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Naofumi Kitabatake - One of the best experts on this subject based on the ideXlab platform.
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introduction of a negative charge at arg82 in thaumatin abolished responses to human t1r2 t1r3 sweet receptors
Biochemical and Biophysical Research Communications, 2011Co-Authors: Keisuke Ohta, Tetsuya Masuda, Fumito Tani, Naofumi KitabatakeAbstract:Abstract Thaumatin, an intensely sweet-tasting protein, elicits a sweet-taste sensation at a level as low as 50 nM. Although previous sensory analyses have suggested that Lys67 and Arg82 are important to the Sweetness of thaumatin, the exact effects of each residue on sweet receptors are still unknown. In the present study, various mutants of thaumatin altered at Arg82 as well as Lys67 were prepared and their Sweetness levels were quantitatively evaluated by cell-based assays using HEK293 cells expressing human sweet receptors. Mutations at Arg82 had a more deteriorative effect on Sweetness than mutations at Lys67. Particularly, a charge inversion at Arg82 (R82E) resulted in an abolishment of the response to sweet receptors even at a concentration as high as 1 mM. These results indicate that Arg82 plays a central role in determining the Sweetness of thaumatin. A strict spatial charge location at residue 82 appears to be required for interaction with sweet receptors.
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Introduction of a negative charge at Arg82 in thaumatin abolished responses to human T1R2–T1R3 sweet receptors
Biochemical and Biophysical Research Communications, 2011Co-Authors: Keisuke Ohta, Tetsuya Masuda, Fumito Tani, Naofumi KitabatakeAbstract:Abstract Thaumatin, an intensely sweet-tasting protein, elicits a sweet-taste sensation at a level as low as 50 nM. Although previous sensory analyses have suggested that Lys67 and Arg82 are important to the Sweetness of thaumatin, the exact effects of each residue on sweet receptors are still unknown. In the present study, various mutants of thaumatin altered at Arg82 as well as Lys67 were prepared and their Sweetness levels were quantitatively evaluated by cell-based assays using HEK293 cells expressing human sweet receptors. Mutations at Arg82 had a more deteriorative effect on Sweetness than mutations at Lys67. Particularly, a charge inversion at Arg82 (R82E) resulted in an abolishment of the response to sweet receptors even at a concentration as high as 1 mM. These results indicate that Arg82 plays a central role in determining the Sweetness of thaumatin. A strict spatial charge location at residue 82 appears to be required for interaction with sweet receptors.
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interactions of the sweet tasting proteins thaumatin and lysozyme with the human sweet taste receptor
Journal of Agricultural and Food Chemistry, 2009Co-Authors: Eriko Sato, Keisuke Ohta, Tetsuya Masuda, Naofumi KitabatakeAbstract:This study investigated the Sweetness of the sweet-tasting protein thaumatin and lysozyme by both an in vitro cell-based assay and an in vivo sensory analysis to elucidate the differences between in vitro and in vivo response profiles. Hek293 cells were constructed that stably expressed the human T1R2+T1R3 sweet-taste receptor, and their responses to thaumatin and lysozyme were analyzed by monitoring the levels of intracellular cAMP. The results indicated that thaumatin and lysozyme as well as aspartame induced a decrease in the intracellular cAMP accumulation of the T1R2+T1R3-transfected cells and that EC50 values of thaumatin and lysozyme determined by cell-based assay are well-consistent with the results of the Sweetness threshold value determined by sensory analysis in the presence of 140 mM NaCl. The results of both in vitro and in vivo experiments confirmed that the Sweetness inhibitor lactisole significantly suppressed the Sweetness of thaumatin and lysozyme.
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critical molecular regions for elicitation of the Sweetness of the sweet tasting protein thaumatin i
FEBS Journal, 2008Co-Authors: Keisuke Ohta, Tetsuya Masuda, Naofumi KitabatakeAbstract:Thaumatin is an intensely sweet-tasting protein. To identify the critical amino acid residue(s) responsible for elicitation of the Sweetness of thaumatin, we prepared mutant thaumatin proteins, using Pichia pastoris, in which alanine residues were substituted for lysine or arginine residues, and the Sweetness of each mutant protein was evaluated by sensory analysis in humans. Four lysine residues (K49, K67, K106 and K163) and three arginine residues (R76, R79 and R82) played significant roles in thaumatin Sweetness. Of these residues, K67 and R82 were particularly important for eliciting the Sweetness. We also prepared two further mutant thaumatin I proteins: one in which an arginine residue was substituted for a lysine residue, R82K, and one in which a lysine residue was substituted for an arginine residue, K67R. The threshold value for Sweetness was higher for R82K than for thaumatin I, indicating that not only the positive charge but also the structure of the side chain of the arginine residue at position 82 influences the Sweetness of thaumatin, whereas only the positive charge of the K67 side chain affects Sweetness.
