Purification and characterization of a cysteine endopeptidase from vasconcellea quercifolia A. St.-Hil. latex displaying high substrate specificity

M. José Torres, Sebastián A. Trejo, M. Inés Martin, Claudia L. Natalucci, Francesc X. AviléS, Laura M.I. López

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17 Citations (Scopus)

Abstract

A new proteolytic preparation from Vasconcellea quercifolia ("oak leaved papaya") latex containing several cysteine endopeptidases with high proteolytic activity has been obtained. The specific activity of the new enzymatic preparation (VQ) was higher than that of Carica papaya latex. VQ was able to coagulate milk and to hydrolyze caseins and then could be used to produce cheeses and/or casein hydrolysates. Ion exchange chromatography of VQ allowed the isolation of a new protease, named quercifoliain I, homogeneous when analyzed by SDS-PAGE, IEF and MALDI-TOF-MS. Molecular mass was 24195 Da, and its isoelectric point was >9.3. The N-terminal sequence was determined (YPESVDWRQ). Insulin B-chain cleavage showed higher specificity than that of papain and was restricted to glycyl and alanyl residues at P' position. The tryptic peptide mass fingerprint of quercifoliain I analyzed with the MASCOT search tool did not find a match with papain or any other plant cysteine proteases. ©2010 American Chemical Society.
Original languageEnglish
Pages (from-to)11027-11035
JournalJournal of Agricultural and Food Chemistry
Volume58
DOIs
Publication statusPublished - 27 Oct 2010

Keywords

  • Caricaceae
  • Latex
  • Papain
  • Plant cysteine protease
  • Vasconcellea quercifolia

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