Simultaneous cell disruption and semi-quantitative activity assays for high-throughput screening of thermostable L-asparaginases View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2018-12

AUTHORS

Xu Li, Xian Zhang, Shuqin Xu, Hengwei Zhang, Meijuan Xu, Taowei Yang, Li Wang, Haifeng Qian, Huiling Zhang, Haitian Fang, Tolbert Osire, Zhiming Rao, Shangtian Yang

ABSTRACT

L-asparaginase, which catalyses the hydrolysis of L-asparagine to L-aspartate, has attracted the attention of researchers due to its expanded applications in medicine and the food industry. In this study, a novel thermostable L-asparaginase from Pyrococcus yayanosii CH1 was cloned and over-expressed in Bacillus subtilis 168. To obtain thermostable L-asparaginase mutants with higher activity, a robust high-throughput screening process was developed specifically for thermophilic enzymes. In this process, cell disruption and enzyme activity assays are simultaneously performed in 96-deep well plates. By combining error-prone PCR and screening, six brilliant positive variants and four key amino acid residue mutations were identified. Combined mutation of the four residues showed relatively high specific activity (3108 U/mg) that was 2.1 times greater than that of the wild-type enzyme. Fermentation with the mutant strain in a 5-L fermenter yielded L-asparaginase activity of 2168 U/mL. More... »

PAGES

7915

References to SciGraph publications

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/s41598-018-26241-7

    DOI

    http://dx.doi.org/10.1038/s41598-018-26241-7

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1103996475

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/29784948


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