Bitter Amino Acids Beef Amino Acids
Nutrients. 2019 Sep; 11(9): 2166.
Glycated Beef Protein Hydrolysates as Sources of Bitter Taste Modifiers
Chunlei Zhang
1Department of Food and Human being Nutritional Sciences, University of Manitoba, Winnipeg, MB R3T 2N2, Canada
Adeola Yard. Alashi
1Department of Food and Homo Nutritional Sciences, University of Manitoba, Winnipeg, MB R3T 2N2, Canada
Nisha Singh
2Manitoba Chemosensory Biology Enquiry Grouping, Department of Oral Biology, Academy of Manitoba, Children'due south Hospital Enquiry Constitute of Manitoba (CHRIM), Winnipeg, MB R3E 0W4, Canada
Prashen Chelikani
iiManitoba Chemosensory Biological science Research Grouping, Section of Oral Biology, University of Manitoba, Children'southward Infirmary Research Institute of Manitoba (CHRIM), Winnipeg, MB R3E 0W4, Canada
Rotimi Eastward. Aluko
aneDepartment of Nutrient and Human being Nutritional Sciences, Academy of Manitoba, Winnipeg, MB R3T 2N2, Canada
Received 2019 Aug 8; Accustomed 2019 Sep 5.
Abstract
Beingness averse to bitter taste is a common phenomenon for humans and other animals, which requires the pharmaceutical and food industries to source compounds that tin block bitterness intensity and increase consumer acceptability. In this piece of work, beef protein alcalase hydrolysates (BPAH) and chymotrypsin hydrolysates (BPCH) were reacted with glucose to initiate Maillard reactions that led to the formation of glycated or advanced glycation cease products (AGEs), BPAH-AGEs and BPCH-AGEs, respectively. The caste of glycation was higher for the BPAH-AGEs (47–55%) than the BPCH-AGEs (30–38%). Analysis by an electronic tongue instrument showed that BPAH-AGEs and BPCH-AGEs had bitterness scores that were significantly (p < 0.05) less than quinine. The addition of BPAH-AGEs or BPCH-AGEs to quinine led to significant (p < 0.05) reductions (up to 38%) in bitterness intensity of quinine. The employ of 3% hydrolysate to react with glucose yielded glycated peptides with a stronger ability to reduce quinine bitterness than when 1% was used. Calcium release from HEK293T cells stably expressing the T2R4 human bitter taste receptor was significantly (p < 0.05) attenuated by BPAH-AGEs (upwardly to 96%) and BPCH-AGEs (up to 92%) when compared to the BPAH (62%) and BPCH (3%) or quinine (0%). We concluded that BPAH-AGEs and BPCH-AGEs may be used as bitter taste blockers to codify better tasting foods.
Keywords: beef, protein hydrolysate, advanced glycation terminate products, Maillard reaction, electronic tongue, bitterness intensity, quinine, T2R4
ane. Introduction
Subsequently the discovery of 25 biting sense of taste receptors and intensive efforts to elucidate the activation mechanisms of these receptors, the search for biting sense of taste modulators that tin specifically block bitter sense of taste receptors has gained increasing attention. So far, at that place are a few bitter taste inhibitors (γ-aminobutryic acid, Nα,Nα-bis(carboxymethyl)-L-lysine, homoeriodictyol and 4-(2,2,3-trimethylcyclopentyl)butanoic acid, probenecid, 6-Methoxylflavanones) that accept been reported to act through interactions with bitter taste receptors [one,two,three,4,v,6]. Among them, Northward, N-bis(carboxymethyl)-50-lysine (BCML) is a derivative of the advanced glycation finish product (AGE) chosen carboxymethyl-lysine (CML), which inhibits quinine-dependent activation of bitter sense of taste receptor iv (T2R4) with an IC50 value of 59 ± eighteen nM [2]. Interestingly, CML inhibited quinine-activated T2R4 with an ICfifty of 32.62 ± ix.v µM; in contrast, it activated T2R20 with an ECl of 65.31 ± 17.79 µM [7].
AGEs are a heterogeneous group of compounds generated from non-enzymatic reactions between the carbonyl grouping of a reducing sugar and an amino group of a poly peptide, which is termed the Maillard reaction. The reaction process includes three stages, which are initiation, propagation and an advanced stage. The early on glycation and oxidation processes form Schiff bases and Amadori products while farther glycation of amino groups of peptides or proteins results in molecular rearrangements that lead to the generation of AGEs. The types and yields of final products are attributed to the selected reducing sugar types, pH, temperature, and heating fourth dimension [8]. The process of Age formation leads to the production of reactive oxygen species (ROS), which are believed to be deleterious to human being health and contribute to several chronic diseases, such as diabetes, cardiovascular affliction, neurodegenerative illness, and chronic kidney affliction (CKD) [9,10]. Nevertheless, peptides from soy protein and milk protein after the Maillard reaction were shown to possess enhanced antioxidant activity [11,12].
