The effect of salinity on the conformation of proteins of four salt-tolerant M2 generation mutants of soybean plants (S04-05/150-2, S04-05/150-8, S04-05/150-106, and S04-05/150-114) was investigated using Fourier transform infrared (FTIR) spectroscopy. Salinity is one of the important abiotic stress factors that limits growth and productivity of plants. The mutants belonging to the M2 generation were determined as tolerant to 90 mM NaCl. The relative contents of α-helix, β-sheet, turn, and irregular conformations for the soybean protein isolates were determined depending on the analysis of the amide I region. The comparison of the secondary structures of soybean proteins of the mutants with those of the control group indicated that the α-helix structure percentage was diminished while β-turn and disordered structures were increased as a result of the salt stress.
Article PDF
Similar content being viewed by others
Avoid common mistakes on your manuscript.
References
C. Wang, L. Jiang, D. Wei, Y. Li, X. Sui, Z. Wang, and D. Li, Procedia Eng., 15, 4819–4827 (2011).
M. Ortbauer, in: Abiotic Stress — Plant Responses and Applications in Agriculture, Eds. K. Vahdati, C. Leslie, INTECH Open Access Publisher, 3–23 (2013); https://doi.org/10.5772/53129.
C. Atak, S. Alikamanoglu, L. Acik, and Y. Canbolat, Mutat. Res., 556, 35–44 (2004).
O. Celik and C. Atak, Pol. J. Environ. Stud., 21, 559–564 (2012).
O. Celik, S. G. Unsal, Plant Omics J., 6, No. 5, 364–370 (2013).
S. Akyuz, T. Akyuz, O. Celik, and C. Atak, J. Mol. Struct., 1044, 67–71 (2013).
K. Kong-ngern, S. Daduang, C. Wongkham, S. Bunnag, M. Kosittrakun, and P. Theerakulpisut, Sci. Asia, 31, 403–408 (2005)
S. Akyuz, T. Akyuz, O. Celik, and C. Atak, Development of Salt Tolerant Soybean Mutants via Mutation Breeding (2010): Unpublished Data.
M. M. Bradford, Anal. Biochem., 72, 248–254 (1976).
E. Goormaghtigh, V. Cabiaux, and J.-M. Ruysschaert, in: Subcellular Biochemistry, 23, Eds. H. J. Hilderson, G. B. Ralston, Springer Science, New York, 329–362, 405–450 (1994).
A. Barth and C. Zscherp, Q. Rev. Biophys., 35, 369–430 (2002).
M. S. Braiman and K. J. Rothschild, Annu. Rev. Biophys. Biophys. Chem., 17, 541–570 (1988).
D. M. Byler and H. Susi, Biopolymers, 25, 469–487 (1986).
Y. El Khoury, R. Hielscher, M. Voicescu, J. Gross, and P. Hellwig, Vib. Spectrosc., 55, 258–266 (2011).
H. H. de Jongh, E. Goormaghtigh, and J. M. Ruysschaert, Anal. Biochem., 242, 95–103 (1996).
Y. N. Chirgadze and E. V. Brazhnikov, Biopolymers, 13, 1701–1712 (1974).
Y. N. Chirgadze, B. V. Shestopalov, and S. Yu. Venyaminov, Biopolymers, 12, 1337–1351 (1973).
S. Yu. Venyaminov and N. N. Kalnin, Biopolymers, 30, 1259–1271 (1990).
G. Vedantham, H. G. Sparks, S. U. Sane, S. Tzannis, and T. M. Przybycien, Anal. Biochem., 285, 33–49 (2000).
Author information
Authors and Affiliations
Corresponding author
Additional information
Published in Zhurnal Prikladnoi Spektroskopii, Vol. 84, No. 6, pp. 942–946, November–December, 2017.
Rights and permissions
About this article
Cite this article
Akyuz, S., Akyuz, T., Celik, O. et al. FTIR Spectroscopy of Protein Isolates of Salt-Tolerant Soybean Mutants. J Appl Spectrosc 84, 1019–1023 (2018). https://doi.org/10.1007/s10812-018-0580-1
Received:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s10812-018-0580-1