ArticleBiotechnology letters2026
Efficient production of L-asparaginase using recombinant Pichia pastoris and strategy to eliminate glutaminase activity.
Article in Biotechnology letters, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The mortality rate of Acute Lymphoblastic Leukemia (ALL) has reduced after the incorporation of L-asparaginase (L-ASNase) in therapeutic regimes, which function via selective starvation of the cancer cells, sparing the rest. However, challenges persist due to the immunogenic nature of the enzyme and the co-glutaminase activity. This study investigates the L-ASNase coded for by the ansB gene from Serratia marcescens MTCC 97. An initial study led to a titer of 1.6 U/mL of L-ASNase in a semi synthetic media. However, due to the opportunistic pathogenic nature of the strain and lower yield of the enzyme, a robust eukaryotic host, and the Pichia pastoris GlycoSwitch® SuperMan
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