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제109회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Residue mutations in the sweetness loops for the sweet-tasting protein brazzein

2012년 3월 1일 12시 03분 57초
BIO.P-712 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
4월 25일 (수요일) 18:00~21:00
저자 및
조현주, 조동현, 윤석영, 공광훈
중앙대학교 화학과, Korea
Brazzein is a sweet-tasting protein first isolated from the fruit of Pentadiplandrabrazzeana Baillon found in West Africa. Brazzein is an intensely sweet-tasting protein with good stability, and it is 500-2000 times sweeter than sucrose on a weight basis. To identify critical residues important for sweetness of the sweet protein brazzein, 11 mutants of the residues in three loops of brazzein were constructed by site-directed mutagenesis. We found that mutations of Glu41 to Ala, Lys, or Arg at position 41 in loop40-43 made the molecules significantly sweeter than brazzein, while mutations at two distant residues (changing Arg43 to Lys or Glu) decreased sweetness. A similar pattern occurred at loop30-33, where mutation of the His31 to Arg significantly increased sweetness, while mutations at positions 30 or 33 in the immediate vicinity of this region significantly decreased sweetness. In addition, a Gln17 residue in the loop9-19 was necessary for structural integrity. From these results, we suggest the loops containing His31 and Glu41 to be critical regions of the molecule for eliciting sweetness, and the charge and/or structure of the side chain of these residues play an important role in the multi-point interactions between brazzein and the sweet-taste receptor.