The Effect of Mutation in Brazzein Deduced from Mutational Sites and Sequence Carbon Content
International Journal of Genetics and Genomics
Volume 3, Issue 6, December 2015, Pages: 59-65
Received: Sep. 25, 2015; Accepted: Oct. 10, 2015; Published: Oct. 26, 2015
Views 4501      Downloads 169
Ezekiel Amri, Department of Science and Laboratory Technology, Dares Salaam Institute of Technology, Dares Salaam, Tanzania
Article Tools
Follow on us
Brazzein is a small sweet-tasting protein isolated from the fruit of the African plant, Pentadiplandra brazzeana Baillon with potential of replacement of carbohydrate sweeteners. Carbon content analysis was used to examine the effect of mutation in brazzein’s two regions at residues 29–33 and 39–43 with residue 36 reported to be important in sweet tasting of the protein. Analysis for local carbon density at the mutational sites for brazzein mutants with increased sweetness taste at residues 29 and 41 revealed normal carbon distribution curves with increased carbon frequency peak compared to the wild-type, consequently stabilized the local structure. Brazzein mutants with reduced sweetness taste at residue position 30, 33, 36 and 43 were mostly characterized by abnormal broadened distribution curve for carbon content with decreased frequency peak which destabilized the local structure and possibly leading to loss of protein functionality. Further analysis of carbon distribution profile along protein sequences of brazzein revealed a variation in carbon distribution between mutants with increased sweetness taste and those with decreased sweetness taste. Mutants with increased sweetness taste had carbon distribution profile balancing well conforming to the globular proteins which prefers to have 31.45% of carbon all along the sequence for stability. This study has provided further information and additional insights into protein atomic composition in brazzein and its role in understanding the effect of mutation.
Brazzein, Carbon Content, Mutation, Sweet-Tasting Protein
To cite this article
Ezekiel Amri, The Effect of Mutation in Brazzein Deduced from Mutational Sites and Sequence Carbon Content, International Journal of Genetics and Genomics. Vol. 3, No. 6, 2015, pp. 59-65. doi: 10.11648/j.ijgg.20150306.11
Copyright © 2015 Authors retain the copyright of this article.
This article is an open access article distributed under the Creative Commons Attribution License ( which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Jin, Z., V. Danilova, F.M. Assadi-Porter, D.J. Aceti, J.L. Markley and G. Hellekant, 2003. Critical regions for the sweetness of brazzein. FEBS Lett., 544: 33–37.
Nagata, K., N. Hongo, Y. Kameda, A. Yamamura, H. Sasaki, W. C. Lee and M. Tanokura, 2013. The structure of brazzein, a sweet-tasting protein from the wild African plant Pentadiplandra brazzeana. Acta Crystallogr. Sect. D-Biol. Crystallogr., 69(4): 642-647.
Ming, D. and G. Hellekant, 1994. Brazzein, a new high-potency thermo stable sweet protein from Pentadiplandra brazzeana B. FEBS letters, 355(1):106-108.
Hellekant, G. and V. Danilova, 2005. Brazzein a Small, Sweet Protein: Discovery and Physiological Overview. Chem. Senses, 30:88–89.
Faus, I., 2000. Recent developments in the characterization and biotechnological production of sweet-tasting proteins. Appl. Microbiol. Biotechnol., 53: 145–251.
Nookaraju, A., C.P. Upadhyaya, S.K. Pandey, K.E. Young, S.J. Hong, S.K. Park and S.W. Park, 2010. Molecular approaches for enhancing sweetness in fruits and vegetables. SciHortic., 127(1) 1-15.
Yount, N.Y. and M.R. Yeaman, 2004. Multidimensional signatures in antimicrobial peptides. Proc. Natl. Acad. Sci. U.S.A. 101:7363-7368.
Assadi-Porter, F.M., D.J. Aceti and J.L. Markley, 2000. Sweetness determinant sites of brazzein, a small, heat-stable, sweet-tasting protein. Arch Biochem Biophys. 376(2): 259-265.
Assadi-Porter, F.M., E.L. Maillet, J.T. Radek, J. Quijada, J.L. Markley and M. Max, 2010. Key amino acid residues involved in multi-point binding interactions between brazzein, a sweet protein, and the T1R2–T1R3 human sweet receptor. J. Mol. Biol, 398(4): 584-599.
