%A DING Ming, Goran Hellekant, HU Zhong %T CHARACTERIZATION AND CHEMICAL MODIFICATION OF BRAZZEIN, A HIGH POTENCY THERMOSTABLE SWEET PROTEIN FROM PENTADIPLANDRA BRAZZEANA %0 Journal Article %D 1996 %J Plant Diversity %R %P 1-3 %V 18 %N 02 %U {https://journal.kib.ac.cn/CN/abstract/article_31017.shtml} %8 1996-04-25 %X 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.