In improver to the aforementioned effects, AGEs are as well undoubtedly important substances for generating a unique smell and taste for thermally processed foods. For example, 4-hydroxy-2 (or5)-ethyl-5(or2)-methyl-three(2H)-furanone, 2-hy-droxy-3-methyl-2-cyclopenten-i-one, and three-hydroxyl-4,5-dimethyl-2(5H)-furanone were reported to enhance the sweetness perception of sugar [13,14]. Moreover, the biting gustation intensity of casein peptide-derived AGEs decreased later 3 h heating, compared to heating casein peptides alone for 12 h [xv]. Information technology was also reported that Maillard reaction products of soy poly peptide hydrolysates exhibited strong caramel-like odor and had a notably weaker bitter sense of taste [eleven]. Recently nosotros showed two AGEs, glyoxal-derived lysine dimer (GOLD) and CML were ligands of the biting taste receptors that acquired either activation (T2R20) or inhibition (T2R4) [7].
Meat has multiple proteins [16] and enzymatic hydrolysis offers the possibility of generating a wide range of peptides that have a desirable function equally modifiers of bitter gustation [5]. Alcalase has been commonly used to hydrolyze proteins considering of its wide substrate specificity [17]. Alcalase has been extensively reported to improve food flavor, including Chinese sausage, soy protein isolates, xanthous tuna and lean beef [17,18,xix,xx]. Additionally, beef protein alcalase hydrolysates (BPAH) and chymotrypsin hydrolysates (BPCH) have been demonstrated to have biting taste-suppressing ability with confirmed activeness at the taste receptor level [21]. Based on the demonstrated weaker bitter gustatory modality of certain Maillard reaction products [11], we hypothesized that glycation of beef protein hydrolysates would generate compounds that could negatively modulate the normal functions of T2R4, ane of the most studied human being bitter taste receptors. Therefore, in this study, BPAH and BPCH were reacted with glucose to produce AGEs and this was followed by the determination of their effect on T2R4 in jail cell-based calcium mobilization assays.
two. Materials and Methods
ii.i. Materials
Basis beef was bought from the local market (Safeway, Winnipeg, MB, Canada). D-glucose, chymotrypsin® (from bovine pancreas, EC 3.4.21.1) and Alcalase® (from fermentation of Bacillus licheniformis, EC 3.iv.21.62) were purchased from Sigma-Aldrich (St. Louis, MO, USA). BPAH and BPCH were produced as previously described [21].
2.2. Maillard Reaction
The Maillard reaction was carried out based on the protocol reported past Dong et al. [fifteen]. Previously prepared BPAH and BPCH at concentrations of 1% and 3% (w/v) were each mixed with 100, 200, 300, 400, or 500 mM D-glucose in phosphate buffer, pH ten. The mixtures were heated at 120 °C in an oven for thirty min followed by rapid cooling in water ice water then freeze drying. In order to extract water soluble AGEs, 2 m of dried glycated hydrolysates were mixed with 50 mL water and fifty mL ethanol for 2 h at room temperature with continuous stirring. The mixture was then centrifuged (3270 thousand at 4 °C) for thirty min and the resulting supernatant nerveless while the residue was used to repeat the extraction procedure. Finally, the supernatants were pooled and evaporated using the vacuum rotary evaporator maintained at a temperature range between 35 and 45 °C. The concentrated supernatant was filtered through a 0.2 μm disc to remove insoluble materials and and then freeze dried.
