Abstract
Sweet-tasting protein is a kind of biomacromolecule that has remarkable sweetening power and is regarded as the promising sugar replacer in the future. Some sweet-tasting proteins has been used in foods and beverages. However, the structure and function relationship of these proteins is still elusive, and guidelines for their protein engineering is limited. It is well-known that the sweet-tasting proteins bind to and activate the sweet taste receptor T1R2/T1R3, thus eliciting their sweetness. The “wedge-model” for describing the interaction between sweet-tasting proteins and sweet taste receptor to elucidate their sweetness has been reported. In this perspective article, we revealed that the intramolecular interaction forces in sweet-tasting proteins is directly correlated to their properties (sweetness and stability). This intramolecular interaction pattern, named as “protein sector,” refers to a small subset of residues forming physically connections, which cooperatively affect the function of the proteins. Based on the analysis of previous experimental data, we suggest that “protein sector” of sweet-tasting proteins is pivotal for their sweet properties, which are meaningful guidelines for the future protein engineering.
Highlights
Sweet-tasting proteins are originated from the natural plants and exhibit extraordinary sweetening power, which are regarded as suitable replacers of sugars and artificial sweeteners in the future to improve the health of human beings, such as the control of obesity, diabetes, and hyperlipemia [1]
Similar structural rearrangements were described in other variants of brazzein [45]. These results highlight the significance of intramolecular interaction patterns (“protein sectors”) for the sweetness of sweet-tasting proteins
Based on the above analysis, it is evident that “protein sector” in sweet-tasting proteins is significant for understanding their structure and function relationship, which is essential for the protein engineering of these biomacromolecules
Summary
Sweet-tasting proteins are originated from the natural plants and exhibit extraordinary sweetening power, which are regarded as suitable replacers of sugars and artificial sweeteners in the future to improve the health of human beings, such as the control of obesity, diabetes, and hyperlipemia [1]. Similar structural rearrangements were described in other variants of brazzein [45] These results highlight the significance of intramolecular interaction patterns (“protein sectors”) for the sweetness of sweet-tasting proteins. The multiple-sites mutant H31R/E36D/E41A of sweet-tasting protein brazzein displayed significantly improved sweetness than those of three double-sites mutants (H31R/E36D, H31R/E41A, and E36D/E41A) and three single-site mutants (H31R, E36D, and E41A) [46] These results further underline the essential roles of intramolecular interaction organization (“protein sectors”) in the sweet-tasting proteins for their performance. All these new interactions establish a stabilizing hydrogen bonds network that account for the improved stability of the mutated protein [43] These results together suggest the crucial roles of intramolecular interaction patterns (“protein sectors”) for the stability of sweettasting proteins
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