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Sweetness and enzymatic activity of lysozyme.
Journal of Agricultural and Food Chemistry, 2001Co-Authors: Tetsuya Masuda, Yuki Ueno, Naofumi KitabatakeAbstract:Hen egg lysozyme elicits a sweet taste sensation for human beings. Effects of reduction of disulfide bonds, heat treatment, and chemical modification of hen egg lysozyme on both Sweetness and hydrolytic activity were investigated. Both the Sweetness and enzymatic activities were lost when the intradisulfide linkage in a lysozyme molecule was reduced and S-3-(trimethylated amino) propylated. The Sweetness and enzymatic activity of lysozyme were lost on heating at 95 °C for 18 h. These facts suggest that tertiary structures of lysozyme are indispensable for eliciting a sweet taste as well as enzymatic activity. Although the modification of carboxyl residues in a lysozyme by glycine methylester or aminomethansulfonic acid resulted in the loss of enzymatic activity by blocking the catalytic residues, the Sweetness was fully retained. These results indicate that the Sweetness of lysozyme was independent of its enzymatic activity. The lysozyme purified from goose egg white similarly elicited a sweet taste, alth...
Sophie Nicklaus - One of the best experts on this subject based on the ideXlab platform.
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Assessment of liking for saltiness, Sweetness and fattiness sensations in children: Validation of a questionnaire
Food Quality and Preference, 2018Co-Authors: Christine Lange, Claire Chabanet, Rachel Schoumacker, Wen Lun Yuan, Amélie Deglaire, Blandine De Lauzon-guillain, Sophie NicklausAbstract:The objective of this study was to perform an internal validation of a questionnaire assessing 7–12 years old children’s liking for saltiness, Sweetness and fattiness in foods. An 83-item questionnaire validated in adults was adapted for children via vocabulary adaptation, picture addition and removal of little known or consumed items. It was launched online, and a paper version was also available. The construct validity was evaluated in 500 French children aged 7–12 y. An exploratory factor analysis (EFA) was performed to identify the factor structure within each sensation. The adult liking factor structure was also tested on the children’s data to compare the factor structures between adults and children. A confirmatory factor analysis (CFA) was performed to validate the factor structure. Finally, a bootstrap analysis was performed to ensure the stability of the structure. Liking for saltiness, Sweetness, fattiness-and-saltiness and fattiness-and-Sweetness sensations showed meaningful factor structures. After the deletion of some items, a one-factor structure was identified for the liking for saltiness (9 items), and multiple-factor structures were identified for the liking for Sweetness (16 items), fattiness-and-saltiness (22 items), and fattiness-and-Sweetness (16 items). A fattiness model was estimated based on two subscales, the fattiness-and-saltiness and fattiness-and-Sweetness subscales. This self-administered questionnaire, available on line or on paper, enables the creation of a factor structure for saltiness, Sweetness, fattiness-and-saltiness, fattiness-and-Sweetness, and fattiness liking in children. This questionnaire represents the first self-administered tool designed to assess children’s liking for Sweetness, saltiness and fattiness sensations in large cohorts.
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The development of basic taste sensitivity and preferences in children
Appetite, 2018Co-Authors: Frida Felicia Fry Vennerød, Sophie Nicklaus, Nanna Lien, Valérie L. AlmliAbstract:This study aims at understanding how preference and sensitivity to the basic tastes develop in the preschool years, and how the two relate to each other. To expand on the existing literature regarding taste preferences conducted in cross-sectional studies, a longitudinal design was applied with children from age four to six years old. During the springs of 2015, 2016, and 2017, 131 children born in 2011 were tested in their kindergartens. To investigate preferences for sweet, sour and bitter tastes, the children performed ranking-by-elimination procedures on fruit-flavored beverages and chocolates with three taste intensity levels. The beverages varied in either sucrose, citric acid, or the bitter component isolone. The chocolates varied in the bitter component theobromine from cocoa and sucrose content. Each year, the children also performed paired-comparison tasks opposing plain water to tastant dilutions at four concentrations. The stimuli consisted of the five basic tastes: sweet (sucrose) sour (citric acid monohydrate) umami (monosodium glutamate), salty (sodium chloride), and bitter (quinine hydrochloride dihydrate). Preference for Sweetness levels increased with age, while preference for bitterness and sourness levels were stable. Concerning taste sensitivity, the children showed an increase in sensitivity for sourness and saltiness, a decrease for Sweetness, and stability for umami and bitterness. A negative association was found between Sweetness sensitivity and preference for Sweetness. The study highlights different trajectories of sensitivity and preferences across tastes. On average, a reduction in Sweetness sensitivity combined with an increase in preference for higher Sweetness was observed from the age of four to six. The weak relationship between taste sensitivity and taste preference in our data suggests that taste preference development is shaped by a multitude of factors in addition to taste sensitivity.
