TY - JOUR
T1 - Biochemical characterisation of MX-4, a plant cysteine protease of broad specificity and high stability
AU - Oliver-Salvador, María Del Carmen
AU - Lian, Zhirui
AU - Laursen, Richard A.
AU - Bolaños-García, Víctor M.
AU - Soriano-García, Manuel
PY - 2011/5/15
Y1 - 2011/5/15
N2 - A new proteinase, mexicain-IV (MX-4), has been purified to homogeneity from the latex fruits of Jacaratia mexicana (formely Pileus mexicanus), a plant member of the Caricaceae family. MX-4 shows a Mr of 23.7 kDa, pI of 9.3 and maximum proteolytic activity on casein and BAPNA at pH 8.0-8.5 and pH 7.0-7.5, respectively. The amino acid sequence of MX-4 and its reversible inhibition by HgCl2 show that the proteinase belongs to the family of cysteine proteinases. This enzyme exhibits rather broad substrate specificity, although there seems to be a slight preference for cleavage of peptides having certain hydrophobic residues in the P2 position. Biochemical and circular dichroism studies revealed that this enzyme belongs to the α + β class of proteins, in agreement with the results obtained by X-ray crystallographic structure determination, and showed that MX-4 has a higher pH and thermal stability than other members of the Caricaceae family, including papain. These properties make this novel protease a suitable novel analytical tool for the proteomic analysis of peptide fragments of great potential interest in the food industry and other industries.
AB - A new proteinase, mexicain-IV (MX-4), has been purified to homogeneity from the latex fruits of Jacaratia mexicana (formely Pileus mexicanus), a plant member of the Caricaceae family. MX-4 shows a Mr of 23.7 kDa, pI of 9.3 and maximum proteolytic activity on casein and BAPNA at pH 8.0-8.5 and pH 7.0-7.5, respectively. The amino acid sequence of MX-4 and its reversible inhibition by HgCl2 show that the proteinase belongs to the family of cysteine proteinases. This enzyme exhibits rather broad substrate specificity, although there seems to be a slight preference for cleavage of peptides having certain hydrophobic residues in the P2 position. Biochemical and circular dichroism studies revealed that this enzyme belongs to the α + β class of proteins, in agreement with the results obtained by X-ray crystallographic structure determination, and showed that MX-4 has a higher pH and thermal stability than other members of the Caricaceae family, including papain. These properties make this novel protease a suitable novel analytical tool for the proteomic analysis of peptide fragments of great potential interest in the food industry and other industries.
KW - Broad protease specificity
KW - Cysteine protease of industrial interest
KW - Jacaratia mexicana
KW - New analytical proteomics tool
KW - Pileus mexicanus
KW - Plant cysteine protease
KW - Plant endopeptidase
UR - http://www.scopus.com/inward/record.url?scp=78650680184&partnerID=8YFLogxK
U2 - 10.1016/j.foodchem.2010.11.040
DO - 10.1016/j.foodchem.2010.11.040
M3 - Artículo
SN - 0308-8146
VL - 126
SP - 543
EP - 552
JO - Food Chemistry
JF - Food Chemistry
IS - 2
ER -