THERMOSTABLE ALKALINE LIPASE FROM A NEWLY ISOLATED THERMOPHILIC BACILLUS, STRAIN A30-1 (ATCC-53841)

A thermophilic bacterium was isolated from a hot spring area of Yellow stone National Park. The organism grew optimally at 60-65 degrees C an d in the pH range of 6-9. It was characterized as Bacillus sp. In the presence of corn or olive oil (1.0%) as the growth substrate, this Bac illus produced an extracellular lipolytic activity (EC 3.1.1.3). The e nzyme activity could be efficiently recovered by ultrafiltration of ce ll-free culture supernatant. The partially purified lipase preparation had an optimum temperature of 60 degrees C, at an optimum pH of 9.5. It retained 100% of the original activity after being heated at 75 deg rees C for half an hour. The half life of the enzyme was 8 h at 75 deg rees C. The enzyme retained at least 90% of tie original activity afte r it was incubated at 60 degrees C for 15 h at pH's in the range of 5 to 10.5. The enzyme was active on triglycerides containing fatty acids having a carbon chain length of C16:0 to C22:0 as well as on natural fats and oils. The enzyme activity was stable to both hydrogen peroxid e and alkaline protease which are detergent ingredients. The purified enzyme had an isoelectric point of 5.15 and an approximate molecular w eight of 65,000.