Taste Enhancers

14,000,000 Leading Edge Experts on the ideXlab platform

Scan Science and Technology

Contact Leading Edge Experts & Companies

Scan Science and Technology

Contact Leading Edge Experts & Companies

The Experts below are selected from a list of 117 Experts worldwide ranked by ideXlab platform

Thomas Hofmann - One of the best experts on this subject based on the ideXlab platform.

  • quantitative determination of thiamine derived Taste Enhancers in aqueous model systems natural deep eutectic solvents nades and thermally processed foods
    Journal of Agricultural and Food Chemistry, 2020
    Co-Authors: Laura Brehm, Oliver Frank, Josef Ranner, Thomas Hofmann
    Abstract:

    To obtain high kokumi active building blocks which can be used to produce savory process flavors, it is essential to get a better understanding on the formation rate of kokumi active compounds like...

  • food grade synthesis of maillard type Taste Enhancers using natural deep eutectic solvents nades
    Molecules, 2018
    Co-Authors: Maximilian Kranz, Thomas Hofmann
    Abstract:

    The increasing demand for healthier food products, with reduced levels of table salt, sugar, and mono sodium glutamate, reinforce the need for novel Taste Enhancers prepared by means of food-grade kitchen-type chemistry. Although several Taste modulating compounds have been discovered in processed foods, their Maillard-type ex food production is usually not exploited by industrial process reactions as the yields of target compounds typically do not exceed 1–2%. Natural deep eutectic solvents (NADES) are reported for the first time to significantly increase the yields of the Taste Enhancers 1-deoxy-d-fructosyl-N-β-alanyl-l-histidine (49% yield), N-(1-methyl-4-oxoimidazolidin-2-ylidene) aminopropionic acid (54% yield) and N2-(1-carboxyethyl) guanosine 5′-monophosphate (22% yield) at low temperature (80–100 °C) within a maximum reaction time of 2 h. Therefore, NADES open new avenues to a “next-generation culinary chemistry” overcoming the yield limitations of traditional Maillard chemistry approaches and enable a food-grade Maillard-type generation of flavor modulators.

  • Salt Taste Enhancing l -Arginyl Dipeptides from Casein and Lysozyme Released by Peptidases of Basidiomycota
    Journal of Agricultural and Food Chemistry, 2018
    Co-Authors: Lisa Harth, Ulrike Krah, Andreas Dunkel, Diana Linke, Thomas Hofmann, Ralf G. Berger
    Abstract:

    Some L-arginyl dipeptides were recently identified as salt Taste Enhancers, thus opening the possibility to reduce the dietary sodium uptake without compromising on palatability. A screening of 15 basidiomycete fungi resulted in the identification of five species secreting a high peptidolytic activity (>3 kaU/mL; azocasein assay). PFP-LC-MS/MS and HILIC-MS/MS confirmed that L-arginyl dipeptides were liberated, when casein or lysozyme served as substrates. Much higher yields of dipeptides (42-75 µmol/g substrate) were released from lysozyme than from casein. The lysozyme hydrolysate generated by the complex set of peptidases of Trametes versicolor showed the highest L-arginyl dipeptide yields and a significant salt Taste enhancing effect in a model cheese matrix and in a curd cheese. With a broad spectrum of novel specific and non-specific peptidases active in the slightly acidic pH range, T. versicolor might be a suitable enzyme source for low-salt dairy products.

  • Salt Taste Enhancing l-Arginyl Dipeptides from Casein and Lysozyme Released by Peptidases of Basidiomycota
    Journal of Agricultural and Food Chemistry, 2016
    Co-Authors: Lisa Harth, Ulrike Krah, Andreas Dunkel, Diana Linke, Thomas Hofmann, Ralf G. Berger
    Abstract:

    Some l-arginyl dipeptides were recently identified as salt Taste Enhancers, thus opening the possibility to reduce dietary sodium uptake without compromising palatability. A screening of 15 basidiomycete fungi resulted in the identification of 5 species secreting a high peptidolytic activity (>3 kAU/mL; azocasein assay). PFP-LC-MS/MS and HILIC-MS/MS confirmed that l-arginyl dipeptides were liberated when casein or lysozyme served as substrate. Much higher yields of dipeptides (42–75 μmol/g substrate) were released from lysozyme than from casein. The lysozyme hydrolysate generated by the complex set of peptidases of Trametes versicolor showed the highest l-arginyl dipeptide yields and a significant salt Taste enhancing effect in a model cheese matrix and in a curd cheese. With a broad spectrum of novel specific and nonspecific peptidases active in the slightly acidic pH range, T. versicolor might be a suitable enzyme source for low-salt dairy products.

