r = 0.71(***)) , and clay (r = 0.49(**), P < 0.05), but not with sand or the pH of the 26 surface soils examined. The activity of this enzyme in soils was significan tly correlated with the activities of L-asparaginase (r = 0.91(***)), L-asp artase (r = 0.90(***)), urease (r = 0.8(7***)), and L-glutaminase (r = 0.84 (***)) and with amidase (r = 0.39(*)). (C) 2001 Elsevier Science Ltd. All r ights reserved.