The linamarase of Leuconostoc mesenteroides: Production, isolation and some properties

Leuconostoc mesenteroides was found to produce highly active linamarase when linamarin was incorporated in its growth medium. The enzyme was isolated from the bacterium and partially purified using diethylaminoethyl (DEAE) cellulose. Its activity was measured spectrophotometrically using linamarin extract. This yielded 62.2 mg CN− g−1 of linamarin. A study of some of its properties showed it was active in the temperature range of ‐10 to +45°C, with an optimum at 29°2°C. Activity was observed over a wide pH range, 4.0–8.0, with optimum at 6.0–6.5. Its pH of stability was 5.5–7.5, while above pH 8.0 there was a rapid loss of activity. Incubating the enzyme at 50°C led to loss of over 90% of its activity within 18 min. The optimal substrate concentration was 0.15–0.20 ml−1. Whereas above 0.25 mg ml−1 there was no observable increase in activity, loss of activity became more pronounced below 0.10 mg ml−1 of substrate.