Structure basis of the improved sweetness and thermostability of a unique double-sites single-chain sweet-tasting protein monellin (MNEI) mutant

Zhao, Meng; Xu, Xiangqun; Liu, Bo

doi:10.1016/j.biochi.2018.08.010

Cited by 10 publications

(5 citation statements)

References 28 publications

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“…Studies following this strategy determined T1R1/T1R3 (umami receptor) active residues were Gln52, His71, Tyr107, Asp147, Ser148, Thr149, Arg151, Ala170, Ser172, Asp192, Tyr220, Arg277, Glu301, Gln302, Ser306, Gly304, His308, His364, and Glu429 [ 56 , 57 , 58 ]. Following this theoretical focus, glutamate receptors’ crystal structures have served to homology model T1R2/T1R3 (sweetness receptor), whose active residues were predicted to be Ala49, Ser53, Ser59, Lys60, Glu148, Asp169, Arg172, Lys174, Asp188, Asp216, Leu245, Pro246, Ser276, Leu313, Tyr314, Asp456, and Ser458 [ 59 , 60 ]. In particular, dry-cured ham-derived peptides KGDESLLA, SEE, ES, and DES were calculated to be recognized by Ser146 and Glu277 in T1R3 [ 61 ].…”

Section: Taste Evaluation Assessmentsmentioning

confidence: 99%

Bioactive and Sensory Di- and Tripeptides Generated during Dry-Curing of Pork Meat

Heres

Toldrá

2023

IJMS

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Dry-cured pork products, such as dry-cured ham, undergo an extensive proteolysis during manufacturing process which determines the organoleptic properties of the final product. As a result of endogenous pork muscle endo- and exopeptidases, many medium- and short-chain peptides are released from muscle proteins. Many of them have been isolated, identified, and characterized, and some peptides have been reported to exert relevant bioactivity with potential benefit for human health. However, little attention has been given to di- and tripeptides, which are far less known, although they have received increasing attention in recent years due to their high potential relevance in terms of bioactivity and role in taste development. This review gathers the current knowledge about di- and tripeptides, regarding their bioactivity and sensory properties and focusing on their generation during long-term processing such as dry-cured pork meats.

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Section: Taste Evaluation Assessmentsmentioning

confidence: 99%

Bioactive and Sensory Di- and Tripeptides Generated during Dry-Curing of Pork Meat

Heres

Toldrá

2023

IJMS

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“…To date, however, an efficient sweet-tasting protein engineering strategy is not widely accepted or considerably applied [67]. Studies reveal that some single-point mutations can improve these sweet-tasting proteins' thermal stability, but these research works were conducted mainly according to random guess, which is time-consuming and very costly [66,[68][69][70][71]. Lately, more attention has been paid to in silico approaches to apply target-oriented mutagenesis given its low cost and relatively good accuracy for high-throughput screening purposes.…”

Section: Applications In the Food Industry And Sustainability Issuesmentioning

confidence: 99%

Brazzein and Monellin: Chemical Analysis, Food Industry Applications, Safety and Quality Control, Nutritional Profile and Health Impacts

Saraiva

Carrascosa

Ramos

et al. 2023

Foods

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Recently, customers have been keener to buy products manufactured using all-natural ingredients with positive health properties, but without losing flavor. In this regard, the objective of the current study is to review the consumption of brazzein and monellin, their nutritional profiles and health effects, and their potential applications in the food industry. This poses challenges with sustainability and important quality and safety indicators, as well as the chemical processes used to determine them. To better understand the utilization of brazzein and monellin, the chemical analysis of these two natural sweet proteins was also reviewed by placing particular emphasis on their extraction methods, purification and structural characterization. Protein engineering is considered a means to improve the thermal stability of brazzein and monellin to enhance their application in food processing, especially where high temperatures are applied. When the quality and safety of these sweet proteins are well-investigated and the approval from safety authorities is secured, the market for brazzein and monellin as food ingredient substitutes for free sugar will be guaranteed in the future. Ultimately, the review on these two natural peptide sweeteners increases the body of knowledge on alleviating problems of obesity, diabetes and other non-communicable diseases.

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“…. π bond interaction with F89, which are responsible for its improved thermostability (Tm values 84.9 and 74.2 • C for E2N/E23A and wild-type MNEI, respectively) (Figures 2C,D) (48).…”

Section: "Proteins Sectors" Determines the Stability Of Sweet-tasting Proteinsmentioning

confidence: 99%

New Insight Into the Structure-Activity Relationship of Sweet-Tasting Proteins: Protein Sector and Its Role for Sweet Properties

Zhao

Wang

Zheng³

et al. 2021

Front. Nutr.

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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.

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Structure basis of the improved sweetness and thermostability of a unique double-sites single-chain sweet-tasting protein monellin (MNEI) mutant

Cited by 10 publications

References 28 publications

Bioactive and Sensory Di- and Tripeptides Generated during Dry-Curing of Pork Meat

Bioactive and Sensory Di- and Tripeptides Generated during Dry-Curing of Pork Meat

Brazzein and Monellin: Chemical Analysis, Food Industry Applications, Safety and Quality Control, Nutritional Profile and Health Impacts

New Insight Into the Structure-Activity Relationship of Sweet-Tasting Proteins: Protein Sector and Its Role for Sweet Properties

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