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How do infants react to Sweetness before the age of two? How is it different for the other primary tastes?
2017Co-Authors: Camille Schwartz, Claire Chabanet, Emilie Szleper, Valérie Feyen, Sylvie Issanchou, Sophie NicklausAbstract:How do infants react to Sweetness before the age of two? How is it different for the other primary tastes?. ILSI Europe Workshop “Dietary Sweetness, is it an issue
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Relation between sweet food consumption and liking for sweet taste in French children
Food Quality and Preference, 2017Co-Authors: Camille Divert, Chantal Martin, Christine Lange, Claire Chabanet, Rachel Schoumacker, Sophie NicklausAbstract:Given the growing evidence that sugar intake could promote a positive energy balance and lead to weight gain and obesity, the World Health Organization published new recommendations in terms of sugar consumption in children and adults. However, the influence of sweet food and drink consumption on Sweetness liking has not been fully characterized. Therefore, the present study aimed at exploring whether sweet food consumption is positively associated with Sweetness liking in 101 children aged between 7 and 12 years. Sweetness 'preference' and liking optima for Sweetness (calculated for 100% and 60% of the children, respectively) were measured by asking the children to taste and rate on a 9-point hedonic scale three ranges of food products that varied in sucrose content. Each range of products (sugar water, strawberry syrup with water, and cornflakes in milk) contained 5 levels of Sweetness. Sweet food consumption from sweet drinks, candies and snacks, cereal/dairy/fruit products or added sugar were calculated using data from a food frequency questionnaire which focused on the children's consumption of sweet products, taking into account the Sweetness intensity of each food. Structural Equation Modelling fitted for the 101 children showed a weak but significant positive association between candy and snack consumption and Sweetness liking (path coefficient = 0.28; p = 0.04). However, Sweetness liking was not associated with sweet drink consumption, cereal/dairy/fruit product consumption or added sugar consumption. The absence of a clear relationship between sweet food consumption and Sweetness liking in this sample calls for further clarifications on the potential effect of sweet food consumption on preferred Sweetness level in liquid and solid foods.
Keisuke Ohta - One of the best experts on this subject based on the ideXlab platform.
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introduction of a negative charge at arg82 in thaumatin abolished responses to human t1r2 t1r3 sweet receptors
Biochemical and Biophysical Research Communications, 2011Co-Authors: Keisuke Ohta, Tetsuya Masuda, Fumito Tani, Naofumi KitabatakeAbstract:Abstract Thaumatin, an intensely sweet-tasting protein, elicits a sweet-taste sensation at a level as low as 50 nM. Although previous sensory analyses have suggested that Lys67 and Arg82 are important to the Sweetness of thaumatin, the exact effects of each residue on sweet receptors are still unknown. In the present study, various mutants of thaumatin altered at Arg82 as well as Lys67 were prepared and their Sweetness levels were quantitatively evaluated by cell-based assays using HEK293 cells expressing human sweet receptors. Mutations at Arg82 had a more deteriorative effect on Sweetness than mutations at Lys67. Particularly, a charge inversion at Arg82 (R82E) resulted in an abolishment of the response to sweet receptors even at a concentration as high as 1 mM. These results indicate that Arg82 plays a central role in determining the Sweetness of thaumatin. A strict spatial charge location at residue 82 appears to be required for interaction with sweet receptors.
