Perturbation of the peptidoglycan network and utilization of the signal recognition particle-dependent pathway enhances the extracellular production of a truncational mutant of CelA in Escherichia coli
DC Field | Value | Language |
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dc.contributor.author | Kang, Tae-Gu | - |
dc.contributor.author | Hong, Seok-Hyun | - |
dc.contributor.author | Jeon, Gi-Beom | - |
dc.contributor.author | Yang, Yung-Hun | - |
dc.contributor.author | Kim, Sun-Ki | - |
dc.date.accessioned | 2021-09-23T07:40:17Z | - |
dc.date.available | 2021-09-23T07:40:17Z | - |
dc.date.issued | 2021-06 | - |
dc.identifier.issn | 1367-5435 | - |
dc.identifier.issn | 1476-5535 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/49655 | - |
dc.description.abstract | Caldicellulosiruptor bescii is the most thermophilic, cellulolytic bacterium known and has the native ability to utilize unpretreated plant biomass. Cellulase A (CelA) is the most abundant enzyme in the exoproteome of C. bescii and is primarily responsible for its cellulolytic ability. CelA contains a family 9 glycoside hydrolase and a family 48 glycoside hydrolase connected by linker regions and three carbohydrate-binding domains. A truncated version of the enzyme (TM1) containing only the endoglucanase domain is thermostable and actively degrades crystalline cellulose. A catalytically active TM1 was successfully produced via the attachment of the PelB signal peptide (P-TM1), which mediates post-translational secretion via the SecB-dependent translocation pathway. We sought to enhance the extracellular secretion of TM1 using an alternative pathway, the signal recognition particle (SRP)-dependent translocation pathway. The co-translational extracellular secretion of TM1 via the SRP pathway (D-TM1) resulted in a specific activity that was 4.9 times higher than that associated with P-TM1 overexpression. In batch fermentations, the recombinant Escherichia coli overexpressing D-TM1 produced 1.86 +/- 0.06 U/ml of TM1 in the culture medium, showing a specific activity of 1.25 +/- 0.05 U/mg cell, 2.7- and 3.7-fold higher than the corresponding values of the strain overexpressing P-TM1. We suggest that the TM1 secretion system developed in this study can be applied to enhance the capacity of E. coli as a microbial cell factory for the extracellular secretion of this as well as a variety proteins important for commercial production. | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | OXFORD UNIV PRESS | - |
dc.title | Perturbation of the peptidoglycan network and utilization of the signal recognition particle-dependent pathway enhances the extracellular production of a truncational mutant of CelA in Escherichia coli | - |
dc.type | Article | - |
dc.identifier.doi | 10.1093/jimb/kuab032 | - |
dc.identifier.bibliographicCitation | JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY, v.48, no.5-6 | - |
dc.description.isOpenAccess | Y | - |
dc.identifier.wosid | 000672768400004 | - |
dc.identifier.scopusid | 2-s2.0-85110432816 | - |
dc.citation.number | 5-6 | - |
dc.citation.title | JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY | - |
dc.citation.volume | 48 | - |
dc.type.docType | Article | - |
dc.publisher.location | 영국 | - |
dc.subject.keywordAuthor | Signal recognition particle-dependent pathway | - |
dc.subject.keywordAuthor | Extracellular secretion | - |
dc.subject.keywordAuthor | CelA | - |
dc.subject.keywordPlus | RECOMBINANT PROTEIN EXPRESSION | - |
dc.subject.keywordPlus | ANTARCTICA LIPASE-B | - |
dc.subject.keywordPlus | CALDICELLULOSIRUPTOR-BESCII | - |
dc.subject.keywordPlus | SECRETION | - |
dc.subject.keywordPlus | DEFICIENT | - |
dc.subject.keywordPlus | MIRABILIS | - |
dc.subject.keywordPlus | STRAINS | - |
dc.subject.keywordPlus | IMPROVE | - |
dc.subject.keywordPlus | TAGS | - |
dc.relation.journalResearchArea | Biotechnology & Applied Microbiology | - |
dc.relation.journalWebOfScienceCategory | Biotechnology & Applied Microbiology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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