10.22376/ijpbs.2019.10.1.p1-12 Volume 4 Issue 4 2013 (October - December) L-Asparaginase gives a great benefit in the cancer treatment, especially in acute lymphoblastic leukemia. L-Asparaginase is also proven to reduce the acrylamide content in the foods. The objective of this study was to perform immobilization and characterization L-Asparaginase produced from  lessThan i greaterThan Bacillus licheniformis lessThan /i greaterThan  Strain HSA3-1a. The results showed that the free form L-Asparaginase from lessThan i greaterThan B. licheniformis lessThan /i greaterThan  HSA3-1a has optimum activity at pH 8 and 50 lessThan sup greaterThan o lessThan /sup greaterThan C, with a specific activity of 616.26 IU/mg protein and stabilized at the optimum pH and temperature for 60 minutes. The immobilized L-Asparaginase with activated glutaraldehyde-carbon carrier has optimum activity at pH 7 and 60 lessThan sup greaterThan ° lessThan /sup greaterThan C with a specific activity of 499.27 IU/mg protein and stabilized at the optimum pH and temperature for 60 minutes. The immobilized L-Asparaginase can retain its activity by 84.79% after 2 times repeated use. AHYAR AHMAD, ABDUL MUIS PATTA AND HASNAH NATSIR L-Asparaginase, Bacillus licheniformis Strain HSA3-1a, immobilization, and specific activity 274-280