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EVALUATION OF THE PROTEOLYTIC SUSCEPTIBILITY OF THREE LECTINS FROM SUBTRIBE DIOCLEINAE USING ENZYMATIC ACTION, HEAT TREATMENT AND MOLECULAR MODELING
Author(s) -
RAMOS MÁRCIO VIANA,
TEIXEIRA CLARISSA ROMERO,
LOPES ROBERVAL OLIVEIRA DE MELO,
CAVADA BENILDO SOUSA
Publication year - 1999
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.1999.tb00037.x
Subject(s) - proteolysis , trypsin , biochemistry , lectin , pepsin , chemistry , enzyme , proteolytic enzymes , cleavage (geology) , peptide , biology , paleontology , fracture (geology)
The enzymatic digestion of the lectins from Canavalia brasiliensis, Dioclea grandiflora and Cratylia floribunda seeds was investigated by heat treatment and gel filtration chromatography. The potential sites of lectin cleavage by pepsin and trypsin was then determined by molecular modelling of the three‐dimensional structure of D.grandiflora lectin. The lectins were shown to be susceptible to proteolytic cleavage using peptide mapping with the FPLC system. However, new peptides arose when hydrolysis was followed by heat treatment at 73C. According to the molecular model of D.grandiflora lectin, there are numerous sites for pepsin and trypsin proteolysis on the surface of the protein. It is suggested that when subjected to enzymatic action, the resulting peptides interact in order to retain the general folding of the protein. This is attributed, at least in part, to the numerous hydrogen bonds and hydrophobic interactions occurring within the inner protein structure. After heat treatment the additional cleavage sites become available and the lectins become completely inactivated .