An improved process for the production of highly purified recombinant thaumatin tagged-variants

Food Chemistry

Volumn 237, Issue , 2017, Pages 825-832

  Healey, Robert D ^a   Lebhar, Helene ^b   Hornung, Simon ^b   Thordarson, Pall ^a   Marquis, Christopher P ^b  

^a UNIVERSITY OF NEW SOUTH WALES   (Australia)

^b UNIVERSITY OF NEW SOUTH WALES   (Australia)

Author keywords

Fermentation; GPCR; Pichia pastoris; Protein disulfide isomerase; Sweet tasting protein; Sweetener; Thaumatin

Indexed keywords

AMINO ACIDS; BEVERAGES; CHROMATOGRAPHY; DICHROISM; FERMENTATION; FLUORESCENCE SPECTROSCOPY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; PROTEINS; PURIFICATION; SUGAR INDUSTRY; SUGAR SUBSTITUTES; YEAST;

GPCR; PICHIA PASTORIS; PROTEIN DISULFIDE ISOMERASES; SWEETENER; THAUMATIN;

SIZE EXCLUSION CHROMATOGRAPHY;

CHAPERONE; THAUMATIN; PLANT PROTEIN; SWEETENING AGENT; THAUMATIN PROTEIN, PLANT;

ARTICLE; CIRCULAR DICHROISM; FLUORESCENCE SPECTROSCOPY; KOMAGATAELLA PASTORIS; LIQUID CHROMATOGRAPHY-MASS SPECTROMETRY; PURIFICATION; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; SIZE EXCLUSION CHROMATOGRAPHY; CHEMISTRY; MARANTACEAE; PICHIA; TANDEM MASS SPECTROMETRY;

MARANTACEAE; PICHIA; PLANT PROTEINS; SWEETENING AGENTS; TANDEM MASS SPECTROMETRY;

EID: 85020450551     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2017.06.018     Document Type: Article

References (32)

