Brazzein is an interesting sweet-tasting protein which is extracted from the a west African fruit of the climbing plant, the Oubli (Pentadiplandra brazzeana, Baillon). It has only been recently extracted being first isolated in 1994 by researchers from the University of Wisconsin-Madison.
Brazzein has a similar intense sweetness similar to other proteins such as thaumatin and monellin. It is between 500 and 2,000 times sweeter than sucrose. On a per-molecule basis, brazzein is actually 9,500 times sweeter than a sucrose molecule making it one of sweetest tasting molecules available.
Many primates are sensitive to its sweetness except gorillas who have a mutation in their sweetness receptors which means they do not find the fruit containing it at all sweet and so do not consume it.
Structure Of Brazzein
The protein contains 54 amino-acids residues and has a molecular mass of 6.4 kDa. (Ming & Hellekant, 1994). It is one of the smallest, most heat-stable and pH-stable members of all the sweet proteins.
There is a minor component of brazzein extracted from the Oubli fruit known as des-pGlu1-brazzein which has 53 amino acids and twice the sweetness of brazzein itself (Assadi-Porter et al., 2000).
Sweetness Of Brazzein
The protein is 500 to 2,000 times sweeter than sucrose on a weight for weight basis, especially when compared to a 10 per cent sucrose or a 2 per cent sucrose solution respectively (Ming & Hellekant, 1994; Izawa et al., 1996).
Its sweetness is perceived to be similar to sucroase rather than other protein sweeteners such as thaumatin. It has a clean, sweet taste with a lingering aftertaste and slight delay which is more prolonged than aspartame in an equi-sweet solution (Pfeiffer et al., 2000).
In product development applications, brazzein is stable over a broad pH range from 2.5 to 8 (Birch, 2000) and heat stable at 98 °Cent. for 2 hours (Ming & Hellekant, 1994).
Product Development Uses
Brazzein is a useful alternative to other low-calorie sweeteners. It is safe for diabetics to use because it is a protein. It has extremely high solubility being greater than 50 mg/ml (Birch, 2000).
References
Assadi-Porter, F.M., Aceti, D.J., Markley, J.L. (April 2000). “Sweetness determinant sites of brazzein, a small, heat-stable, sweet-tasting protein”. Arch. Biochem. Biophys. 376 (2): 259-265. doi:10.1006/abbi.2000.1726. PMID 10775411
Birch, G. G. (2000). Ingredients Handbook – Sweeteners (Ingredients Handbook Series). Leatherhead Food Research Association. ISBN 0-905748-90-5.
Izawa, H., Ota, M., Kohmura, M., Ariyoshi, Y. (July, 1996). Synthesis and characterization of the sweet protein brazzein. Biopolymers. 39 (1): pp. 95–101. doi:10.1002/(SICI)1097-0282(199607)39:1<95::AID-BIP10>3.0.CO;2-B. PMID 8924630
Ming, D., Hellekant, G. (November, 1994). Brazzein, a new high-potency thermostable sweet protein from Pentadiplandra brazzeana B. FEBS Lett. 355 (1): pp. 106–8. doi:10.1016/0014-5793(94)01184-2. PMID 7957951
Pfeiffer, J.F., Boulton, R.B., Noble, A.C. (2000). Modelling the sweetness response using time-intensity data. Food Quality and Preference. 11 (1): pp. 129–138. doi:10.1016/S0950-3293(99)00036-1.
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