Yoon, S.Y., J.N. Kong, D.H. Jo and K.H. Kong, 2011. Residue mutations in the sweetness loops for the sweet-tasting protein brazzein. Food Chem., 129(4): 1327-1330.
Lee, J.W., J.E. Cha, D.H. Jo and K.H. Kong, 2013. Multiple mutations of the critical amino acid residues for the sweetness of the sweet-tasting protein, brazzein. Food Chem., 138(2): 1370-1373.
Rajasekaran, E., K. Akila and M. Vijayasarathy, 2011. Allotment of carbon is responsible for disorders in proteins. Bioinformaution, 6(8): 291.
Rajasekaran, E., 2012. CARd: Carbon distribution analysis program for protein sequences. Bioinformation, 8(11): 508.
Akila, K., N. Sneha and E. Rajasekaran, 2012. Study on carbon distribution at protein regions of disorder. Intern. J. Biosc., Biochem And Bioinf., 2(2): 58–60.
Caldwell, J.E., F. Abildgaard, Ž. Džakula, D. Ming, G. Hellekant, and J.L. Markley, 1998. Solution structure of the thermostable sweet-tasting protein brazzein. Nat Struct. Mol. Biol, 5(6): 427-431.
Rajasekaran, E. and M. Vijayasarathy, 2011. CARBANA: Carbon analysis program for protein sequences. Bioinformation, 5(10): 455.
Zelko, I.N., T.J. Mariani and R. J. Folz, 2002. Superoxide dismutase multigene family: a comparison of the Cu Zn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression. Free Radic Biol Med., 33(3): 337-349.
Amri, E., F.A. Mamboya, P.D. Nsimama and E. Rajasekaran, 2012. Role of carbon in crystal structures of wild-type and mutated form of dihydrofolate reductase-thymidylate synthase of plasmodium falciparum. Inter. J. Appl. Biol. Pharmaceut Tech. 3(3): 1-6.
Yue, P., Z. Li, and J. Moult, 2005. Loss of protein structure stability as a major causative factor in monogenic disease. J. Mol. Biol., 353(2): 459-473.
Reva, B., Y. Antipin and C. Sander, 2011. Predicting the functional impact of protein mutations: Application to cancer genomics. Nucleic Acids Res., 1: 39(17): e118.
Mamboya, F.A., P.D. Nsimama, E. Amri, J.S. Sharmila and E. Rajasekaran, 2012. Carbon distribution analysis on mutations responsible for Li-Fraumeni syndrome.GSTF J. Bio Sci., 1(2): 1-6.
Nsimama, P.D., A.F. Mamboya, E. Amri and E. Rajasekaran, 2012. Correlation between the mutated colour tunings and carbon distributions in Luciferase bioluminescence. J. Comput. Intel. Bioinf., 5(2): 106-112.
Johri, P., 2013. Atomic level sequence analysis–A Review. Int. J. Comput Bioinfo in Silico Model, 2(4): 173-179.
Senthil, R. and E. Rajasekaran, 2009. Comparative analysis of carbon distribution and hydropathy plot. J. Adv. Biotech., 8(9): 30-31.
Bragg, G.J. and L. Hyder, 2004. Nitrogen versus carbon use in prokaryotic genomes and proteomes. Biol. Sci., 271: 374-377.
Esposito, V., R. Gallucci, D. Picone, G. Saviano, T. Tancredi and P.A. Temussi, 2006.The importance of electrostatic potential in the interaction of sweet proteins with the sweet taste receptor. J. Mol. Biol., 360(2): 448-456.
Jo, H.J., J.S. Noh and K.H. Kong, 2013. Efficient secretory expression of the sweet-tasting protein brazzein in the yeast Kluyveromyces lactis. Protein expression and purification, 90(2): 84-89.
Suh, J.Y., H.S. Kim, M.C. Kim and, K.H. Kong, 2014. Design and Evaluation of Synthetic Peptides Corresponding to the Sweetness Loop of the Sweet-Tasting Protein Brazzein. Bull. Korean Chem. Soc, 35(11): 3353.
Fake, G. and J. Howard, 2014. Brazzein: A High-Intensity Natural Sweetener. In Commercial Plant-Produced Recombinant Protein Products (pp. 247-257). Springer Berlin Heidelberg.
Science Publishing Group
1 Rockefeller Plaza,
10th and 11th Floors,
New York, NY 10020
Tel: (001)347-983-5186