Improving the freeze-thaw stability of soy protein emulsions via combing limited hydrolysis and Maillard-induced glycation

Improving the freeze-thaw stability of soy protein emulsions via combing limited hydrolysis and... The investigation of limited hydrolysis combined with Maillard-induced glycation on improving the freeze-thaw stability of soy protein isolate (SPI) was carried out. Soy protein isolate hydrolysate (SPH) was first prepared by trypsin, with a hydrolysis degree of 2% and 5%. Afterwards, SPI and SPH were conjugated with dextran to form a covalent complex macromolecule, which were named SPI-D, SPH2-D and SPH5-D, respectively. Covalent bond was formed between SPI/SPH and dextran molecules via the glycation reaction has been confirmed by fourier transform infrared (FTIR) spectroscopy analysis. Subsequently, the freeze-thaw stability of SPI-D and SPH-D was evaluated. After three freeze-thaw cycles, the characters of SPH-D emulsions exhibited smaller values than those of SPI-D emulsions in terms of oiling off, particle size, flocculation degree (FD) and coalescence degree (CD). In addition, SPH2-D emulsions were more stable after freeze-thaw treatment compared with SPH5-D emulsions. Optical microscopy analysis also supported the results above. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png LWT - Food Science and Technology Elsevier

Improving the freeze-thaw stability of soy protein emulsions via combing limited hydrolysis and Maillard-induced glycation

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Publisher
Elsevier
Copyright
Copyright © 2018 Elsevier Ltd
ISSN
0023-6438
D.O.I.
10.1016/j.lwt.2018.01.031
Publisher site
See Article on Publisher Site

Abstract

The investigation of limited hydrolysis combined with Maillard-induced glycation on improving the freeze-thaw stability of soy protein isolate (SPI) was carried out. Soy protein isolate hydrolysate (SPH) was first prepared by trypsin, with a hydrolysis degree of 2% and 5%. Afterwards, SPI and SPH were conjugated with dextran to form a covalent complex macromolecule, which were named SPI-D, SPH2-D and SPH5-D, respectively. Covalent bond was formed between SPI/SPH and dextran molecules via the glycation reaction has been confirmed by fourier transform infrared (FTIR) spectroscopy analysis. Subsequently, the freeze-thaw stability of SPI-D and SPH-D was evaluated. After three freeze-thaw cycles, the characters of SPH-D emulsions exhibited smaller values than those of SPI-D emulsions in terms of oiling off, particle size, flocculation degree (FD) and coalescence degree (CD). In addition, SPH2-D emulsions were more stable after freeze-thaw treatment compared with SPH5-D emulsions. Optical microscopy analysis also supported the results above.

Journal

LWT - Food Science and TechnologyElsevier

Published: May 1, 2018

References

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