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

doi:https://doi.org/10.1021/jf904295x

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

Research output: Contribution to journal › Article › Research › peer-review

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 language	English
Pages (from-to)	11027-11035
Journal	Journal of Agricultural and Food Chemistry
Volume	58
DOIs	https://doi.org/10.1021/jf904295x
Publication status	Published - 27 Oct 2010

Keywords

Caricaceae
Latex
Papain
Plant cysteine protease
Vasconcellea quercifolia

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@article{661bb1f2d1284457aad16b2dd8330ad4,

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

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. {\textcopyright}2010 American Chemical Society.",

keywords = "Caricaceae, Latex, Papain, Plant cysteine protease, Vasconcellea quercifolia",

author = "Torres, {M. Jos{\'e}} and Trejo, {Sebasti{\'a}n A.} and Martin, {M. In{\'e}s} and Natalucci, {Claudia L.} and Avil{\'e}S, {Francesc X.} and L{\'o}pez, {Laura M.I.}",

year = "2010",

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day = "27",

doi = "https://doi.org/10.1021/jf904295x",

language = "English",

volume = "58",

pages = "11027--11035",

journal = "Journal of Agricultural and Food Chemistry",

issn = "0021-8561",

publisher = "American Chemical Society",

}

Purification and characterization of a cysteine endopeptidase from vasconcellea quercifolia A. St.-Hil. latex displaying high substrate specificity. / Torres, M. José; Trejo, Sebastián A.; Martin, M. Inés; Natalucci, Claudia L.; AviléS, Francesc X.; López, Laura M.I.

In: Journal of Agricultural and Food Chemistry, Vol. 58, 27.10.2010, p. 11027-11035.

Research output: Contribution to journal › Article › Research › peer-review

TY - JOUR

T1 - Purification and characterization of a cysteine endopeptidase from vasconcellea quercifolia A. St.-Hil. latex displaying high substrate specificity

AU - Torres, M. José

AU - Trejo, Sebastián A.

AU - Martin, M. Inés

AU - Natalucci, Claudia L.

AU - AviléS, Francesc X.

AU - López, Laura M.I.

PY - 2010/10/27

Y1 - 2010/10/27

N2 - 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.

AB - 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.

KW - Caricaceae

KW - Latex

KW - Papain

KW - Plant cysteine protease

KW - Vasconcellea quercifolia

U2 - https://doi.org/10.1021/jf904295x

DO - https://doi.org/10.1021/jf904295x

M3 - Article

VL - 58

SP - 11027

EP - 11035

JO - Journal of Agricultural and Food Chemistry

JF - Journal of Agricultural and Food Chemistry

SN - 0021-8561

ER -