Dataset Information

Taste Detection of Maltooligosaccharides with Varying Degrees of Polymerization.

ABSTRACT: Previous studies have shown that humans can taste maltooligosaccharides [MOS; degree of polymerization (DP) of 3-20] but not maltopolysaccharides (MPS; DP of >20) and that their taste detection is independent of the canonical sweet taste receptor. The objectives of this study were to determine the DP ranges of target stimuli that are tasted and further to investigate the impact of DP on taste detectability. To achieve this goal, we prepared three food-grade MOS samples with narrow DP ranges using flash chromatography: low (4-6), medium (7-12), and high (14-21) DP samples. Following sample preparation, we asked subjects to discriminate the MOS stimuli from blanks after the stimuli were swabbed on the tip of tongue. All stimuli were initially presented at 75 mM. Acarbose, an α-glucosidase inhibitor, was added to all stimuli, including blanks, to prevent oral hydrolysis of MOS. After determining that all three MOS samples were detected at a significant degree, we conducted follow-up studies to explore whether the detection of these samples differed at a range of concentrations (18-56 mM). The results showed that detection rates of medium- and high-DP MOS varied in a concentration-dependent manner (p < 0.05). In contrast, low-DP MOS showed a consistent detection rate across concentrations tested. These results demonstrate that humans can taste MOS stimuli of all chain lengths and that relative taste detection rates are generally similar across MOS with varying chain lengths.

SUBMITTER: Martin LE

PROVIDER: S-EPMC10561598 | biostudies-literature | 2023 May

REPOSITORIES: biostudies-literature

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Publications

Taste Detection of Maltooligosaccharides with Varying Degrees of Polymerization.

Martin Laura E LE Andrewson Toren S TS Penner Michael H MH Lim Juyun J

Journal of agricultural and food chemistry 20230421 17

Previous studies have shown that humans can taste maltooligosaccharides [MOS; degree of polymerization (DP) of 3-20] but not maltopolysaccharides (MPS; DP of >20) and that their taste detection is independent of the canonical sweet taste receptor. The objectives of this study were to determine the DP ranges of target stimuli that are tasted and further to investigate the impact of DP on taste detectability. To achieve this goal, we prepared three food-grade MOS samples with narrow DP ranges usin ...[more]

PMID: 37083361

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Project description:Replication protein A (RPA) is known to interact with guanine- (G-) rich sequences that adopt G-quadruplex (GQ) structures. Most studies reported in the literature were performed on GQ formed by homogeneous sequences, such as the human telomeric repeat, and RPA's ability to unfold GQ structures of differing stability is not known. We compared the thermal stability of three potential GQ-forming DNA sequences (PQSs) to their stability against RPA-mediated unfolding using single-molecule fluorescence resonance energy transfer (FRET) and bulk biophysical and biochemical experiments. One of these sequences is the human telomeric repeat and the other two, located in the promoter region of tyrosine hydroxylase gene, are highly heterogeneous sequences that better represent PQSs in the genome. The three GQ constructs have thermal stabilities that differ significantly. Our measurements showed that the most thermally stable structure (Tm = 86 °C) was also the most stable against RPA-mediated unfolding, although the least thermally stable structure (Tm = 69 °C) had at least an order-of-magnitude higher stability against RPA-mediated unfolding than the structure with intermediate thermal stability (Tm = 78 °C). The significance of this observation becomes more evident when considered within the context of the cellular environment where protein-DNA interactions can be an important determinant of GQ viability. Considering these results, we conclude that thermal stability is not necessarily an adequate criterion for predicting the physiological viability of GQ structures. Finally, we measured the time it takes for an RPA molecule to unfold a GQ from a fully folded to a fully unfolded conformation using a single-molecule stopped-flow method. All three GQ structures were unfolded within Δt ≈ 0.30 ± 0.10 s, a surprising result considering that the unfolding time does not correlate with thermal stability or stability against RPA-mediated unfolding. These results suggest that the limiting step in G-quadruplex unfolding by RPA is simply the accessibility of the structure to the RPA protein.

Dataset Information

Taste Detection of Maltooligosaccharides with Varying Degrees of Polymerization.

Publications

Taste Detection of Maltooligosaccharides with Varying Degrees of Polymerization.

Similar Datasets

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