Abstract A novel asparaginase (designated srnASNase) has been purified from soybean root nodules and identified by MALDI‐TOF/TOF‐MS. And the enzymatic properties, antitumor activity and the ability to prevent acrylamide formation in fried foods of srnASNase were evaluated. SrnASNase had high specific activity (531.37 U/mg) toward L‐asparagine under optimum conditions (pH 8.0 and 40°C), no activity toward L‐glutamine and D‐glutamine, but trace activity toward D‐asparagine. It was stable in the pH range of 7.0–9.0 and up to 40°C. The Km ...