Improvements of Modified Wheat Protein Disulfide Isomerases with Chaperone Activity Only on the Processing Quality of Flour

Food and Bioprocess Technology

Volumn 10, Issue 3, 2017, Pages 568-581

  Liu, Guang ^a   Wang, JingJing ^a   Hou, Yi ^a   Huang, Yan Bo ^a   Li, Cun Zhi ^b   Li, Lin ^a   Hu, Song Qing ^a  

^a SOUTH CHINA UNIVERSITY OF TECHNOLOGY   (China)

^b JINAN UNIVERSITY   (China)

Author keywords

Alkylation; Bread quality; Site directed mutagenesis; Wheat flour; Wheat protein; wPDI

Indexed keywords

ALKYLATION; CHEMICAL ANALYSIS; CHROMATOGRAPHY; COVALENT BONDS; ELECTROPHORESIS; ENZYME ACTIVITY; FOOD PRODUCTS; MUTAGENESIS; SCANNING ELECTRON MICROSCOPY; SIZE EXCLUSION CHROMATOGRAPHY; SULFUR COMPOUNDS;

BREAD QUALITY; SITE DIRECTED MUTAGENESIS; WHEAT FLOURS; WHEAT PROTEINS; WPDI;

PROTEINS;

EID: 85001842119     PISSN: 19355130     EISSN: 19355149     Source Type: Journal    
DOI: 10.1007/s11947-016-1840-9     Document Type: Article

References (62)

