L-Asparaginase Immobilized within Semipermeable Microcapsules: in vitro and in vivo Stability

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Abstract
L-Asparaginase from E. coli has been immobilized within semipermeable microcapsules which retain the enzyme and allow asparagine to enter the microcapsules to be acted on by the microencapsulated asparaginase. When stored in vitro at 4°C the microencapsulated asparaginase retained 90% of its original activity after 100 days ; at 37 °C, the microencapsulated enzyme is also much more stable than the same enzyme in free solution. After intraperitoneal injection into mice, the microencapsulated asparaginase lowered the plasma asparagine level to zero and maintained this level for a significantly longer period of time than asparaginase in free solution with the same assayed activity.

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