Heterologous expression and mutagenesis of recombinant Vespa affinis hyaluronidase protein (rVesA2).
Prapenpuksiri RungsaPiyapon JanpanYutthakan SaengkunNisachon JangprommaSompong KlaynongsruangRina PatramanonNunthawun UawonggulJureerat DaduangSakda DaduangPublished in: The journal of venomous animals and toxins including tropical diseases (2019)
The recombinant wild-type protein showed its maximal activity at pH 2, more acidic pH than that found in the crude venom. The glycosylation was predicted to be responsible for the pH optimum and thermal stability of the enzymes activity.