Raman spectroscopy analysis of the effect of electrolysis treatment on the structure of soy protein isolate
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ORIGINAL PAPER
Raman spectroscopy analysis of the effect of electrolysis treatment on the structure of soy protein isolate Dianyu Yu1 · Xin Zhang1 · Wenrong Zou1 · Honglin Tang1 · Fuming Yang1 · Liqi Wang2 · Walid Elfalleh3 Received: 28 April 2020 / Accepted: 18 October 2020 © Springer Science+Business Media, LLC, part of Springer Nature 2020
Abstract The effect of electrolysis on soy protein isolate (SPI) was studied by Raman spectroscopy and ultraviolet spectroscopy. The results showed that with the prolongation of electrolysis time, the α-helix content decreased first and then increased. Trp and Tyr residues tended to be exposed from their original embedded state, while electrolysis gradually shifted the SPI disulfide bond from the g–g–g configuration to g–g–t and t–g–t configuration. Therefore, the electrolysis treatment influences the SPI disulfide bond, resulting in intermolecular disulfide bond. Raman spectra showed the secondary and tertiary structure changes of SP and revealed that the structure of SPI would be affected by electrolysis. And the results of UV scanning spectrum confirm the above conclusions. Keywords Electrolysis · Soy protein isolate (SPI) · Raman spectroscopy
Introduction Soy protein is one of the main nutritional ingredients of soybean and one of the world’s high-quality plant proteins [1, 2]. Its content exceeds the dry basis of soybeans and contains essential amino acids required by the human body. It is an ideal edible protein resource because of its balanced composition. Depending on the sedimentation coefficient, soy protein isolate (SPI) is mainly composed of 2S, 7S, 11S and 15S (differentiated according to the centrifugal sedimentation index). Among them, 7S and 11S globulins account for about 70% of the total weight of SPI, which play a leading role in the functional properties of SPI [3]. Protein modification refers to the means of enhancing or * Dianyu Yu [email protected] * Walid Elfalleh [email protected] 1
School of Food Science, Northeast Agricultural University, Harbin 150030, China
2
School of Computer and Information Engineering, Harbin University of Commerce, Harbin 150028, Heilongjiang, China
3
Laboratoire Energie, Eau, Environnement et Procèdes, (LEEEP) LR18ES35, Ecole Nationale d’Ingénieurs de Gabès, Université de Gabès, 6072 Gabès, Tunisia
improving the functional properties of proteins, inhibiting the activity of enzymes, or removing harmful substances by changing one or several physical and chemical properties of proteins, thereby achieving the purpose of removing odor and improving nutrient utilization. At present, the main research focuses on modification techniques such as physical methods, chemical methods, enzymatic methods and genetic engineering methods [4, 5]. The functional properties of SPI can be broadly classified into surface properties, hydration properties, and properties associated with protein interactions. The surface properties of SPI mainly refer to emulsification, oil absorbing and foaming properties, and the hydratio
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