Amino acid sequenced and biological activities of proteins from Sesnania grandiflora flowers

Abstract

Legume proteins present a lot of nutrition value for human consumption. Some of them are bioactive proteins which can be application to many works. Protein from Sesbnia grandiflora (L.) Desv., leguminous tree, has a few records in databases. Therefore, this research interested to study composition and biological activities of proteins from Sesbnia grandiflora flowers. Crude Proteins from Sesbnia grandiflora flowers were extracted and fractionation precipitated with ammonium sulfate. By using ion exchange and gel filtration chromatography, SGF60 and SGF90 were separated. Both purified proteins shows a-glucosidase inhibitory activity and hemagglutinating activity with rabbit erythrocyte. Approximate molecular weight of SGF60 and SGF90 protein from gel electrophoresis are 40 and 63 kDa, respectively. When analyzed amino acid sequence of these proteins by using ESI-Q/TOF, the result shown that this SGF60 has partial of amino acid sequence similar to p27SJ, a novel protein inhibited HIV-1 from Hypericum perforatum. For SGF90, the amino acid sequences of this protein matched with beta-glucosidase (AJ5G36890) AND BETA-GLUCOSIDASE f8k4.3 PROTEIN FROM Arabidopsis thaliana. Moreover, 2-D gel electrophoresis was used to separate crude protein precipitating with TCA/acetone solution. From this technique, there are at less six proteins in Sesbnia grandiflora flowers.