2012 ©
Journal Publication
Title of Article Comparative of Recombinant Vespa affinis Hyaluronidase Expressed in Different Cloning Vector and their Biological Properties 
Date of Acceptance 23 May 2018 
     Title of Journal International Journal of Applied and Physical Sciences (IJAPS) 
     Standard OTHER () 
     Institute of Journal kkg publications 
     ISBN/ISSN 2414-8946 
     Volume 2018 
     Issue Volume 4, Issue 2 
     Month July
     Year of Publication 2018 
     Page 38-44 
     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. 
     Keyword Hyaluronidase enzyme, hyaluronic acid, banded tiger wasp  
585150037-8 Mr. PIYAPON JANPAN [Main Author]
Pharmaceutical Sciences Master's Degree
Pharmaceutical Sciences Master's Degree

Reviewing Status มีผู้ประเมินอิสระ 
Status ตีพิมพ์แล้ว 
Level of Publication นานาชาติ 
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