Journal
CYTA-JOURNAL OF FOOD
Volume 14, Issue 1, Pages 138-144Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1080/19476337.2015.1067646
Keywords
soybean protein isolate; degraded chitosan; transglutaminase; secondary structure; property
Categories
Funding
- National High Technology Research and Development Program (863 Program) of China [2013AA102205]
- Specialized Research Fund for the Doctoral Program of Higher Education [20132325130001]
- Innovation Foundation for Postgraduate of Northeast Agricultural University [YJSCX14062]
Ask authors/readers for more resources
A glycated and cross-linked soybean protein isolate (GC-SPI) with the glucosamine content of 19.40g/kg protein was prepared by using SPI, transglutaminase, and a degraded chitosan under fixed conditions, aiming to assess modified properties and potential application of GC-SPI. GC-SPI has less reactable -NH2 groups than SPI (0.38 versus 0.48mol/kg protein), and is verified by electrophoretic analysis to be a glycated and cross-linked protein product. Infrared spectroscopy and circular dichroism analyses demonstrate that GC-SPI contains more -OH groups, and has a more open secondary structure. In comparison with SPI, GC-SPI has higher surface hydrophobicity but lower in vitro digestibility due to protein cross-linking, and exhibits greater water- and oil-binding capacities (9.9 versus 6.4 and 3.7 versus 2.0kg/kg protein). It is concluded that the glycation and cross-linking confer an open structure and modified properties of SPI, and GC-SPI is a potential ingredient with better hydration and oil-binding than SPI.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available