Evaluation of the Solubility and Emulsifying Property of Soybean Proglycinin and Rapeseed Procruciferin in Relation to Structure Modified by Protein Engineering

The presence or absence of a highly negatively charged extension region in β-conglycinin (J. Agric. Food Chem. 1999, 47, 5278) and the length of a highly negatively charged variable region IV in glycinin (J. Agric. Food Chem. 2004, 52, 8197) are important determinants of solubility and emulsifying p...

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Published in:Journal of agricultural and food chemistry 2005-11, Vol.53 (22), p.8736-8744
Main Authors: Tandang, Mary Rose G, Atsuta, Nami, Maruyama, Nobuyuki, Adachi, Motoyasu, Utsumi, Shigeru
Format: Article
Language:English
Subjects:
Antigens, Plant
Biological and medical sciences
Brassica rapa - chemistry
emulsifiers
emulsifying
Emulsifying Agents
Escherichia coli
Food industries
Fruit and vegetable industries
Fundamental and applied biological sciences. Psychology
gene expression
Globulins - chemistry
Globulins - genetics
Glycine max - chemistry
glycinin
mutants
Mutation
plant proteins
Plant Proteins - chemistry
Plant Proteins - genetics
procruciferin
proglycinin
Protein Engineering
protein secondary structure
rapeseed
recombinant proteins
Seed Storage Proteins
Solubility
Soybean Proteins - chemistry
Soybean Proteins - genetics
soybeans
Structure-Activity Relationship
Transfection
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Summary:The presence or absence of a highly negatively charged extension region in β-conglycinin (J. Agric. Food Chem. 1999, 47, 5278) and the length of a highly negatively charged variable region IV in glycinin (J. Agric. Food Chem. 2004, 52, 8197) are important determinants of solubility and emulsifying property. To examine the effects of the variable region IV from proglycinin A1aB1b and A3B4 and of the extension region from β-conglycinin α‘ (α‘ext) on solubility and emulsifying properties in detail, several mutants of proglycinin, procruciferin, and β-conglycinin were designed and prepared in Escherichia coli. Nine out of 10 mutants were expressed at high levels in E. coli and shown to be homotrimer similar to the wild types as assessed by gel filtration. The position of the introduced negatively charged region as well as the amino acid composition were demonstrated to affect solubility at μ = 0.08. All of the proglycinin, procruciferin, and β-conglycinin mutants with the α‘ext in the C-terminus, especially the proglycinin mutant, exhibited excellent emulsifying ability and emulsion stability. These indicate that improvement of emulsifying properties by insertion of the α‘ext in the C-terminus may be generally applicable to seed globulins. Keywords: Emulsion; rapeseed; procruciferin; proglycinin; protein engineering; solubility; soybean
ISSN:0021-8561
1520-5118
DOI:10.1021/jf050871y