Spectroscopic analysis of the effect of vitamin B12-soy protein isolate on the soy protein isolate structure

In this paper, the influence of the interaction between vitamin B-12 and soybean protein isolate (SPI) on the structure of the SPI was studied by Fourier transform infrared (ITIR), Circular dichroism (CD), and Raman spectra. The results of the FTIR and CD spectra show that when the concentration of vitamin B-12 combined with the SPI increases, the beta-sheet and irregular curl in the SPI will gradually change into an alpha-helix and beta-tum structure, making the structure of SPI more orderly. In addition, the conformation of amide, the vibrational modes of side-chain amino acids and disulfide bonds, and the vibrational modes of aliphatic C-H bonds of SPI were analyzed by Raman spectroscopy. The results showed that the interaction between SPI and vitamin B-12 increased with the increase in the concentration of vitamin B-12. At the same lime, aggregates were formed between the complexes, which made the structure of the SPI tend to be orderly. This paper provides a basis for the study of vitamin B-12 in improving the structure and function of protein. and also provides a theoretical basis for the further study of the interaction between vitamin B-12 and protein. (C) 2020 Elsevier B.V. All rights reserved.

Automated summary

The influence of the interaction between vitamin B-12 and soybean protein isolate (SPI) on the structure of SPI was studied. The results show that as the concentration of vitamin B-12 combined with SPI increases, the structure becomes more orderly. Raman spectroscopy analysis also indicates an increase in interaction between SPI and vitamin B-12 with higher concentration of the vitamin.