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Leghemoglobin C2 is a protein found in soybean nodules, and it is one of the three major forms of leghemoglobin present in these nodules, alongside leghemoglobin a and cl [1]. The amino acid differences between leghemoglobin a and leghemoglobin c2 of soybean indicate that they are likely encoded by independent genes, but they possess highly similar tertiary structures [2]. This suggests that despite being encoded by different genes, these proteins share structural similarities.
The safety of using recombinant soy leghemoglobin in food has been investigated, and it has been reported that there are no potential allergenicity and toxigenicity associated with its use [3]. This conclusion was drawn from a literature search, bioinformatics analyses on the amino acid sequence of leghemoglobin and 17 Pichia host proteins, as well as in vitro pepsin digestibility of leghemoglobin. This indicates that leghemoglobin C2, as a form of soy leghemoglobin, is considered safe for consumption.
Furthermore, leghemoglobin uses an iron cofactor, and it has been speculated that a decrease in nodule GmSACPD-C iron binding may lead to an increase in leghemoglobin iron binding and expression [4]. This suggests that the regulation of iron binding may impact the expression and function of leghemoglobin C2 in soybean nodules.
References:
[1] E. Truelsen, K. Gausing, B. Jochimsen, P. Jørgensen, & K. Marcker, "Cloning of soybean leghemoglobin structural gene sequences synthesized in vitro", Nucleic Acids Research, vol. 6, no. 9, p. 3061-3072, 1979. https://doi.org/10.1093/nar/6.9.3061
[2] W. Brill, "Biochemical genetics of nitrogen fixation.", Microbiological Reviews, vol. 44, no. 3, p. 449-467, 1980. https://doi.org/10.1128/mmbr.44.3.449-467.1980
[3] J. Hadi and G. Brightwell, "Safety of alternative proteins: technological, environmental and regulatory aspects of cultured meat, plant-based meat, insect protein and single-cell protein", Foods, vol. 10, no. 6, p. 1226, 2021. https://doi.org/10.3390/foods10061226
[4] N. Lakhssassi, V. Colantonio, N. Flowers, Z. Zhou, J. Henry, S. Liuet al., "Stearoyl-acyl carrier protein desaturase mutations uncover an impact of stearic acid in leaf and nodule structure", Plant Physiology, vol. 174, no. 3, p. 1531-1543, 2017. https://doi.org/10.1104/pp.16.01929
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