Effect of High Pressure Microfluidization on Secondary Structure of Wheat Gluten in Different Solvents

Article Preview

Abstract:

Far-UV circular dichroism (CD) spectroscopy was used to study the conformation of wheat gluten protein treatmented by dynamic high pressure microfluidization (DHPM), acid treatment and its comprehensive treatment in two solvents. The results showed, the secondary structure of control sample are mainly consist of α-helix and random-coil in phosphate-buffered saline (PBS) and phosphate buffered solution with SDS(SDS), the secondary structure of control sample are mainly consist of β-Sheet and random-coil. The CD data also showed that SDS interacts with the gluten protein and modifies the protein conformation, which switched the conformation from α-helix and β-Turn to β-sheet and random-coil. However, the CD analysis also indicated that some of the ordered structures of α-helix, β-Turn and β-sheet were destroyed and converted random-coil coped with acid in two solvents, in other words, the acid treatment can directed change the secondary structure. Furthermore, the effect of comprehensive treatment (DHPM plus acid) is not equal to the simple sum of the individual treatment effect.

You might also be interested in these eBooks

Info:

Periodical:

Advanced Materials Research (Volumes 781-784)

Pages:

770-773

Citation:

Online since:

September 2013

Export:

Price:

Permissions CCC:

Permissions PLS:

Сopyright:

© 2013 Trans Tech Publications Ltd. All Rights Reserved

Share:

Citation:

* - Corresponding Author

[1] Liao, L., Liu, T. X., Zhao, M. M., Cui, C., Yuan, B. E., Tang, S., & Yang, F. Functional, nutritional and conformational changes from deamidation of wheat gluten with succinic acid and citric acid. Food Chemistry, 123(1), 123-130. (2010).

DOI: 10.1016/j.foodchem.2010.04.017

Google Scholar

[2] Shen, L., & Tang, C. H. Microfluidization as a potential technique to modify surface properties of soy protein isolate. Food Research International, 48(1), 108-118. (2012).

DOI: 10.1016/j.foodres.2012.03.006

Google Scholar

[3] Huang, K. L., Yin, S. W., & Yang, X. Q. Effect of Micro-fluidization Treatment on Conformational and Functional Properties of Red Bean (Phaseolus angularis) Protein Isolates. Modern Food Science and Technology (In Chinese), 27(9), 1062-1065. (2011).

Google Scholar

[4] Oboroceanu, D., Wang, L., Kroes-Nijboer, A., Brodkorb, A., Venema, P., Magner, E., & Auty, M. A. The effect of high pressure microfluidization on the structure and length distribution of whey protein fibrils. International Dairy Journal, 21(10), 823-830. (2011).

DOI: 10.1016/j.idairyj.2011.03.015

Google Scholar

[5] Petruccelli, S., & Añón, M. C. pH-induced modifications in the thermal stability of soybean protein isolates. Journal of agricultural and food chemistry, 44(10), 3005-3009. (1996).

DOI: 10.1021/jf9600061

Google Scholar

[6] Lakemond, C. M., de Jongh, H. H., Hessing, M., Gruppen, H., & Voragen, A. G. Heat denaturation of soy glycinin: influence of pH and ionic strength on molecular structure. Journal of agricultural and food chemistry, 48(6), 1991-1995. (2000).

DOI: 10.1021/jf9908704

Google Scholar

[7] A. Torbica, M. Antov, J. Mastilović, D. Knežević. The influence of changes in gluten complex structure on technological quality of wheat (Triticum aestivum L. ). Food Research International, 40, 1038–1045. (2007).

DOI: 10.1016/j.foodres.2007.05.009

Google Scholar

[8] Liu, G. Q., Yan, N.J., Zhao L., etc. Effect of Frozen Storage on the Secondary Structure of Wheat Gluten. Journal of South China University of Technology (Natural Science Edition), 5, 115-120. (2012).

Google Scholar

[9] A.M. Andrade, P. Chacon, J.J. Merelo, F. Moran, Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised leaning neural network, Protein Eng. 6 (1993) 383–390.

DOI: 10.1093/protein/6.4.383

Google Scholar

[10] L. Whitmore, B.A. Wallace. DICHROWEB, an online server for protein secondary structure analyses from circular dichroism data, Nucleic Acids Res. 32 (1994) W668–W673.

DOI: 10.1093/nar/gkh371

Google Scholar

[11] Kwaambwa, H. M., and R. Maikokera. Infrared and circular dichroism spectroscopic characterisation of secondary structure components of a water treatment coagulant protein extracted from< i> Moringa oleifera</i> seeds., Colloids and Surfaces B: Biointerfaces 64. 1 (2008).

DOI: 10.1016/j.colsurfb.2008.01.014

Google Scholar