Sokoine University of Agriculture

Molecular improvement of food functional properties of Soybean glycinin by protein engineering

Show simple item record Gidamis, A. B. Nnko, S. A. Bunzo, M. Utsumi, S. Kito, M. 2017-12-06T16:31:29Z 2017-12-06T16:31:29Z 1998
dc.description Tanzania Journal of Agriculture Science 1998. Vol 1(1): pp 50-56 en_US
dc.description.abstract A study was made to elucidate the three dimensional structure of soybean glydnin which is one of the dominant storage proteins of soybean seeds. Previously, the twodisulphide bonds Cys12-Cys45 and Cys88-Cys298 in the proglydnin AlaBlb subunit were deleted andCys residues were replaced by Gly and Ser by Oligonucleotide-directed mutagenesis. The mutant proglycinins Gly12, and Ser88 showed to have better gelation and emulsifying properties. The mutant proglydnins were crystallised along with the normal proglycinin (AlaBlb -3) and subjected to X-ray structure analysis in an attempt to determine their structure-junction relationships. The crystals diffracted X-ray to a resollttion limit of 2.9 - 3.4A on stillphotographs and belongto the tetragonal system, space group P41 or P43 with cell dimensions of a = b·= 114.3 - 115.2A. and d;= 145.7 - 147.1A with 3 protomers per asymmetric unit. Further refinement data for the' crystals of normal prpglycinin were obtained by multiple isomorphous replacement and solvent flattening techniques. The tri1?ler dimensions of tlie normal proglydnin as determined at 6A were 93A by 93A with·the thickness of 36A. en_US
dc.language.iso en en_US
dc.publisher Tanzania Journal of Agricultural Sciences en_US
dc.subject Crystallisation en_US
dc.subject Proglycinin en_US
dc.subject Protein Engineering en_US
dc.subject Soybean gfycinin en_US
dc.subject X-ray Crystallography en_US
dc.title Molecular improvement of food functional properties of Soybean glycinin by protein engineering en_US
dc.type Article en_US

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