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Introduction of a negative charge at Arg82 in thaumatin abolished responses to human T1R2–T1R3 sweet receptors
Biochemical and Biophysical Research Communications, 2011Co-Authors: Keisuke Ohta, Tetsuya Masuda, Fumito Tani, Naofumi KitabatakeAbstract:Abstract Thaumatin, an intensely sweet-tasting protein, elicits a sweet-taste sensation at a level as low as 50 nM. Although previous sensory analyses have suggested that Lys67 and Arg82 are important to the Sweetness of thaumatin, the exact effects of each residue on sweet receptors are still unknown. In the present study, various mutants of thaumatin altered at Arg82 as well as Lys67 were prepared and their Sweetness levels were quantitatively evaluated by cell-based assays using HEK293 cells expressing human sweet receptors. Mutations at Arg82 had a more deteriorative effect on Sweetness than mutations at Lys67. Particularly, a charge inversion at Arg82 (R82E) resulted in an abolishment of the response to sweet receptors even at a concentration as high as 1 mM. These results indicate that Arg82 plays a central role in determining the Sweetness of thaumatin. A strict spatial charge location at residue 82 appears to be required for interaction with sweet receptors.
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interactions of the sweet tasting proteins thaumatin and lysozyme with the human sweet taste receptor
Journal of Agricultural and Food Chemistry, 2009Co-Authors: Eriko Sato, Keisuke Ohta, Tetsuya Masuda, Naofumi KitabatakeAbstract:This study investigated the Sweetness of the sweet-tasting protein thaumatin and lysozyme by both an in vitro cell-based assay and an in vivo sensory analysis to elucidate the differences between in vitro and in vivo response profiles. Hek293 cells were constructed that stably expressed the human T1R2+T1R3 sweet-taste receptor, and their responses to thaumatin and lysozyme were analyzed by monitoring the levels of intracellular cAMP. The results indicated that thaumatin and lysozyme as well as aspartame induced a decrease in the intracellular cAMP accumulation of the T1R2+T1R3-transfected cells and that EC50 values of thaumatin and lysozyme determined by cell-based assay are well-consistent with the results of the Sweetness threshold value determined by sensory analysis in the presence of 140 mM NaCl. The results of both in vitro and in vivo experiments confirmed that the Sweetness inhibitor lactisole significantly suppressed the Sweetness of thaumatin and lysozyme.
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critical molecular regions for elicitation of the Sweetness of the sweet tasting protein thaumatin i
FEBS Journal, 2008Co-Authors: Keisuke Ohta, Tetsuya Masuda, Naofumi KitabatakeAbstract:Thaumatin is an intensely sweet-tasting protein. To identify the critical amino acid residue(s) responsible for elicitation of the Sweetness of thaumatin, we prepared mutant thaumatin proteins, using Pichia pastoris, in which alanine residues were substituted for lysine or arginine residues, and the Sweetness of each mutant protein was evaluated by sensory analysis in humans. Four lysine residues (K49, K67, K106 and K163) and three arginine residues (R76, R79 and R82) played significant roles in thaumatin Sweetness. Of these residues, K67 and R82 were particularly important for eliciting the Sweetness. We also prepared two further mutant thaumatin I proteins: one in which an arginine residue was substituted for a lysine residue, R82K, and one in which a lysine residue was substituted for an arginine residue, K67R. The threshold value for Sweetness was higher for R82K than for thaumatin I, indicating that not only the positive charge but also the structure of the side chain of the arginine residue at position 82 influences the Sweetness of thaumatin, whereas only the positive charge of the K67 side chain affects Sweetness.
Tetsuya Masuda - One of the best experts on this subject based on the ideXlab platform.
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introduction of a negative charge at arg82 in thaumatin abolished responses to human t1r2 t1r3 sweet receptors
Biochemical and Biophysical Research Communications, 2011Co-Authors: Keisuke Ohta, Tetsuya Masuda, Fumito Tani, Naofumi KitabatakeAbstract:Abstract Thaumatin, an intensely sweet-tasting protein, elicits a sweet-taste sensation at a level as low as 50 nM. Although previous sensory analyses have suggested that Lys67 and Arg82 are important to the Sweetness of thaumatin, the exact effects of each residue on sweet receptors are still unknown. In the present study, various mutants of thaumatin altered at Arg82 as well as Lys67 were prepared and their Sweetness levels were quantitatively evaluated by cell-based assays using HEK293 cells expressing human sweet receptors. Mutations at Arg82 had a more deteriorative effect on Sweetness than mutations at Lys67. Particularly, a charge inversion at Arg82 (R82E) resulted in an abolishment of the response to sweet receptors even at a concentration as high as 1 mM. These results indicate that Arg82 plays a central role in determining the Sweetness of thaumatin. A strict spatial charge location at residue 82 appears to be required for interaction with sweet receptors.
