Pentadiplandra brazzeana

Pentadin is a sweet protein extracted from the plant, Pentadiplandra brazzeana Baillon, a shrub found in tropical forests of a few African... 

Van der Wei H, Larson G, Hladik A, Hladik CM, Hellekant G, Glaser D, Isolation and characterization of pentadin, the sweet principle of Pentadiplandra brazzeana Baillon, Chem Senses 14 75-79, 1989. 

Ming D, Hellekant G, Brazzein, a new high potency thermostable sweet protein from Pentadiplandra Brazzeana B, EEBS Lett, 355 106-108, 1994. 

Brazzein is a sweet protein that was isolated from the fruit of the West African climbing plant Oubli (Pentadiplandra brazzeana Baillon). Along with pentadin, which was discovered in 1989, brazzein is the second sweet protein that was discovered in this fruit. Like other natural sweet proteins such as monellin and thaumatin, it is highly sweet. On a weight basis, brazzein is 500 times sweeter than sucrose when compared to 10% sucrose solution and 2000 times sweeter when compared to 2% sucrose solution. Its sweet perception is more similar to that of sucrose than that of thaumatin, and it presents a clean sweet taste with a lingering aftertaste. Brazzein is stable over a broad pH range from 2.5 to 8 and is heat stable at 80 °C for 4h.84... 

Des-pGlu 1 -brazzein Pentadiplandra brazzeana Sweet — 2X >Brazzein,... 

Brazzein, the smallest of sweet proteins, was discovered only in 1994 (Ming and Hellekant, 1994) in Pentadiplandra brazzeana B. This protein, whose sequence contains 54-amino acid residues, is 2000 times sweeter than sucrose when compared to a 2% sucrose aqueous solution. Its taste was described as more similar to sucrose than that of thaumatin (Ming and Hellekant, 1994). As can be seen in Figure 5C, the 3D structure of brazzein, determined by NMR spectroscopy in solution at pH 5.2 (Caldwell et al., 1998), is very simple. It contains one a-helix and three strands of antiparallel )3-sheet. The structure is stabilized by four disulfide bonds, three connecting the helix to the jS-sheet. It does not resemble either that of monellin or that of thaumatin instead, it resembles those of plant y-thionins and defensins and arthropod toxins. According to the SCOP classification (Murzin et al., 1995), brazzein belongs to the Scorpion toxin-like superfamily. 

Brazzain. Polypeptide of 54 amino acids, Mr 6473, from the west African tree Pentadiplandra brazzeana (llliaceae). In a 2% solution it is 2000 times sweeter than cane sugar and shows good thermal stability (no loss of activity after 4 h at 80 °C), compare with mo-nellin, thaumatin. B. can also be obtained by synthesis (solid phase method) or biotechnologic ly in genetically engineered Escherichia coli cultures, lit.- Biopolymers 39, 95-101 (1996). PaL WO 9531 547 (publ. 23.11.1995). gen. FEBS Utt. 355,106 ff. (1994). 

Pentadin. Sweet-tasting protein (Mr 12000) ft-om the plant Pentadiplandra brazzeana (Pentadiplandraceae) having a 500-fold higher sweetness than sucrose. In contrast to other, protein-based sweeteners, P. is stable to heat. 

---