ii.3. Degree of Glycation (DG)
Based on previous reports [22,23], the O-phthalic aldehyde method was used to determine the contents of gratis amino groups (FAG) of the BPAH and BPCH and their AGEs. The DG was calculated co-ordinate to the following equation:
2.four. Interpretation of Bitter Scores by Electronic Tongue
Diagnostic solutions including 0.one K HCl, 0.1 Thou NaCl and 0.1 M monosodium glutamate (MSG) as well every bit the calibration solution (one M HCl) were purchased from Alpha Chiliad.O.S (Toulouse, France). Known bitter score substances such as acetaminophen, caffeine monohydrate, quinine hydrochloride, leporamide hydrochloride and femotidine were purchased from MP Biomedicals (Solon, OH, Usa). Each freeze-dried AGE sample was dissolved in distilled water to requite 0.v, 1.0, ii.0, 5.0 and 10.0 mg/mL concentrations followed by filtration first through a 0.45 μm polytetrafluorethylene (PTFE) filter disc and then a 0.2 μm PTFE filter. Bitter scores of AGEs were evaluated using the Astree Two eastward-Tongue organisation (Alpha M.O.S., Toulouse, French republic). This system is a completely automatic taste analyzer equipped with seven sensors, BD, EB, JA, JG, KA, OA, and JE, based on the ChemFET engineering science (Chemic modified Field Effect Transistor) to analyze liquid samples [24]. Firstly, 0.01 M HCl was used to status and calibrate the sensors and the reference electrode repeatedly until stable signals were obtained for all seven sensors with minimal or no racket and migrate. Secondly, the diagnostic procedure was performed repeatedly, using 0.1 Grand HCl, NaCl, and MSG to ensure the sensors could identify distinctive tastes, until the discrimination index accomplished at least 0.94 on a principle component analysis (PCA) map. Post-obit this, the bitter scores of AGEs were detected using 5 mg/mL, which was the minimum amount of sample that provided the required chemical signal on the instrument. The biting scores were so projected using the bitterness standard partial least square (PLS) regression model of the instrument. The PLS bitterness standard model was constructed from several biting taste compounds (caffeine, quinine, prednisolone, paracetamol, loperamide and famotidine) with known bitter taste scores that were determined by man panelists [24]. The specific concentrations are shown in Tabular array 1.
Table 1
Compounds with known bitter scores from a human sensory analysis panel *.
| Compounds | Used to Build Bitterness Standard Model | Used to Validate Bitterness Standard Model | Concentration (mM) | Published Values |
|---|---|---|---|---|
| Caffeine | √ | 0.24 2.36 | 2.5 8.5 | |
| Quinine | √ | 0.03 0.12 | 9 15.five | |
| Prednisolone | √ | 0.44 0.88 | 13.5 17 | |
| Paracetamol | √ | 3.31 19.85 | 4 11 | |
| Loperamide | √ | 0.002 0.01 | 7.5 xiv | |
| Famotidine | √ | 0.06 0.15 | 4.two nine |
2.five. Determination of Calcium Mobilization
Conclusion of the ability of AGEs to actuate or block T2R4 was carried out by measuring intracellular Catwo+ mobilization using a Fluo-four NW calcium assay kit [21]. Stable transfected HEK293T cells expressing T2R4 and K-alpha xvi/44 or HEK293T expressing only K-alpha sixteen/44 were used every bit experimental and control groups, respectively. A viable cell count was taken afterwards 6–8 h of transfection, and approximately 1 × xv viable cells/well were plated in the 96-well clear bottom black-walled BD falcon biolux plates, which were then incubated at 37 °C in a CO2 incubator for sixteen h. Post-obit this, the culture medium was substituted with Fluo-4 NW dye (lyophilized dye in 10 mL of assay buffer and 100 µL ii.5 mM probenecid added to prevent dye leakage from the cytosol) for 40 min at 37 °C in the CO2 incubator and followed by 30 min incubation at room temperature. Calcium mobilization was measured after the improver of AGEs to the cells in the presence or absence of agonist quinine and relative fluorescence units (RFUs) using a Flexstation-3 microplate reader (Molecular Devices, CA, Usa) at 525 nm were recorded, following 494 nm excitation. Data were nerveless from two independent experiments each done in triplicate and PRISM software version 6.0 (GraphPad Software, San Diego, CA, USA) was used to generate the graphs.
2.6. Statistical Assay
Data analyses were performed using one-way assay of variance (ANOVA) with an IBM SPSS Statistical package, version twenty (Armonk, NY, U.s.a.). Mean values were compared using the Duncan Multiple Range Test, and significant differences were accepted at p < 0.05.
three. Results
3.1. Degree of Glycation
The degree of glycation (DG) of AGEs is summarized in Table 2, and information technology shows that BPCH-AGEs had significantly (p < 0.05) less values than the BPAH-AGEs. The DG improved with the increase of D-glucose concentration; thus, the AGEs produced with 0.5 Yard D-glucose had significantly (p < 0.05) higher values than the other AGEs from lower glucose concentrations. The relationship between the hydrolysate concentration and the DG of the AGEs was not linear. For example, the i% (westward/v) hydrolysate AGEs did not always have a lower DG than those produced from three%. Therefore, caste of glycation was more dependent on glucose concentration rather than protein hydrolysate concentration.
