Buchumschlag

Improving of pelB-Secreted MPT64 protein released by Escherichia coli BL21 (DE3) using Triton X-100 and Tween-80

pelB has been known as a successful signal peptide to translocate the protein target extracellularly in the Escherichia coli system. However, in our previous study, the yield of MPT64 protein extracellular recovery was still low and plenty of this protein was remain trapped in cytoplasm and periplas...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Hauptverfasser: Kusuma, Sri Agung Fitri, Subroto, Toto, Parwati, Ida, Rukayadi, Yaya, Fadhlillah, Muhammad, Pardede, Ruth Michellee
Format: Artikel
Veröffentlicht: Wolters Kluwer Medknow Publications 2022
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
id oai:psasir.upm.edu.my:101825
record_format eprints
spelling oai:psasir.upm.edu.my:101825 http://psasir.upm.edu.my/id/eprint/101825/ Improving of pelB-Secreted MPT64 protein released by Escherichia coli BL21 (DE3) using Triton X-100 and Tween-80 Kusuma, Sri Agung Fitri Subroto, Toto Parwati, Ida Rukayadi, Yaya Fadhlillah, Muhammad Pardede, Ruth Michellee pelB has been known as a successful signal peptide to translocate the protein target extracellularly in the Escherichia coli system. However, in our previous study, the yield of MPT64 protein extracellular recovery was still low and plenty of this protein was remain trapped in cytoplasm and periplasm. Recently, nonionic surfactants were efficiently reported to secrete recombinant protein extracellularly. Nonetheless, it must be clarified whether the surfactant supplementation can improve the yield of MPT64 extracellular protein significantly without giving impact on the structure of isolated MPT64 protein and can minimized the cell lysis effect. MPT64 protein secretion was carried out by comparing the effects of surfactants Tween 80 and Triton × 100 at various concentrations. Triton × 100 was able to increase the extracellular MPT64 protein gain up to 3 times higher than Tween 80 and it was in line with the greater level ratio of cell leakage of Triton × 100 compared to that of Tween 80. Similarly, the viable cell of the cultures decreased dramatically. However, both surfactants did not interfere the structure of MPT64 protein. In conclusion, Triton × 100 can be chosen as the supporting surfactant to assist the act of peptide signal in improving the resulting of MPT64 extracellular protein. Wolters Kluwer Medknow Publications 2022 Article PeerReviewed Kusuma, Sri Agung Fitri and Subroto, Toto and Parwati, Ida and Rukayadi, Yaya and Fadhlillah, Muhammad and Pardede, Ruth Michellee (2022) Improving of pelB-Secreted MPT64 protein released by Escherichia coli BL21 (DE3) using Triton X-100 and Tween-80. Journal of Advanced Pharmaceutical Technology and Research, 13 (3). 171 - 176. ISSN 2231-4040; ESSN: 0976-2094 https://journals.lww.com/japtr/toc/2022/13030 10.4103/japtr.japtr_25_22
institution UPM IR
collection UPM IR
description pelB has been known as a successful signal peptide to translocate the protein target extracellularly in the Escherichia coli system. However, in our previous study, the yield of MPT64 protein extracellular recovery was still low and plenty of this protein was remain trapped in cytoplasm and periplasm. Recently, nonionic surfactants were efficiently reported to secrete recombinant protein extracellularly. Nonetheless, it must be clarified whether the surfactant supplementation can improve the yield of MPT64 extracellular protein significantly without giving impact on the structure of isolated MPT64 protein and can minimized the cell lysis effect. MPT64 protein secretion was carried out by comparing the effects of surfactants Tween 80 and Triton × 100 at various concentrations. Triton × 100 was able to increase the extracellular MPT64 protein gain up to 3 times higher than Tween 80 and it was in line with the greater level ratio of cell leakage of Triton × 100 compared to that of Tween 80. Similarly, the viable cell of the cultures decreased dramatically. However, both surfactants did not interfere the structure of MPT64 protein. In conclusion, Triton × 100 can be chosen as the supporting surfactant to assist the act of peptide signal in improving the resulting of MPT64 extracellular protein.
format Article
author Kusuma, Sri Agung Fitri
Subroto, Toto
Parwati, Ida
Rukayadi, Yaya
Fadhlillah, Muhammad
Pardede, Ruth Michellee
spellingShingle Kusuma, Sri Agung Fitri
Subroto, Toto
Parwati, Ida
Rukayadi, Yaya
Fadhlillah, Muhammad
Pardede, Ruth Michellee
Improving of pelB-Secreted MPT64 protein released by Escherichia coli BL21 (DE3) using Triton X-100 and Tween-80
author_facet Kusuma, Sri Agung Fitri
Subroto, Toto
Parwati, Ida
Rukayadi, Yaya
Fadhlillah, Muhammad
Pardede, Ruth Michellee
author_sort Kusuma, Sri Agung Fitri
title Improving of pelB-Secreted MPT64 protein released by Escherichia coli BL21 (DE3) using Triton X-100 and Tween-80
title_short Improving of pelB-Secreted MPT64 protein released by Escherichia coli BL21 (DE3) using Triton X-100 and Tween-80
title_full Improving of pelB-Secreted MPT64 protein released by Escherichia coli BL21 (DE3) using Triton X-100 and Tween-80
title_fullStr Improving of pelB-Secreted MPT64 protein released by Escherichia coli BL21 (DE3) using Triton X-100 and Tween-80
title_full_unstemmed Improving of pelB-Secreted MPT64 protein released by Escherichia coli BL21 (DE3) using Triton X-100 and Tween-80
title_sort improving of pelb-secreted mpt64 protein released by escherichia coli bl21 (de3) using triton x-100 and tween-80
publisher Wolters Kluwer Medknow Publications
publishDate 2022
_version_ 1819301298884837376
score 13.4562235

Ähnliche Einträge