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Protein Engineering vol. 3 no. 8 pp. 725-731, 1990
© 1990 Oxford University Press

RESEARCH-ARTICLE

Improvement of nutritional value and functional properties of soybean glycinin by protein engineering

Chan-Shick Kim, Seigo Kamiya, Toshiro Sato, Shigeru Utsumi1 and Makoto Kito

The Research Institute for Food Services, Kyoto University Uji, Kyoto 611, Japan

1To whom correspondence should be addressed

Glycinin is one of the predominant storage proteins of soybean. To improve its functional properties (heat-induced gelation and emulsification) and/or nutritional value, the A1aB1b proglycinin subunit was modified on the basis of genetically variable domains suggested from the comparison of amino acid sequences of glycinin-type globulins from various legumes and nonlegumes and the relationships between the structure and the functional properties of glycinin. Thus, nucleotide sequences corresponding to each of the variable domains were deleted from the cDN A encoding the A1aB1b proglycinin, and a synthetic DNA encoding four continuous methionines was inserted into the cDNA region corresponding to each of the variable domains. Expression plasmids carrying the modified cDNAs were constructed and expressed in Escherichia coli strain JM105. Some of the modified proteins were accumulated as soluble proteins in the cells at a high level and self-assembled. They exhibited functional properties superior to those of the native glycinin from soybean, which establishes the possibility of creating theoretically designed novel glycinins with high food qualities.

Keywords: food functionality/glycinin subunit precursor/nutritional value/proglycinin/soybean storage protein

Received February 2, 1990; accepted April 22, 1990.


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