  • umami compounds and Taste Enhancers
    Flavour Development Analysis and Perception in Food and Beverages, 2015
    Co-Authors: Barbara Suess, Daniel Festring, Thomas Hofmann
    Abstract:

    This chapter outlines the discovery of umami Taste, and the basis of umami Taste perception then presents the function of the umami Taste receptor as well as structural prerequisites for its activation and modulation. A review of the isolation, identification and subsequent sensory characterization of natural umami (modulating) compounds by activity-guided fractionation is performed in the following. Different chemical classes of umami tastants and Taste modulators of both synthetic and natural origin as well as structural prerequisites for their Taste (modulating) activity are discussed, followed by an outline of their biosynthetic and/or non-enzymatic formation pathways.

Maximilian Kranz - One of the best experts on this subject based on the ideXlab platform.

  • food grade synthesis of maillard type Taste Enhancers using natural deep eutectic solvents nades
    Molecules, 2018
    Co-Authors: Maximilian Kranz, Thomas Hofmann
    Abstract:

    The increasing demand for healthier food products, with reduced levels of table salt, sugar, and mono sodium glutamate, reinforce the need for novel Taste Enhancers prepared by means of food-grade kitchen-type chemistry. Although several Taste modulating compounds have been discovered in processed foods, their Maillard-type ex food production is usually not exploited by industrial process reactions as the yields of target compounds typically do not exceed 1–2%. Natural deep eutectic solvents (NADES) are reported for the first time to significantly increase the yields of the Taste Enhancers 1-deoxy-d-fructosyl-N-β-alanyl-l-histidine (49% yield), N-(1-methyl-4-oxoimidazolidin-2-ylidene) aminopropionic acid (54% yield) and N2-(1-carboxyethyl) guanosine 5′-monophosphate (22% yield) at low temperature (80–100 °C) within a maximum reaction time of 2 h. Therefore, NADES open new avenues to a “next-generation culinary chemistry” overcoming the yield limitations of traditional Maillard chemistry approaches and enable a food-grade Maillard-type generation of flavor modulators.

Ralf G. Berger - One of the best experts on this subject based on the ideXlab platform.

  • Salt Taste Enhancing l -Arginyl Dipeptides from Casein and Lysozyme Released by Peptidases of Basidiomycota
    Journal of Agricultural and Food Chemistry, 2018
    Co-Authors: Lisa Harth, Ulrike Krah, Andreas Dunkel, Diana Linke, Thomas Hofmann, Ralf G. Berger
    Abstract:

    Some L-arginyl dipeptides were recently identified as salt Taste Enhancers, thus opening the possibility to reduce the dietary sodium uptake without compromising on palatability. A screening of 15 basidiomycete fungi resulted in the identification of five species secreting a high peptidolytic activity (>3 kaU/mL; azocasein assay). PFP-LC-MS/MS and HILIC-MS/MS confirmed that L-arginyl dipeptides were liberated, when casein or lysozyme served as substrates. Much higher yields of dipeptides (42-75 µmol/g substrate) were released from lysozyme than from casein. The lysozyme hydrolysate generated by the complex set of peptidases of Trametes versicolor showed the highest L-arginyl dipeptide yields and a significant salt Taste enhancing effect in a model cheese matrix and in a curd cheese. With a broad spectrum of novel specific and non-specific peptidases active in the slightly acidic pH range, T. versicolor might be a suitable enzyme source for low-salt dairy products.

  • Salt Taste Enhancing l-Arginyl Dipeptides from Casein and Lysozyme Released by Peptidases of Basidiomycota
    Journal of Agricultural and Food Chemistry, 2016
    Co-Authors: Lisa Harth, Ulrike Krah, Andreas Dunkel, Diana Linke, Thomas Hofmann, Ralf G. Berger
    Abstract:

    Some l-arginyl dipeptides were recently identified as salt Taste Enhancers, thus opening the possibility to reduce dietary sodium uptake without compromising palatability. A screening of 15 basidiomycete fungi resulted in the identification of 5 species secreting a high peptidolytic activity (>3 kAU/mL; azocasein assay). PFP-LC-MS/MS and HILIC-MS/MS confirmed that l-arginyl dipeptides were liberated when casein or lysozyme served as substrate. Much higher yields of dipeptides (42–75 μmol/g substrate) were released from lysozyme than from casein. The lysozyme hydrolysate generated by the complex set of peptidases of Trametes versicolor showed the highest l-arginyl dipeptide yields and a significant salt Taste enhancing effect in a model cheese matrix and in a curd cheese. With a broad spectrum of novel specific and nonspecific peptidases active in the slightly acidic pH range, T. versicolor might be a suitable enzyme source for low-salt dairy products.

