Plant Diversity ›› 1996, Vol. 18 ›› Issue (02): 1-3.
• Articles •
DING Ming, Goran Hellekant, HU Zhong
A sweet protein, brazzein, has been discovered from the fruits of Pentadiplandra brazzeana B., a tropical wild plant in west Africa. Brazzein has 54 amino acid residues; it is 2000 times sweeter than sucrose (Ming and Hellekant, 1994 ). In this article, further characterization shows that its molecular weight is 6.5 kD and isoelectric point is 5. It has 8 cysteines and they form four disulfide bonds. After treating its aqueous solution at 80 ℃ for 4 hrs, no changes in sweetness and behavior of electrophoresis are found. Secondary structures predictions suggests that beta turns and beta sheets are the dominant structures in the protein.
Sweet protein brazzein,
DING Ming, Goran Hellekant, HU Zhong. CHARACTERIZATION AND CHEMICAL MODIFICATION OF BRAZZEIN, A HIGH POTENCY THERMOSTABLE SWEET PROTEIN FROM PENTADIPLANDRA BRAZZEANA[J]. Plant Diversity, 1996, 18(02): 1-3.
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