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Introduction of a negative charge at Arg82 in thaumatin abolished responses to human T1R2–T1R3 sweet receptors
Biochemical and Biophysical Research Communications, 2011Co-Authors: Keisuke Ohta, Tetsuya Masuda, Fumito Tani, Naofumi KitabatakeAbstract:Abstract Thaumatin, an intensely sweet-tasting protein, elicits a sweet-taste sensation at a level as low as 50 nM. Although previous sensory analyses have suggested that Lys67 and Arg82 are important to the Sweetness of thaumatin, the exact effects of each residue on sweet receptors are still unknown. In the present study, various mutants of thaumatin altered at Arg82 as well as Lys67 were prepared and their Sweetness levels were quantitatively evaluated by cell-based assays using HEK293 cells expressing human sweet receptors. Mutations at Arg82 had a more deteriorative effect on Sweetness than mutations at Lys67. Particularly, a charge inversion at Arg82 (R82E) resulted in an abolishment of the response to sweet receptors even at a concentration as high as 1 mM. These results indicate that Arg82 plays a central role in determining the Sweetness of thaumatin. A strict spatial charge location at residue 82 appears to be required for interaction with sweet receptors.
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interactions of the sweet tasting proteins thaumatin and lysozyme with the human sweet taste receptor
Journal of Agricultural and Food Chemistry, 2009Co-Authors: Eriko Sato, Keisuke Ohta, Tetsuya Masuda, Naofumi KitabatakeAbstract:This study investigated the Sweetness of the sweet-tasting protein thaumatin and lysozyme by both an in vitro cell-based assay and an in vivo sensory analysis to elucidate the differences between in vitro and in vivo response profiles. Hek293 cells were constructed that stably expressed the human T1R2+T1R3 sweet-taste receptor, and their responses to thaumatin and lysozyme were analyzed by monitoring the levels of intracellular cAMP. The results indicated that thaumatin and lysozyme as well as aspartame induced a decrease in the intracellular cAMP accumulation of the T1R2+T1R3-transfected cells and that EC50 values of thaumatin and lysozyme determined by cell-based assay are well-consistent with the results of the Sweetness threshold value determined by sensory analysis in the presence of 140 mM NaCl. The results of both in vitro and in vivo experiments confirmed that the Sweetness inhibitor lactisole significantly suppressed the Sweetness of thaumatin and lysozyme.
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critical molecular regions for elicitation of the Sweetness of the sweet tasting protein thaumatin i
FEBS Journal, 2008Co-Authors: Keisuke Ohta, Tetsuya Masuda, Naofumi KitabatakeAbstract:Thaumatin is an intensely sweet-tasting protein. To identify the critical amino acid residue(s) responsible for elicitation of the Sweetness of thaumatin, we prepared mutant thaumatin proteins, using Pichia pastoris, in which alanine residues were substituted for lysine or arginine residues, and the Sweetness of each mutant protein was evaluated by sensory analysis in humans. Four lysine residues (K49, K67, K106 and K163) and three arginine residues (R76, R79 and R82) played significant roles in thaumatin Sweetness. Of these residues, K67 and R82 were particularly important for eliciting the Sweetness. We also prepared two further mutant thaumatin I proteins: one in which an arginine residue was substituted for a lysine residue, R82K, and one in which a lysine residue was substituted for an arginine residue, K67R. The threshold value for Sweetness was higher for R82K than for thaumatin I, indicating that not only the positive charge but also the structure of the side chain of the arginine residue at position 82 influences the Sweetness of thaumatin, whereas only the positive charge of the K67 side chain affects Sweetness.
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Sweetness and enzymatic activity of lysozyme.
Journal of Agricultural and Food Chemistry, 2001Co-Authors: Tetsuya Masuda, Yuki Ueno, Naofumi KitabatakeAbstract:Hen egg lysozyme elicits a sweet taste sensation for human beings. Effects of reduction of disulfide bonds, heat treatment, and chemical modification of hen egg lysozyme on both Sweetness and hydrolytic activity were investigated. Both the Sweetness and enzymatic activities were lost when the intradisulfide linkage in a lysozyme molecule was reduced and S-3-(trimethylated amino) propylated. The Sweetness and enzymatic activity of lysozyme were lost on heating at 95 °C for 18 h. These facts suggest that tertiary structures of lysozyme are indispensable for eliciting a sweet taste as well as enzymatic activity. Although the modification of carboxyl residues in a lysozyme by glycine methylester or aminomethansulfonic acid resulted in the loss of enzymatic activity by blocking the catalytic residues, the Sweetness was fully retained. These results indicate that the Sweetness of lysozyme was independent of its enzymatic activity. The lysozyme purified from goose egg white similarly elicited a sweet taste, alth...
