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Comparative of Recombinant Vespa affinis Hyaluronidase Expressed in Different Cloning Vectors and their Biological Properties

Author

Listed:
  • Piyapon Janpan

    (Faculty of Pharmaceutical Sciences, Khon Kaen University, Khon Kaen, Thailand)

  • Yutthakan Saengkun

    (Faculty of Pharmaceutical Sciences, Khon Kaen University, Khon Kaen, Thailand)

  • Prapenpuksiri Rungsa

    (Faculty of Pharmaceutical Sciences, Protein and Proteomics Research Center for Commercial and Industrial Purposes Khon Kaen University, Khon Kaen, Thailand)

  • Mongkol Vesaratchavest

    (Research and Development Center Betagro Public Company Limited Klong Nueng, Klong Luang, Pathumthani)

  • Tewa Upathanpreecha

    (Research and Development Center, Betagro Public Company Limited, Klong Nueng, Klong Luang, Pathumthani)

  • Patthana Tastub

    (Research and Development Center, Betagro Public Company Limited, Klong Nueng, Klong Luang, Pathumthani)

  • Sakda Daduang

    (Faculty of Pharmaceutical Sciences Protein and Proteomics Research Center for Commercial and Industrial Purposes Khon Kaen University, Khon Kaen, Thailand)

Abstract

Cloning and expression of recombinant Vespa affinis hyaluronidase (rVesA2) were successfully expressed in Escherichia coli system. The VesA2 gene was cloned into pET-17b and pET-32a cloning vectors 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 37â—¦C 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 vectors 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.

Suggested Citation

  • Piyapon Janpan & Yutthakan Saengkun & Prapenpuksiri Rungsa & Mongkol Vesaratchavest & Tewa Upathanpreecha & Patthana Tastub & Sakda Daduang, 2018. "Comparative of Recombinant Vespa affinis Hyaluronidase Expressed in Different Cloning Vectors and their Biological Properties," International Journal of Applied and Physical Sciences, Dr K.Vivehananthan, vol. 4(2), pages 38-44.
    • Handle: RePEc:apa:ijapss:2018:p:38-44
    DOI: 10.20469/ijaps.4.50001-2.pdf
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    1. Rory Anthony Hutagalung & Hermawan & Stella Magdalena & Isdaryanto Iskandar & Sylvain Mastrorillo, 2017. "Increasing Growth and Survival Rate of Land Hermit Crabs (Coenobita sp.) in Artificial Habitat through Feeding Habit," International Journal of Applied and Physical Sciences, Dr K.Vivehananthan, vol. 3(3), pages 55-59.
    2. Patama Bunruk & Duangporn Kantachote & Ampaitip Sukhoom, 2017. "Isolation and selection of purple non-sulfur bacteria for phosphate removal in rearing water from shrimp cultivation," Journal of Applied and Physical Sciences, Prof. Vakhrushev Alexander, vol. 3(2), pages 73-80.
    3. Noraini Mahmad & Rosna Mat Taha & Norlina Rawi & Sadegh Mohajer, 2015. "The effects of picloram and 2,4-dichlorophenoxyacetic acid on induction of red coloured callus from celosia plumosa, an attractive ornamental plant," Journal of Applied and Physical Sciences, Prof. Vakhrushev Alexander, vol. 1(1), pages 9-12.
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