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- Title
Pre-deamidation of soy protein isolate exerts impacts on transglutaminase-induced glucosamine glycation and cross-linking as well as properties of the products.
- Authors
Yao, Xin‐Tong; Zhao, Xin‐Huai
- Abstract
BACKGROUND Transglutaminase ( TGase) induces protein glycation and cross-linking, but results in lower solubility and digestibility due to excessive cross-linking. Deamidation of soy protein isolate ( SPI) by HCl converts glutamine residues, and provides less opportunity for the two reactions. Two deamidated SPI products ( DSPI1 and DSPI2) were thus glucosamine-glycated and cross-linked, to clarify the effects of pre-deamidation on the two reactions and properties of the products. RESULTS DSPI1 and DSPI2 had respective degrees of deamidation of 12.2% and 27.4%. They and SPI were used to generate three glycated and cross-linked products ( GC-DSPI1, GC-DSPI2 and GC-SPI) containing glucosamine of 12.0, 4.4 and 19.7 g kg−1 protein, respectively, which were reflected in their infrared spectra at two regions. These three (especially GC-SPI) had higher water-binding than SPI (8.2-12.6 versus 6.2 g g−1 protein). GC-DSPI1 and GC-DSPI2 showed better enzymatic digestion than GC-SPI. Thermogravimetric and circular dichroism analyses verified that GC-DSPI1 and GC-DSPI2 had maximum degradation rates at temperatures 12-14 °C lower than GC-SPI, and possessed a more open secondary structure. CONCLUSION SPI deamidation decreases forthcoming glycation and cross-linking, and gives the products higher digestibility, less increased hydration, lower thermal stability, and a more open secondary structure. Pre-deamidation is applicable to control the properties of GC-proteins. © 2015 Society of Chemical Industry
- Subjects
DEAMINATION; SOY proteins; TRANSGLUTAMINASES; GLUCOSAMINE; CROSSLINKING (Polymerization)
- Publication
Journal of the Science of Food & Agriculture, 2016, Vol 96, Issue 7, p2418
- ISSN
0022-5142
- Publication type
Article
- DOI
10.1002/jsfa.7361