1. AACC. (2000). Approved methods of the American Association of Cereal Chemists, 11th ed. Method 54–21. The Association: St. Paul, MN.
2. Anders, J. C., Parten, B. F., Petrie, G. E., Marlowe, R. L., & McEntire, J. E. (2003). Using amino acid analysis to determine absorptivity constants. BioPharm International (February), 2, 30–37.
3. Boja, E. S., & Fales, H. M. (2001). Overalkylation of a protein digest with iodoacetamide. Analytical Chemistry, 73(15), 3576–3582.
4. Bonet, A., Rosell, C. M., Caballero, P. A., Gomez, M., Perez-Munuera, I., & Lluch, M. A. (2006). Glucose oxidase effect on dough rheology and bread quality: a study from macroscopic to molecular level. Food Chemistry, 99(2), 408–415.
5. Bueno, M. M., Thys, R. C. S., & Rodrigues, R. C. (2016a). Microbial enzymes as substitutes of chemical additives in baking wheat flour—part I: individual effects of nine enzymes on flour dough rheology. Food and Bioprocess Technology, 1–12.
6. Bueno, M. M., Thys, R. C. S., & Rodrigues, R. C. (2016b). Microbial enzymes as substitutes of chemical additives in baking wheat flour—part II: combined effects of nine enzymes on dough rheology. Food and Bioprocess Technology, 1–14.
7. Bulleid, N. J., & Freedman, R. B. (1988). Defective co-translational formation of disulphide bonds in protein disulphide-isomerase-deficient microsomes. Nature, 335(6191), 649–651.
8. Caballero, P. A., Gomez, M., & Rosell, C. M. (2007). Improvement of dough rheology, bread quality and bread shelf-life by enzymes combination. Journal of Food Engineering, 81(1), 42–53.
9. Cai, H., Wang, C. C., & Tsou, C. L. (1994). Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds. Journal of Biological Chemistry, 269(40), 24550–24552.
10. Colakoglu, A. S., & Özkaya, H. (2012). Potential use of exogenous lipases for DATEM replacement to modify the rheological and thermal properties of wheat flour dough. Journal of Cereal Science, 55(3), 397–404.
11. Every, D., Simmons, L., & Ross, M. (2006). Distribution of redox enzymes in millstreams and relationships to chemical and baking properties of flour. Cereal Chemistry, 83(1), 62–68.
12. Fu, X. M., & Zhu, B. T. (2010). Human pancreas-specific protein disulfide-isomerase (PDIp) can function as a chaperone independently of its enzymatic activity by forming stable complexes with denatured substrate proteins. Biochemical Journal, 429(1), 157–169.
13. Gerrard, J. A. (2002). Protein-protein crosslinking in food: methods, consequences, applications. Trends in Food Science & Technology, 13(12), 391–399.
14. Gibert, S., Bakalara, N., & Santarelli, X. (2000). Three-step chromatographic purification procedure for the production of a His-tag recombinant kinesin overexpressed in E. coli. Journal of Chromatography B: Biomedical Sciences and Applications, 737(1), 143–150.
15. Grynberg, A., Nicolas, J., & Drapron, R. (1977). Presence of a protein disulfide isomerase (EC 5.3. 4.1) in wheat germ. Comptes rendus hebdomadaires des seances de l’Academie des sciences. Serie D: Sciences Naturelles, 284(3), 235–238.
16. Hatahet, F., & Ruddock, L. W. (2009). Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation. Antioxidants & Redox Signaling, 11(11), 2807–2850.
17. Hayano, T., Hirose, M., & Kikuchi, M. (1995). Protein disulfide isomerase mutant lacking its isomerase activity accelerates protein folding in the cell. FEBS Letters, 377(3), 505–511.
18. Horibe, T., Iguchi, D., Masuoka, T., Gomi, M., Kimura, T., & Kikuchi, M. (2004). Replacement of domain b of human protein disulfide isomerase-related protein with domain b of human protein disulfide isomerase dramatically increases its chaperone activity. FEBS Letters, 566(1–3), 311–315.
19. Horton, R. M., Cai, Z., Ho, S. N., & Pease, L. R. (2013). Gene splicing by overlap extension. BioTechniques, 54(3), 528–535.
20. Johnson, J. C., Clarke, B. C., & Bhave, M. (2001). Isolation and characterisation of cDNAs encoding protein disulphide isomerases and cyclophilins in wheat. Journal of Cereal Science, 34(2), 159–171.
21. Joye, I. J., Lagrain, B., & Delcour, J. A. (2009a). Endogenous redox agents and enzymes that affect protein network formation during breadmaking—a review. Journal of Cereal Science, 50(1), 1–10.
22. Joye, I. J., Lagrain, B., & Delcour, J. A. (2009b). Use of chemical redox agents and exogenous enzymes to modify the protein network during breadmaking—a review. Journal of Cereal Science, 50(1), 11–21.
23. Kamata, Y., Ojima, E., Yamaki, M., & Ohtsubo, S. (2014). Increase in the viscosity of soft-flour batter by weak direct-current processing. Food Science and Technology Research, 20(4), 815–819.
24. Karala, A. R., & Ruddock, L. W. (2010). Bacitracin is not a specific inhibitor of protein disulfide isomerase. FEBS Journal, 277(11), 2454–2462.
25. Kim, J. H., Maeda, T., & Morita, N. (2006). Effect of fungal alpha-amylase on the dough properties and bread quality of wheat flour substituted with polished flours. Food Research International, 39(1), 117–126.
26. Kirk, O., Borchert, T. V., & Fuglsang, C. C. (2002). Industrial enzyme applications. Current Opinion in Biotechnology, 13(4), 345–351.
27. Koh, A., Nishimura, K., & Urade, R. (2010). Relationship between endogenous protein disulfide isomerase family proteins and glutenin macropolymer. Journal of Agricultural and Food Chemistry, 58(24), 12970–12975.
28. Kozlov, G., Maattanen, P., Thomas, D. Y., & Gehring, K. (2010). A structural overview of the PDI family of proteins. FEBS Journal, 277(19), 3924–3936.
29. Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227(5259), 680–685.
30. Lee, J. Y., Beom, H. R., Altenbach, S. B., Lim, S. H., Kim, Y. T., Kang, C. S., et al. (2016). Comprehensive identification of LMW-GS genes and their protein products in a common wheat variety. Functional & Integrative Genomics, 16(3), 269–279.
31. Lerner, A., & Matthias, T. (2016). Comment on “Microbial enzymes as substitutes of chemical additives in baking wheat flour—part II: combined effects of nine enzymes on dough rheology [MM Bueno, RCS Thys and RC Rodrigues (2016), Food and bioprocess technology, 9 (9), 1598–1611]”. Food and Bioprocess Technology, 1–2. doi:10.1007/s11947-016-1794-y.
