Comprehensive analysis of a Vibrio parahaemolyticus strain extracellular serine protease VpSP37

Valentina Catania, Giulio Ghersi, Paola Quatrini, Aldo Nicosia, Carmelo Bennici, Angela Cuttitta, Giulio Ghersi, Monica Salamone, Salvatore Mazzola, Aldo Nicosia, Monica Salamone

Risultato della ricerca: Articlepeer review

16 Citazioni (Scopus)


Proteases play an important role in the field of tissue dissociation combined with regenerative medicine. During the years new sources of proteolytic enzymes have been studied including proteases from different marine organisms both eukaryotic and prokaryotic. Herein we have purified a secreted component of an isolate of Vibrio parahaemolyticus, with electrophoretic mobilities corresponding to 36 kDa, belonging to the serine proteases family. Sequencing of the N-terminus enabled the in silico identification of the whole primary structure consisting of 345 amino acid residues with a calculated molecular mass of 37.4 KDa. The purified enzyme, named VpSP37, contains a Serine protease domain between residues 35 and 276 and a canonical Trypsin/Chimotrypsin 3D structure. Functional assays were performed to evaluate protease activity of purified enzyme. Additionally the performance of VpSP37 was evaluated in tissue dissociations experiments and the use of such enzyme as a component of enzyme blend for tissue dissociation procedures is strongly recommended.
Lingua originaleEnglish
pagine (da-a)1-19
Numero di pagine19
RivistaPLoS One
Stato di pubblicazionePublished - 2015

All Science Journal Classification (ASJC) codes

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  • ???subjectarea.asjc.1100.1100???
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