| Research Title |
Comparative of recombinant Vespa affinis hyaluronidase expressed in different cloning vector and their biological properties |
| Date of Distribution |
1 June 2018 |
| Conference |
| Title of the Conference |
ANICEAS International Conference on Applied Sciences, Engineering Management and Information Technology (AEMI-JUNE-2018) |
| Organiser |
Society of Computer, Engineering Technology & Applied Sciences |
| Conference Place |
The Aqueen Hotel Paya Lebar 33 Jalan Afifi, Singapore |
| Province/State |
Jalan Afifi, Singapore |
| Conference Date |
1 June 2018 |
| To |
2 June 2018 |
| Proceeding Paper |
| Volume |
2018 |
| Issue |
AEMI-JUNE-2018 |
| Page |
15 |
| Editors/edition/publisher |
|
| Abstract |
Cloning and expression of recombinant Vespa affinis hyaluronidase (rVesA2) was successfully expressed in Escherichia coli system. The VesA2 gene was cloned into pET-17b and pET-32a cloning vector which had molecular
weight 41.71 and 59.0 kDa, respectively. The recombinant plasmid of pET-17b was composed 1.08 kDa his-tag at the
N-terminal. The 17.14 kDa of fusion tag; thioredoxin tag, histidine tag, and S-tag, was found in pET-32a. The verified
expression conditions of rVesA2 induced under the conditions of 0.1 mM IPTG at 37C for 4 hrs gave the highest
quantity of protein expression. The colony PCR and sequencing analysis were used to verify the rVesA2. The positive clones were detected the hyaluronidase activity by a zymographic gel. Recombinant proteins from both cloning vec-
tors were insoluble. However, the recombinant from pET-32a showed higher solubility than that form pET-17b, after dissolving in 4 M urea solution. This result suggests that the fusion tag increase protein solubility. |
| Author |
|
| Peer Review Status |
มีผู้ประเมินอิสระ |
| Level of Conference |
นานาชาติ |
| Type of Proceeding |
Full paper |
| Type of Presentation |
Oral |
| Part of thesis |
true |
| Presentation awarding |
false |
| Attach file |
|
| Citation |
0
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Publication
Journal Publication
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