32. Li, Z. J., Deng, C., Li, H. F., Liu, C. H., & Bian, K. (2015). Characteristics of remixed fermentation dough and its influence on the quality of steamed bread. Food Chemistry, 179, 257–262.
33. Liang, R., Zhu, B. Q., Zhang, Y. B., Wang, H. Y., Li, C. Y., Su, Y. H., et al. (2004). The research of applying primer premier 5.0 to design PCR primer. Journal of Jinzhou Medical College, 25(6), 43–46.
34. Lowry, O. H., Rosebrough, N. J., Farr, A. L., & Randall, R. J. (1951). Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry, 193(1), 265–275.
35. Lutz, E., Wieser, H., & Koehler, P. (2012). Identification of disulfide bonds in wheat gluten proteins by means of mass spectrometry/electron transfer dissociation. Journal of Agricultural and Food Chemistry, 60(14), 3708–3716.
36. Miralbés, C. (2004). Quality control in the milling industry using near infrared transmittance spectroscopy. Food Chemistry, 88(4), 621–628.
37. Miś, A., Grundas, S., Dziki, D., & Laskowski, J. (2012). Use of farinograph measurements for predicting extensograph traits of bread dough enriched with carob fibre and oat wholemeal. Journal of Food Engineering, 108(1), 1–12.
38. NØrgaard, P., & Winther, J. R. (2001). Mutation of yeast Eug1p CXXS active sites to CXXC results in a dramatic increase in protein disulphide isomerase activity. Biochemistry Journal, 358, 269–274.
39. Osborn, S. (2014). Labelling relating to natural ingredients and additives. Advances in Food and Beverage Labelling: Information and Regulations, 207.
40. Pirneskoski, A., Klappa, P., Lobell, M., Williamson, R. A., Byrne, L., Alanen, H. I., et al. (2004). Molecular characterization of the principal substrate binding site of the ubiquitous folding catalyst protein disulfide isomerase. Journal of Biological Chemistry, 279(11), 10374–10381.
41. Pongjaruvat, W., Methacanon, P., Seetapan, N., Fuongfuchat, A., & Gamonpilas, C. (2014). Influence of pregelatinised tapioca starch and transglutaminase on dough rheology and quality of gluten-free jasmine rice breads. Food Hydrocolloids, 36, 143–150.
42. Quan, H., Fan, G., & Wang, C. C. (1995). Independence of the chaperone activity of protein disulfide isomerase from its thioredoxin-like active site. Journal of Biological Chemistry, 270(29), 17078–17080.
43. Roccia, P., Ribotta, P. D., Ferrero, C., Pérez, G. T., & León, A. E. (2012). Enzymes action on wheat–soy dough properties and bread quality. Food and Bioprocess Technology, 5(4), 1255–1264.
44. Schwaller, M., Wilkinson, B., & Gilbert, H. F. (2003). Reduction-reoxidation cycles contribute to catalysis of disulfide isomerization by protein-disulfide isomerase. Journal of Biological Chemistry, 278(9), 7154–7159.
45. Simonian, M. H., & Smith, J. A. (2006). Spectrophotometric and colorimetric determination of protein concentration. Current Protocols in Molecular Biology, 10–11.
46. Song, J. L., Quan, H., & Wang, C. C. (1997). Dependence of the anti-chaperone activity of protein disulphide isomerase on its chaperone activity. Biochemical Journal, 328, 841–846.
47. Steffolani, M. E., Ribotta, P. D., Pérez, G. T., & León, A. E. (2010). Effect of glucose oxidase, transglutaminase, and pentosanase on wheat proteins: relationship with dough properties and bread-making quality. Journal of Cereal Science, 51(3), 366–373.
48. Sudha, M., Vetrimani, R., & Leelavathi, K. (2007). Influence of fibre from different cereals on the rheological characteristics of wheat flour dough and on biscuit quality. Food Chemistry, 100(4), 1365–1370.
49. Sun, X. X., Dai, Y., Liu, H. P., Chen, S. M., & Wang, C. C. (2000). Contributions of protein disulfide isomerase domains to its chaperone activity. Biochimica et Biophysica Acta, 1481(1), 45–54.
50. Tian, R., Li, S. J., Wang, D. L., Zhao, Z., Liu, Y., & He, R. Q. (2004). The acidic C-terminal domain stabilizes the chaperone function of protein disulfide isomerase. Journal of Biological Chemistry, 279(47), 48830–48835.
51. Tian, G., Xiang, S., Noiva, R., Lennarz, W. J., & Schindelin, H. (2006). The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites. Cell, 124(1), 61–73.
52. Tosi, P. (2012). Trafficking and deposition of prolamins in wheat. Journal of Cereal Science, 56(1), 81–90.
53. Walker, K. W., Lyles, M. M., & Gilbert, H. F. (1996). Catalysis of oxidative protein folding by mutants of protein disulfide isomerase with a single active site cysteine. Biochemistry, 35(6), 1972–1980.
54. Wang, L., Wang, X., & Wang, C. C. (2015a). Protein disulfide-isomerase, a folding catalyst and a redox-regulated chaperone. Free Radical Biology and Medicine, 83, 305–313.
55. Wang, Q., Li, Y., Sun, F. S., Li, X. Y., Wang, P. D., Sun, J. T., et al. (2015b). Tannins improve dough mixing properties through affecting physicochemical and structural properties of wheat gluten proteins. Food Research International, 69, 64–71.
56. Wang, X. Y., Guo, X. N., & Zhu, K. X. (2016). Polymerization of wheat gluten and the changes of glutenin macropolymer (GMP) during the production of Chinese steamed bread. Food Chemistry, 201, 275–283.
57. Watanabe, E., Bell, A. E., & Brockway, B. E. (1998). The effect of protein disulphide isomerase on dough rheology assessed by fundamental and empirical testing. Food Chemistry, 61(4), 481–486.
58. Wilkinson, B., & Gilbert, H. F. (2004). Protein disulfide isomerase. Biochimica et Biophysica Acta, 1699(1–2), 35–44.
59. Yao, Y., Zhou, Y. C., & Wang, C. C. (1997). Both the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A2. The EMBO Journal, 16(3), 651–658.
60. Zhang, C., Zhang, S., Lu, Z. X., Bie, X. M., Zhao, H. Z., Wang, X. M., et al. (2013). Effects of recombinant lipoxygenase on wheat flour, dough and bread properties. Food Research International, 54(1), 26–32.
61. Zhang, Y., Zhang, H., Ding, X., Cheng, L., Wang, L., Qian, H., et al. (2016). Purification and identification of antifreeze protein from cold-acclimated oat (Avena sativa L.) and the cryoprotective activities in ice cream. Food and Bioprocess Technology, 9, 1–10.
62. Zhu, J., Hao, P., Chen, G., Han, C., Li, X., Zeller, F. J., et al. (2014). Molecular cloning, phylogenetic analysis, and expression profiling of endoplasmic reticulum molecular chaperone BiP genes from bread wheat (Triticum aestivum L.). BMC Plant Biology, 14, –260.