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- W4384204544 abstract "Abstract L-asparaginase ( ASNase ), as a pivotal amidohydrolase enzyme, has been used in removing acrylamide in food processing and treating acute lymphoblastic leukaemia in clinic. In this study, a novel ASNase from Bifidobacterium thermophilum ( BtASNase ) was successfully cloned and heterologously expressed in E. coli host. BtASNase was identified to share maximum 40% structural similarity with other ASNases in PDB database. The purified BtASNase with monomeric size about 35 kDa had the highest specific activity (554.82 IU/mg) at 55℃ and pH 8.0. Further investigation indicated that BtASNase showed great stability at wide pH range (6.0–11.0), and retained more than 85% of its activity for 50 min at 37℃. To be noted, BtASNase exhibited high L-asparaginase specificity and zero glutaminase activity. To our knowledge, this is the first time to explore ASNase from Bifidobacterium thermophilum , and explored BtASNase could be a potential candidate with desirable advantages for unraveling glutaminase activity, narrow pH range stability, and low thermostability restrict in industry applications of ASNase ." @default.
- W4384204544 created "2023-07-14" @default.
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- W4384204544 date "2023-07-13" @default.
- W4384204544 modified "2023-09-25" @default.
- W4384204544 title "Characterization of a Novel Glutaminase-free L-asparaginase from Bifidobacterium Thermophilum" @default.
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- W4384204544 doi "https://doi.org/10.21203/rs.3.rs-3113826/v1" @default.
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