Importance of Glu53 in the C-terminal region of brazzein, a sweet-tasting protein
- Authors
- Lim, Jin-Kyung; Jang, Jin-Chul; Kong, Ji-Na; Kim, Myung-Chul; Kong, Kwang-Hoon
- Issue Date
- Jul-2016
- Publisher
- WILEY-BLACKWELL
- Keywords
- brazzein; Glu53; mutagenesis; sweetness determinant
- Citation
- JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, v.96, no.9, pp 3202 - 3206
- Pages
- 5
- Journal Title
- JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE
- Volume
- 96
- Number
- 9
- Start Page
- 3202
- End Page
- 3206
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/6751
- DOI
- 10.1002/jsfa.7501
- ISSN
- 0022-5142
1097-0010
- Abstract
- BACKGROUND: The sweetness of brazzein, one of the known sweet proteins, is dependent on charges and/or structures of its specific amino acid side chains. As the residues in the C-terminus of brazzein are known to play a critical role in sweetness, the currently unknown function of Glu53 requires further study.
RESULTS: To identify important residues responsible for the sweetness of the protein brazzein, four mutants of theGlu53 residue in the C-terminal region of des-pE1M-brazzein, which lacks the N-terminal pyroglutamate, were constructed using site-directed mutagenesis. Mutations of Glu53 substitution to Ala or Asp significantly decreased the sweetness. On the other hand, a Lys mutation resulted in a molecule with sweetness similar to that of des-pE1M-brazzein. Mutation of Glu53 to Arg resulted in a molecule significantly sweeter than des-pE1M-brazzein, which agrees with previous findings showing that mutation with positively charged residues results in a sweeter protein.
CONCLUSION: Our results suggest that the residue at position 53 is crucial for the sweetness of brazzein, which may be interacting with the sweet-taste receptor. (C) 2015 Society of Chemical Industry
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