Extracellular expression of <i>Saccharomyces cerevisiae</i>’s L-asparaginase II in <i>Pichia pastoris</i> results in novel enzyme with better parameters

Biasoto, Henrique Pellin; Hebeda, Cristina Bichels; Farsky, Sandra Helena Poliselli; Pessoa, Adalberto; Costa-Silva, Tales A.; Monteiro, Gisele

doi:10.1080/10826068.2022.2111582

Cited by 2 publications

(1 citation statement)

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“…As a result, L-ASNase with a specific activity of 218.2 IU mg −1 was expressed, and the resulting enzyme was 40% more stable when incubated with human serum than the commercially available E. coli ASNase (EcASNaseII). In addition, ScASNaseII has 50% less cross-reactivity with an anti-ASNase antibody raised against EcASNaseII than with ASNase from E. chrysanthemi [189].…”

Section: Affinity Tagsmentioning

confidence: 98%

Engineering and Expression Strategies for Optimization of L-Asparaginase Development and Production

Shishparenok,

Gladilina,

Zhdanov

2023

IJMS

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Genetic engineering for heterologous expression has advanced in recent years. Model systems such as Escherichia coli, Bacillus subtilis and Pichia pastoris are often used as host microorganisms for the enzymatic production of L-asparaginase, an enzyme widely used in the clinic for the treatment of leukemia and in bakeries for the reduction of acrylamide. Newly developed recombinant L-asparaginase (L-ASNase) may have a low affinity for asparagine, reduced catalytic activity, low stability, and increased glutaminase activity or immunogenicity. Some successful commercial preparations of L-ASNase are now available. Therefore, obtaining novel L-ASNases with improved properties suitable for food or clinical applications remains a challenge. The combination of rational design and/or directed evolution and heterologous expression has been used to create enzymes with desired characteristics. Computer design, combined with other methods, could make it possible to generate mutant libraries of novel L-ASNases without costly and time-consuming efforts. In this review, we summarize the strategies and approaches for obtaining and developing L-ASNase with improved properties.

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Section: Affinity Tagsmentioning

confidence: 98%