Enhanced production of extracellular L-methioninase by entire cell immobilization of Streptomyces MDMMH4 and examination of its utilization as an antioxidant agent.

Streptomyces MDMMH4 cells were immobilized in various matrices with two different techniques for the enhanced and semi-continuous production of extracellular L-methioninase. Of these, agarose was proven to be the most suitable matrix for the immobilization of cells. The optimal agarose concentration was approximately 3% and the initial cell concentration was 150mg/ml (wet cell weight). Agarose-entrapped cells increased the enzyme yield by 21% compared to the highest yield obtained with free cells. Even after twelve successive and efficient fermentation operations, the agarose blocks had good stability. They maintained 69.3% of the enzyme yield obtained in the first cycle. Applying this process on an industrial scale using agarose-entrapped cells, an inexpensive and renewable matrix will allow the stable production of L-methioninase. The purified L-methioninase could be successfully obtained after applying the purification protocol as mentioned in the previous studies. Subsequently, the purified enzyme showed that L- methioninase possessed moderate scavenging activity with high IC50 values of 390.4μg/mL (corresponding to 11.62U/mL). To our knowledge, this is the first report on L-methioninase production by whole-cell immobilization.