Twin-arginine signal peptide of Bacillus licheniformis GlmU efficiently mediated secretory expression of protein glutaminase

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dc.contributor.authorNiu, Dandanen_ZA
dc.contributor.authorLi, Congyingen_ZA
dc.contributor.authorWang, Pengen_ZA
dc.contributor.authorHuang, Leien_ZA
dc.contributor.authorMchunu, Nokuthula Peaceen_ZA
dc.contributor.authorSingh, Surenen_ZA
dc.contributor.authorPrior, Bernard A.en_ZA
dc.contributor.authorYe, Xiuyunen_ZA
dc.date.accessioned2021-09-08T06:37:33Z
dc.date.available2021-09-08T06:37:33Z
dc.date.issued2019
dc.descriptionCITATION: Niu, D., et al. 2019. Twin-arginine signal peptide of Bacillus licheniformis GlmU efficiently mediated secretory expression of protein glutaminase. Electronic Journal of Biotechnology, 42:49-55. doi:10.1016/j.ejbt.2019.10.006
dc.descriptionThe original publication is available at https://www.sciencedirect.com/journal/electronic-journal-of-biotechnology
dc.description.abstractBackground: Protein glutaminase specifically deamidates glutamine residue in protein and therefore significantly improves protein solubility and colloidal stability of protein solution. In order to improve its preparation efficiency, we exploited the possibility for its secretory expression mediated by twin-arginine translocation (Tat) pathway in Bacillus licheniformis. Results: The B. licheniformis genome-wide twin-arginine signal peptides were analyzed. Of which, eleven candidates were cloned for construction of expression vectors to mediate the expression of Chryseobacterium proteolyticum protein glutaminase (PGA). The signal peptide of GlmU was confirmed that it significantly mediated PGA secretion into media with the maximum activity of 0.16 U/ml in Bacillus subtilis WB600. A mutant GlmU-R, being replaced the third residue aspartic acid of GlmU twin-arginine signal peptide with arginine by site-directed mutagenesis, mediated the improved secretion of PGA with about 40% increased (0.23 U/ml). In B. licheniformis CBBD302, GlmU-R mediated PGA expression in active form with the maximum yield of 6.8 U/ml in a 25-l bioreactor. Conclusions: PGA can be produced and secreted efficiently in active form via Tat pathway of B. licheniformis, an alternative expression system for the industrial-scale production of PGA.en_ZA
dc.description.sponsorshipNational Natural Science Foundation of China
dc.description.sponsorshipIntergovernmental International Scientific and Technological Innovation Cooperation Program
dc.description.urihttps://www.sciencedirect.com/science/article/pii/S0717345819300466
dc.description.versionPublisher's version
dc.format.extent7 pages
dc.identifier.citationNiu, D., et al. 2019. Twin-arginine signal peptide of Bacillus licheniformis GlmU efficiently mediated secretory expression of protein glutaminase. Electronic Journal of Biotechnology, 42:49-55. doi:10.1016/j.ejbt.2019.10.006
dc.identifier.otherdoi:10.1016/j.ejbt.2019.10.006
dc.identifier.urihttp://hdl.handle.net/10019.1/123001
dc.language.isoen_ZAen_ZA
dc.publisherElsevier
dc.rights.holderPontificia Universidad Católica de Valparaíso
dc.subjectArginineen_ZA
dc.subjectAspartic aciden_ZA
dc.subjectBacillus licheniformisen_ZA
dc.subjectBacillus subtilis -- Geneticsen_ZA
dc.subjectEscherichia colien_ZA
dc.subjectProstaglandins Aen_ZA
dc.subjectProtein glutaminaseen_ZA
dc.subjectProtein sorting signalsen_ZA
dc.subjectSecretion expressionen_ZA
dc.subjectSignal peptideen_ZA
dc.subjectTat pathwayen_ZA
dc.subjectBacillus (Bacteria) -- Biotechnologyen_ZA
dc.titleTwin-arginine signal peptide of Bacillus licheniformis GlmU efficiently mediated secretory expression of protein glutaminaseen_ZA
dc.typeArticleen_ZA
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