Abstract：
:An Acacia victoriae trypsin inhibitor (AvTI) was purified from the seeds of prickly wattle (A. victoriae Bentham) by salt precipitation, ion-exchange and gel filtration chromatography, and its degree of glycosylation, amino acid composition, and kinetic properties were determined. Gel electrophoresis revealed at least four glycoprotein bands in the crude extract, salt-precipitated and ion-exchange protein fractions, while the purified AvTI showed only one band and a degree of glycosylation of 2.06%. Glutamate (13.3%), aspartate (10.3%), leucine (7.62%) and lysine (7.01%) were the major amino acids in AvTI while the contents of sulphur-containing amino acids, cysteine (1.38%) and methionine (0.75%), as well as of tryptophan (1.17%) were low. Its dissociation constant (Ki) for the inhibition of bovine trypsin was found to be 1.06×10(-8)M, indicating a high affinity between AvTI and this enzyme, and its role as a competitive inhibitor was confirmed by a double reciprocal plot. These results complement our earlier studies which indicated the presence of three isoforms of this Kunitz-type trypsin inhibitor in prickly wattle seed.
journal_name
Food Chemjournal_title
Food chemistryauthors
Ee KY,Zhao J,Rehman A,Agboola Sdoi
10.1016/j.foodchem.2011.05.026subject
Has Abstractpub_date
2011-12-01 00:00:00pages
1224-7issue
3eissn
0308-8146issn
1873-7072pii
S0308-8146(11)00715-1journal_volume
129pub_type
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