Xiaodong Li - One of the best experts on this subject based on the ideXlab platform.

  • the discovery and mechanism of sweet Taste Enhancers
    Biomolecular Concepts, 2011
    Co-Authors: Xiaodong Li, Guy Servant, Catherine Tachdjian
    Abstract:

    : Excess sugar intake posts several health problems. Artificial sweeteners have been used for years to reduce dietary sugar content, but they are not ideal substitutes for sugar owing to their off-Taste. A new strategy focused on allosteric modulation of the sweet Taste receptor led to identification of sweet Taste 'Enhancers' for the first time. The enhancer molecules do not Taste sweet, but greatly potentiate the sweet Taste of sucrose and sucralose selectively. Following a similar mechanism as the natural umami Taste Enhancers, the sweet enhancer molecules cooperatively bind with the sweeteners to the Venus flytrap domain of the human sweet Taste receptor and stabilize the active conformation. Now that the approach has proven successful, Enhancers for other sweeteners and details of the molecular mechanism for the enhancement are being actively pursued.

  • molecular mechanism of the sweet Taste Enhancers
    Proceedings of the National Academy of Sciences of the United States of America, 2010
    Co-Authors: Feng Zhang, Guy Servant, Catherine Tachdjian, Boris Klebansky, Richard Fine, Hong Xu, Mark Zoller, Xiaodong Li
    Abstract:

    Positive allosteric modulators of the human sweet Taste receptor have been developed as a new way of reducing dietary sugar intake. Besides their potential health benefit, the sweet Taste Enhancers are also valuable tool molecules to study the general mechanism of positive allosteric modulations of T1R Taste receptors. Using chimeric receptors, mutagenesis, and molecular modeling, we reveal how these sweet Enhancers work at the molecular level. Our data argue that the sweet Enhancers follow a similar mechanism as the natural umami Taste enhancer molecules. Whereas the sweeteners bind to the hinge region and induce the closure of the Venus flytrap domain of T1R2, the Enhancers bind close to the opening and further stabilize the closed and active conformation of the receptor.

Catherine Tachdjian - One of the best experts on this subject based on the ideXlab platform.

  • the discovery and mechanism of sweet Taste Enhancers
    Biomolecular Concepts, 2011
    Co-Authors: Xiaodong Li, Guy Servant, Catherine Tachdjian
    Abstract:

    : Excess sugar intake posts several health problems. Artificial sweeteners have been used for years to reduce dietary sugar content, but they are not ideal substitutes for sugar owing to their off-Taste. A new strategy focused on allosteric modulation of the sweet Taste receptor led to identification of sweet Taste 'Enhancers' for the first time. The enhancer molecules do not Taste sweet, but greatly potentiate the sweet Taste of sucrose and sucralose selectively. Following a similar mechanism as the natural umami Taste Enhancers, the sweet enhancer molecules cooperatively bind with the sweeteners to the Venus flytrap domain of the human sweet Taste receptor and stabilize the active conformation. Now that the approach has proven successful, Enhancers for other sweeteners and details of the molecular mechanism for the enhancement are being actively pursued.

  • molecular mechanism of the sweet Taste Enhancers
    Proceedings of the National Academy of Sciences of the United States of America, 2010
    Co-Authors: Feng Zhang, Guy Servant, Catherine Tachdjian, Boris Klebansky, Richard Fine, Hong Xu, Mark Zoller, Xiaodong Li
    Abstract:

    Positive allosteric modulators of the human sweet Taste receptor have been developed as a new way of reducing dietary sugar intake. Besides their potential health benefit, the sweet Taste Enhancers are also valuable tool molecules to study the general mechanism of positive allosteric modulations of T1R Taste receptors. Using chimeric receptors, mutagenesis, and molecular modeling, we reveal how these sweet Enhancers work at the molecular level. Our data argue that the sweet Enhancers follow a similar mechanism as the natural umami Taste enhancer molecules. Whereas the sweeteners bind to the hinge region and induce the closure of the Venus flytrap domain of T1R2, the Enhancers bind close to the opening and further stabilize the closed and active conformation of the receptor.