Brazzein is a sweet- tasting protein secreted from the fruits of the West African plant Pentadiplandra brazzeana . It was first isolated at the University of Wisconsin-Madison in 1994 [2] .
| Brazzein | |
|---|---|
 Protein structure determined by NMR [1] . | |
| Designations | |
| Characters | MONA_DIOCU |
| PDB | 1BRZ , More structures |
| Uniprot | P56552 |
Brazzein is found in the intercellular space of the pulp surrounding the seeds of the fetus. After pentadine, discovered in 1989, brazzein is the second sweet taste protein found in Pentadiplandra brazzeana [3] .
Like other sweet proteins found in plants, such as moneline and thaumatin , it is much sweeter than usual substitutes (500–2000 times sweeter than sucrose) [4] . The fruit has a sweet taste for monkeys, chimpanzees and humans, but gorillas, due to mutations in the sweet receptors, do not perceive brazzein as sweet and therefore do not eat the fruits of plants [5] [6] .
Content
- 1 Traditional use
- 2 Protein structure
- 3 Sweet properties
- 4 Use as a sweetener
- 5 See also
- 6 notes
Traditional Usage
The shrub Pentadiplandra brazzeana, from which the protein was isolated, grows in Gabon and Cameroon, where its fruits have been consumed by primates and local residents for a long time. Thanks to brazzein and pentadine, the berries have a strong sweet taste. African Aborigines call the fruit “oubli” (from the French. Forget), because it is believed that their taste can make babies forget about their mother’s milk.
Protein Structure
Monomeric protein, consisting of 54 amino acid residues, is the smallest of sweet proteins with a molecular weight of 6.5 kDa [2] . The amino acid sequence of brazzein shown in the Swiss-Prot protein database is as follows: QDKCKKVYEN YPVSKCQLAN QCNYDCKLDK HARSGECFYD EKRNLQCICD YCEY [7]
The structure of brazzein was determined by nuclear magnetic resonance (NMR) at pH 5.2 and 22 ° C. Brazzein has four uniformly distributed disulfide bonds and does not contain sulfhydryl groups.
Three-dimensional analysis of brazzein showed one alpha helix and three antiparallel beta folds. Its structure is not similar to any of the other two taste-sweet proteins, monellin and thaumatin [8] .
However, a recent three-dimensional study shows that these three proteins have similar “sweet fingers” that are believed to cause a sweet taste [9] .
It was found that residues 29-33 and 39-43, residue 36, as well as the C-terminus contribute to the sweet taste of the protein. Protein charge also plays an important role in its interaction with the sweet taste receptor [2] .
Based on these factors, an improved brazzein called pGlu-1-brazzein was synthesized, which was reported to be twice as sweet as the natural counterpart [10] .
Sweet Properties
In terms of the mass of brazzein, it is 500-2000 times sweeter than sucrose compared with 10% sucrose and 2% sucrose solution, respectively [8] .
Its sweet taste is more reminiscent of sucrose than thaumatin, with a long finish and a slight delay (longer than that of aspartame) in an equally sweet solution [11] .
Brazzein is stable in a wide pH range from 2.5 to 8 [12] and is resistant to 98 ° C for 2 hours [2] .
Use as a sweetener
Brazzein is an alternative to affordable low-calorie sweeteners. Like protein, it is safe for diabetics. It is also very soluble in water (> 50 mg / ml) [12] .
When mixed with other sweeteners, such as aspartame and stevia, brazzein reduces the side aftertaste and complements their taste [13] .
In terms of taste, it is closer to sucrose than other natural sweeteners (except thaumatin). Unlike other proteins with a sweet taste, it withstands heat, which makes it more suitable for industrial processing of food products [14] .
In laboratory studies, the creation of a protein using peptide synthesis was reported [8] , and recombinant proteins were successfully obtained using E. coli. [fifteen]
Texas-based Prodigene and Nectar Worldwide were among the licensees to use the Wisconsin Alumni Research Foundation's brazzein patents and added genetically to corn. Such brazzein can be commercially extracted from corn by conventional grinding. About one ton of corn gives 1-2 kilograms of brazzein. It can also be applied to plants, such as wheat, to produce pre-sweetened grains, such as cereals. [fourteen]
See also
- Curculin
- Miraculin
Notes
- ↑ PDB 2brz ; Caldwell JE, Abildgaard F., Dzakula Z., Ming D., Hellekant G., Markley JL Solution structure of the thermostable sweet-tasting protein brazzein (Eng.) // Nat. Struct. Biol. : journal. - 1998 .-- June ( vol. 5 , no. 6 ). - P. 427-431 . - DOI : 10.1038 / nsb0698-427 . - PMID 9628478 .