1. Asherie, N., Ginsberg, C., Greenbaum, A., Blass, S., Knafo, S., Effects of protein purity and precipitant stereochemistry on the crystallization of thaumatin. Crystal Growth & Design 8:12 (2008), 4200–4207.
2. Chiu, J., March, P.E., Lee, R., Tillett, D., Site-directed, Ligase-Independent Mutagenesis (SLIM): A single-tube methodology approaching 100% efficiency in 4 h. Nucleic Acids Research, 32(21), 2004, e174.
3. Chiu, J., Tillett, D., Dawes, I.W., March, P.E., Site-directed, Ligase-Independent Mutagenesis (SLIM) for highly efficient mutagenesis of plasmids greater than 8kb. Journal of Microbiological Methods 73:2 (2008), 195–198.
4. Faus, I., Del Moral, C., Adroer, N., Del Río, J.L., Patiño, C., Sisniega, H., et al. Secretion of the sweet-tasting protein thaumatin by recombinant strains of Aspergillus niger var. awamori. Applied Microbiology and Biotechnology 49:4 (1998), 393–398.
5. Firsov, A., Shaloiko, L., Kozlov, O., Vinokurov, L., Vainstein, A., Dolgov, S., Purification and characterization of recombinant supersweet protein thaumatin II from tomato fruit. Protein Expression and Purification 123 (2016), 1–5.
6. Greenfield, N.J., Using circular dichroism spectra to estimate protein secondary structure. Nature Protocols 1:6 (2006), 2876–2890.
7. Healey, R.D., Prasad, S., Rajendram, V., Thordarson, P., Unravelling the interaction between α-cyclodextrin with the thaumatin protein and a peptide mimic. Supramolecular Chemistry 27:5–6 (2015), 414–419.
8. Hellfritsch, C., Brockhoff, A., Stähler, F., Meyerhof, W., Hofmann, T., Human psychometric and taste receptor responses to steviol glycosides. Journal of Agricultural and Food Chemistry 60:27 (2012), 6782–6793.
9. Inan, M., Aryasomayajula, D., Sinha, J., Meagher, M.M., Enhancement of protein secretion in Pichia pastoris by overexpression of protein disulfide isomerase. Biotechnology and Bioengineering 93:4 (2006), 771–778.
10. Iyengar, R.B., Smits, P., van der Ouderaa, F., van der Wel, H., van Brouwershaven, J., Ravestein, P., et al. The complete amino-acid sequence of the sweet protein Thaumatin I. European Journal of Biochemistry 96:1 (1979), 193–204.
11. Jiang, P., Ji, Q., Liu, Z., Snyder, L.A., Benard, L.M.J., Margolskee, R.F., et al. The cysteine-rich region of T1R3 determines responses to intensely sweet proteins. The Journal of Biological Chemistry 279:43 (2004), 45068–45075.
12. Kim, S.H., de Vos, A., Ogata, C., Crystal structures of two intensely sweet proteins. Trends in Biochemical Sciences 13:1 (1988), 13–15.
13. Korver, O., Van, G.M., van der Wel, H., Spectrometric investigation of thaumatin I and II, two sweet-tasting proteins from Thaumatococcus daniellii Benth. European Journal of Biochemistry 35:3 (1973), 554–558.
14. Lee, J., Weickmann, J.L., Koduri, R.K., Ghosh-Dastidar, P., Saito, K., Blair, L.C., et al. Expression of synthetic thaumatin genes in yeast. Biochemistry 27:14 (1988), 5101–5107.
15. Lorber, B., Giegé, R., Nucleation and growth of thaumatin crystals within a gel under microgravity on STS-95 mission vs. under Earth's gravity. Journal of Crystal Growth 231:1–2 (2001), 252–261.
16. Mason, A.F., Thordarson, P., Synthesis of protein bioconjugates via cysteine-maleimide chemistry. Journal of Visualized Experiments, 113, 2016, e54157.
17. Masuda, T., Ide, N., Ohta, K., Kitabatake, N., High-yield secretion of the recombinant sweet-tasting protein thaumatin I. Food Science and Technology Research 16:6 (2010), 585–592.
18. Masuda, T., Ohta, K., Ojiro, N., Murata, K., Mikami, B., Tani, F., et al. A hypersweet protein: Removal of the specific negative charge at Asp21 enhances thaumatin sweetness. Scientific Reports, 6, 2015, 20255.
19. Nonaka, H., Fujishima, S., Uchinomiya, S., Ojida, A., Hamachi, I., FLAG-tag selective covalent protein labeling via a binding-induced acyl-transfer reaction. Bioorganic & Medicinal Chemistry Letters 19:23 (2009), 6696–6699.
20. Ohta, K., Masuda, T., Ide, N., Kitabatake, N., Critical molecular regions for elicitation of the sweetness of the sweet-tasting protein, thaumatin I. FEBS Journal 275:14 (2008), 3644–3652.
21. Ohta, K., Masuda, T., Tani, F., Kitabatake, N., Introduction of a negative charge at Arg82 in thaumatin abolished responses to human T1R2-T1R3 sweet receptors. Biochemical and Biophysical Research Communications 413:1 (2011), 41–45.
22. Ohta, K., Masuda, T., Tani, F., Kitabatake, N., The cysteine-rich domain of human T1R3 is necessary for the interaction between human T1R2-T1R3 sweet receptors and a sweet-tasting protein, thaumatin. Biochemical and Biophysical Research Communications 406:3 (2011), 435–438.
23. Pham, N., Schäfer, H., Wink, M., Production and secretion of recombinant thaumatin in tobacco hairy root cultures. Biotechnology Journal 7 (2012), 537–545.
24. Pronin, A.N., Tang, H., Connor, J., Keung, W., Identification of ligands for two human bitter T2R receptors. Chemical Senses 29:7 (2004), 583–593.
25. Robinson, A.S., Hines, V., Wittrup, K.D., Protein disulfide isomerase overexpression increases secretion of foreign proteins in Saccharomyces cerevisiae. Nature Biotechnology 12 (1994), 381–384.
26. Sha, C., Yu, X.-W., Zhang, M., Xu, Y., Efficient secretion of lipase r27RCL in Pichia pastoris by enhancing the disulfide bond formation pathway in the endoplasmic reticulum. Journal of Industrial Microbiology & Biotechnology 40:11 (2013), 1241–1249.
27. Shi, P., Zhang, J., Extraordinary diversity of chemosensory receptor genes repertoires among vertebrates. Korsching, S., Meyerhof, W., (eds.) Chemosensory systems in mammals, fishes and insects, 2008, Springer, New York, 1–23.
28. Szwacka, M., Siedlecka, E., Zawirska-Wojtasiak, R., Wiśniewski, Ł., Malepszy, S., Expression pattern of the pre-prothaumatin II gene under the control of the CaMV 35S promoter in transgenic cucumber (Cucumis sativus L.) flower buds and fruits. Journal of Applied Genetics 50:1 (2009), 9–16.
29. Thordarson, P., Le Droumaguet, B., Velonia, K., Well-defined protein–polymer conjugates-synthesis and potential applications. Applied Microbiology and Biotechnology 73:2 (2006), 243–254.
30. Tian, H., Fürstenberg, A., Huber, T., Labeling and single-molecule methods to monitor g protein-coupled receptor dynamics. Chemical Reviews 117:1 (2017), 186–245.
31. van der Wel, H., Loeve, K., Isolation and characterization of thaumatin I and II, the sweet-tasting proteins from Thaumatococcus daniellii Benth. European Journal of Biochemistry 31:2 (1972), 221–225.
32. van der Wel, H., Van, S.T.C., Royers, E.C., Crystallization and crystal data of thaumatin I, a sweet-tasting protein from Thaumatococcus daniellii benth. FEBS Letters 56:2 (1975), 316–317.