Improving Surface Functional Properties of Tofu Whey-Derived Peptides by Chemical Modification with Fatty Acids
Article first published online: 19 MAR 2012
© 2012 Institute of Food Technologists®
Journal of Food Science
Volume 77, Issue 4, pages C333–C339, April 2012
How to Cite
Matemu, A. O., Katayama, S., Kayahara, H., Murasawa, H. and Nakamura, S. (2012), Improving Surface Functional Properties of Tofu Whey-Derived Peptides by Chemical Modification with Fatty Acids. Journal of Food Science, 77: C333–C339. doi: 10.1111/j.1750-3841.2012.02631.x
- Issue published online: 19 APR 2012
- Article first published online: 19 MAR 2012
- MS 20101255 Submitted 11/4/2010, Accepted 1/12/2012.
- emulsifying properties;
- fluorescence intensity;
- Protease M ‘Amano’ G;
- tofu whey
Abstract: Effect of acylation with saturated fatty acids on surface functional properties of tofu whey-derived peptides was investigated. Tofu whey (TW) and soy proteins (7S, 11S, and acid-precipitated soy protein [APP]) were hydrolyzed by Protease M ‘Amano’ G, and resulting peptide mixtures were acylated with esterified fatty acids of different chain length (6C to 18C) to form a covalent linkage between the carboxyl group of fatty acid and the free amino groups of peptide. Acylation significantly (P < 0.05) increased emulsifying properties of 7S, 11S, and APP peptides independent of fatty acid chain length. Acylation decreased water binding capacity although oil binding capacity of acylated tofu whey ultra filtered fraction (UFTW < 3 kDa), 7S- and 11S-peptides were improved compared to native peptides. 7S peptides acylated with long chain fatty acids had shown significant higher surface hydrophobicity as in contrast with acylated UFTW < 3 kDa and APP peptides. Fluorescence spectra studies revealed structural conformation of acylated soy peptides as compared to native peptides. This study shows that chemical modification with fatty acids can further affect functional properties of soy proteins.