What question did this study set out to answer?

The aim is to express and characterize a synthetic L-asparaginase from Pseudoalteromonas tetraodonis in E. coli for potential therapeutic applications.

April 3, 2026Indonesian Journal of BiotechnologyOpen Access

Recombinant expression and preliminary characterization of a synthetic L‐asparaginase from the marine bacterium Pseudoalteromonas tetraodonis GFC in Escherichia coli BL21 (DE3)

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Authors

WPWulan PertiwiBandung Institute of Technology TTTaufik Ramdani TohariPadjadjaran University QSQori Atur Rodiah SuhadaBandung Institute of Technology

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Implication

Demonstrates the recombinant expression of L-asparaginase in E. coli, indicating its potential as a cancer treatment enzyme.

Key Points

The aim is to express and characterize a synthetic L-asparaginase from Pseudoalteromonas tetraodonis in E. coli for potential therapeutic applications.
The synthetic L-asparaginase gene was cloned into a pD861-SR expression vector.
The vector was transformed into Escherichia coli BL21 (DE3) for protein expression.
Recombinant protein expression was induced with L-rhamnose under the rhaBAD promoter.
Protein purification was performed using Ni-Sepharose affinity chromatography and membrane dialysis.
SDS-PAGE analysis was conducted to verify the molecular weight of expressed protein.
The expressed L-asparaginase achieved a protein purity of 73.6%.
SDS-PAGE revealed a prominent band at approximately 37 kDa, consistent with the expected molecular weight.
The purified enzyme exhibited a specific activity of 5.863 U/mg.

Cite This Study

Pertiwi et al. (2026) studied this question.

synapsesocial.com/papers/69cf5ecb5a333a821460d687 https://doi.org/10.22146/ijbiotech.114307

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Recombinant expression and preliminary characterization of a synthetic L‐asparaginase from the marine bacterium Pseudoalteromonas tetraodonis GFC in Escherichia coli BL21 (DE3)

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Key Points

Cite This Study

Recombinant expression and preliminary characterization of a synthetic L‐asparaginase from the marine bacterium Pseudoalteromonas tetraodonis GFC in Escherichia coli BL21 (DE3)

Discussion

Member takes

Implication

Key Points

Cite This Study

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