- ↑ 1 2 3 4 Ming D., Hellekant G. Brazzein, a new high-potency thermostable sweet protein from Pentadiplandra brazzeana B (English) // FEBS Lett. : journal. - 1994 .-- November ( vol. 355 , no. 1 ). - P. 106-108 . - DOI : 10.1016 / 0014-5793 (94) 01184-2 . - PMID 7957951 .
- ↑ van der Wel H., Larson G., Hladik A., Hladik CM, Hellekant G., Glaser D. Isolation and characterization of pentadin, the sweet principle of Pentadiplandra brazzeana Baillon (Eng.) // Chem. Senses : journal. - 1989. - Vol. 14 , no. 1 . - P. 75-79 . - DOI : 10.1093 / chemse / 14.1.75 .
- ↑ Sweet-tasting Proteins // Biopolymers: Polyamides and Complex Proteinaceous Materials II. - 8th. - Weinheim: Wiley-VCH, 2004. - P. 203–209. - ISBN 978-3-527-30223-9 .
- ↑ Guevara EE, Veilleux CC, Saltonstall K., Caccone A., Mundy NI, Bradley BJ Potential arms race in the coevolution of primates and angiosperms: brazzein sweet proteins and gorilla taste receptors (English) // American Journal of Physical Anthropology : journal. - 2016 .-- July ( vol. 161 , no. 1 ). - P. 181-185 . - DOI : 10.1002 / ajpa.23046 . - PMID 27393125 .
- ↑ Gorillas may have evolved a way to beat a cheating berry plant (Eng.) // New Scientist : magazine. - 2016 .-- 23 July.
- ↑ UniProtKB / Swiss-Prot database entry # PP56552
- ↑ 1 2 3 Izawa H., Ota M., Kohmura M., Ariyoshi Y. Synthesis and characterization of the sweet protein brazzein (Eng.) // Biopolymers: journal. - 1996 .-- July ( vol. 39 , no. 1 ). - P. 95-101 . - DOI : 10.1002 / (SICI) 1097-0282 (199607) 39: 1 <95 :: AID-BIP10> 3.0.CO; 2-B . - PMID 8924630 .
- ↑ Tancredi T., Pastore A., Salvadori S., Esposito V., Temussi PA Interaction of sweet proteins with their receptor. A conformational study of peptides corresponding to loops of brazzein, monellin and thaumatin (English) // Eur. J. Biochem. : journal. - 2004 .-- June ( vol. 271 , no. 11 ). - P. 2231-2240 . - DOI : 10.1111 / j.1432-1033.2004.04154.x . - PMID 15153113 .
- ↑ Assadi-Porter FM, Aceti DJ, Markley JL Sweetness determinant sites of brazzein, a small, heat-stable, sweet-tasting protein (Eng.) // Archives of Biochemistry and Biophysics : journal. - Elsevier , 2000 .-- April ( vol. 376 , no. 2 ). - P. 259-265 . - DOI : 10.1006 / abbi.2000.1726 . - PMID 10775411 .
- ↑ Pfeiffer JF, Boulton RB, Noble AC Modeling the sweetness response using time-intensity data (Eng.) // Food Quality and Preference : journal. - 2000. - Vol. 11 , no. 1 . - P. 129-138 . - DOI : 10.1016 / S0950-3293 (99) 00036-1 .
- ↑ 1 2 Birch, Gordon Gerard. Ingredients Handbook - Sweeteners (Ingredients Handbook Series). - Leatherhead Food Research Association, 2000. - ISBN 978-0-905748-90-0 .
- ↑ Hellekant G., Danilova V. Brazzein a Small, Sweet Protein: Discovery and Physiological Overview (Eng.) // Chem. Senses : journal. - 2005. - Vol. 30 , no. Supplement 1 . - P. i88 — i89 . - DOI : 10.1093 / chemse / bjh127 . - PMID 15738210 .
- ↑ 1 2 Template: US patent reference
- ↑ Assadi-Porter FM, Aceti DJ, Cheng H., Markley JL Efficient production of recombinant brazzein, a small, heat-stable, sweet-tasting protein of plant origin (Eng.) // Archives of Biochemistry and Biophysics : journal. - Elsevier , 2000 .-- April ( vol. 376 , no. 2 ). - P. 252—258 . - DOI : 10.1006 / abbi.2000.1725 . - PMID 10775410 .