Markus Stieger - One of the best experts on this subject based on the ideXlab platform.
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Combinatory Effects of Texture and Aroma Modification on Taste Perception of Model Gels
Chemosensory Perception, 2013Co-Authors: Janine Editha Knoop, Guido Sala, Gerrit Smit, Markus StiegerAbstract:In this study, the effects of texture modification and aroma-induced Sweetness enhancement were systematically investigated in apple-flavored semi-solid Na-caseinate gels. Gels containing apple juice as a basic flavor were developed differing in stiffness, brittleness and serum release (texture modification), aroma, and sugar concentration (flavor modification). In a full factorial design (2 × 2 × 2), eight samples were evaluated by a sensory panel on ten attributes (five texture, five flavor). Sweetness was enhanced significantly by modification of texture, aroma, and sugar concentration. Texture modification was found to be by far the greatest contributor to overall Sweetness. In comparison to texture modifications, aroma modification and changes of sugar concentration resulted only in small Sweetness enhancement. When texture and aroma modifications are combined, a small additive effect of aroma modification on Sweetness enhancement was found in addition to the Sweetness enhancement caused by texture modification. This suggests that the relationship between texture (modification) and flavor (modification) and Sweetness is additive in a nonlinear manner. It can be concluded that texture modification is a valid tool to enhance taste intensity. Hence, texture modification can compensate for a loss of sweet taste intensity induced by sugar reduction, while aroma-induced Sweetness enhancement can contribute to further taste enhancement in order to develop healthier products.
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effect of gel texture and sucrose spatial distribution on Sweetness perception
Lwt - Food Science and Technology, 2012Co-Authors: Ana Carolina Mosca, Johannes H F Bult, Fred Van De Velde, Martinus A J S Van Boekel, Markus StiegerAbstract:Abstract Layered gels differing in mechanical and breakdown properties (soft, medium and hard gels) and in the distribution of sucrose in the matrix (homogeneous and inhomogeneous distributions) were used to investigate the effects of texture and spatial distribution of sucrose on Sweetness perception. Rating tests, 2-Alternative forced choice tests and time-intensity analysis were performed to compare the Sweetness of soft, medium and hard gels with homogeneous and inhomogeneous distributions of sucrose. Results showed that all gels with an inhomogeneous distribution of sucrose were perceived sweeter than gels in which sucrose was homogeneously distributed. This indicates that the enhancement of Sweetness by an inhomogeneous distribution of sucrose does not depend on the texture of the gel matrix. Furthermore, the time-intensity profiling showed that soft gels, which had low values of fracture strain and fracture stress and broke down in a large number of small fragments upon chewing, had the highest Sweetness intensity. The time required to reach the maximum Sweetness intensity tended to be shorter in soft gels. These findings suggest that the breakdown behavior of the gel matrix during oral processing affects the perception of Sweetness of layered gels.
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enhancement of Sweetness intensity in gels by inhomogeneous distribution of sucrose
Food Quality and Preference, 2010Co-Authors: Ana Carolina Mosca, Fred Van De Velde, Johannes H F Bult, Martinus A J S Van Boekel, Markus StiegerAbstract:Model systems consisting of layers of mixed agar/gelatin gel were used to investigate the effect of the spatial distribution of sucrose on perceived Sweetness intensity. 2-Alternative forced choice tests were performed with consumers to compare the Sweetness of layered samples with an inhomogeneous distribution of sucrose to the Sweetness of a reference sample with a homogeneous distribution. All samples had the same overall sucrose concentration (10%) and similar mechanical and rheological properties. Inhomogeneous samples that had large concentration gradients of sucrose between layers were perceived sweeter than the homogeneous reference. No differences in Sweetness were observed between the reference and samples with small concentration gradients of sucrose. Additionally, the position of the layers containing sucrose did not affect Sweetness. Results showed that an inhomogeneous distribution of sucrose can be used to reduce sucrose content by 20% without a decrease in Sweetness intensity.