Please use this identifier to cite or link to this item: https://hdl.handle.net/10321/3763
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dc.contributor.authorRamlucken, Uraishaen_US
dc.contributor.authorKrishna, Suresh Babu Naiduen_US
dc.contributor.authorGovender, Patricken_US
dc.date.accessioned2022-01-13T08:43:15Z-
dc.date.available2022-01-13T08:43:15Z-
dc.date.issued2021-12-31-
dc.identifier.citationRamlucken, U., Babu Naidu, K.S. and Govender, P. 2021.Improved production of HIV-1 subtype C protease from transgenic E. Coli. The Open Microbiology Journal. 15(1): 168-176. doi:10.2174/1874285802115010168en_US
dc.identifier.issn1874-2858-
dc.identifier.urihttps://hdl.handle.net/10321/3763-
dc.description.abstractBackground: Human Immunodeficiency Virus 1 (HIV-1) subtype C is responsible for the majority of infections of patients in Southern Africa. The HIV protease is a primary target for the development of highly efficient anti-retroviral pharmaceuticals because of its pivotal role in the maturation of the virus in the host cell. For target validation of novel HIV protease inhibitors, there is a need for the availability of an abundance of this protease. Objective: This study reports an optimized method to produce HIV-1 protease derived from HIV-1 subtype C. Methods: It involves the use of a transgenic E. colistrain that overexpresses the native form of the enzyme <jats:italic>via</jats:italic> inclusion bodies. A stringent method for the isolation, purification, and renaturation resulted in the production of highly pure active HIV-1 protease. In order to facilitate an increase in protease yields, an optimized growth strategy was developed. In this regard, a chemically defined medium with lower glucose content and devoid of essential amino acids of the TCA cycle was used as an alternative to the widely used nutrient-rich Luria Bertani (LB) medium. Results: Results indicated an increase in protease yield up to twice the amount, thereby making this medium an attractive alternative for increasing biomass and HIV protease production for future research. Conclusion: An optimized method for HIV-1 protease derived from HIV-1 subtype C production using chemically defined media was established. This was achieved using a known method to isolate and purify the enzyme with the use of a specialized feeding strategy.en_US
dc.format.extent9 p.en_US
dc.language.isoenen_US
dc.publisherBentham Science Publishers Ltd.en_US
dc.relation.ispartofThe Open Microbiology Journal; Vol. 15, Issue 1en_US
dc.subject0707 Veterinary Sciencesen_US
dc.subjectE. colien_US
dc.subjectHIV proteaseen_US
dc.subjectIon exchange chromatographyen_US
dc.subjectOptimizationen_US
dc.subjectSulfate-polyacrylamide gelen_US
dc.subjectElectrophoresis.en_US
dc.titleImproved production of HIV-1 subtype C protease from transgenic E. colien_US
dc.typeArticleen_US
dc.date.updated2022-01-11T11:35:36Z-
dc.identifier.doi10.2174/1874285802115010168-
local.sdgSDG03-
item.fulltextWith Fulltext-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.languageiso639-1en-
item.openairetypeArticle-
item.grantfulltextopen-
item.cerifentitytypePublications-
Appears in Collections:Research Publications (Applied Sciences)
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