Table 2
Caste of glycation (DG) for alcalase hydrolysate and chymotrypsin hydrolysate advanced glycation terminate products (AGEs).
| Hydrolysate Concentration (%) | Glucose Concentration (M) | DG (%) * | |
|---|---|---|---|
| Alcalase AGEs | Chymotrypsin AGEs | ||
| ane | 0.1 | 46.67 a | 29.53 a |
| ane | 0.2 | 47.53 b | 29.eleven a |
| ane | 0.3 | 54.15 due east | 30.13 b |
| 1 | 0.4 | 54.57 f | 36.67 d |
| i | 0.5 | 56.45 g | 37.14 e |
| 3 | 0.1 | 48.00 c | 29.49 a |
| 3 | 0.2 | 48.29 c | 28.86 a |
| 3 | 0.3 | 48.68 d | 36.63 cd |
| 3 | 0.4 | 54.88 f | 36.xl c |
| 3 | 0.5 | 54.96 fg | 38.lx f |
3.2. Prediction of Biting Score from Electronic Tongue
Predicted bitter score of BPAH-AGEs and BPCH-AGEs are shown in Figure 1A,B, respectively. The results show that all AGEs (5 mg/mL) had significantly (p < 0.05) higher bitterness scores than that of BCML but significantly lower than that of quinine. Based on the acceptability of humans for bitter gustatory modality as shown in Table three, the bitter gustatory modality of all AGEs (<15.0) is acceptable for human consumption. In the presence of BCML, quinine bitterness also significantly (p < 0.05) reduced. For a combination of BPAH-AGEs and quinine, AGEs from 0.3 Thou, 0.4 M, 0.5 One thousand D-glucose concentrations combined with ane% BPAH had significantly (p < 0.05) lower bitter scores than other AGEs. In contrast, the effect of glucose concentrations on the reduction of quinine bitterness intensity by BPCH-AGEs was not significant. However, BPCH-AGEs prepared with a 3% hydrolysate concentration had significantly (p < 0.05) stronger suppression of quinine bitterness intensity than AGEs from 1%.
Estimated electronic tongue bitter scores of glycated poly peptide hydrolysates and their power to suppress quinine bitterness intensity: AH-AGEs, glycated alcalase hydrolysate (A); (B) CH-AGEs, glycated chymotrypsin hydrolysate (B). BCML (Nα, Nα-bis(carboxymethyl)-Llysine) was used as a positive control. Bars with different letters take significantly different (p < 0.05) mean values as determined from Duncan Multiple Range tests while mistake confined correspond standard deviation.
Tabular array three
Bitter intensity level with respective scores from the human taste evaluation panelists *.
| Intensity | Range |
|---|---|
| Gustatory modality not detected | ane–iv.five |
| Slight taste | four.5–8.5 |
| Adequate | 8.5–12.5 |
| Acceptable limit | 12.5–16.5 |
| Not acceptable | 16.5–20.0 |
The unglycosylated AH was more than constructive in reducing quinine bitterness when compared to some of the AGEs produced with 0.1 and 0.2 M glucose. Nevertheless, the add-on of 0.3 or 0.4 Chiliad glucose produced AGEs with a significantly higher suppression of quinine bitterness than the unglycosylated AH. In contrast, with the exception of the CH-AGEs from 0.ane Grand glucose, there were no pregnant differences in the quinine bitter gustatory modality suppressing ability of the AH-AGEs when compared to the unglycosylated CH.
iii.three. Determination of Inhibitory Power Against T2R4 Activated by Quinine
In this study, HEK293T cells expressing T2R4-Ga16/44 were used as the experiment group, while HEK293 T cells expressing only Ga16/44 were used as the command group. Results of the calcium analysis of AGEs are shown in Effigy 2A,B for BPAH-AGEs and BPCH-AGEs, respectively. The results showed that all selected AGEs induced a significantly (p < 0.05) lower calcium release when compared to their respective hydrolysates, suggesting that the Maillard reaction reduced the biting taste of beef poly peptide enzymatic hydrolysates. Consistent with the electronic tongue data, calcium mobilization by BPAH-AGEs prepared with 3% hydrolysates was significantly lower than those of the 1% concentration. The BPAH-AGEs from 1% hydrolysate + 0.4 or 0.5 M glucose were especially plant to be the least effective suppressors of quinine bitterness based on their significantly (p < 0.05) higher calcium releases when compared to other AGEs. The BPCH-AGEs likewise significantly (p < 0.05) decreased quinine-dependent calcium mobilization although this occurred with greater efficiency when prepared with 0.1–0.three M glucose than 0.4 and 0.v M glucose.
Calcium mobilization in T2R4 expressing HEK293T cell organization after treatment with poly peptide hydrolysates, glycated protein hydrolysates (5 mg/mL) and quinine (i mM): A. alcalase hydrolysate (AH), one% AH + 0.3 Grand D-glucose (A1), 3% AH + 0.3 M D-glucose (A2), i% AH + 0.4 M D-glucose (A3), 3% AH + 0.four M D-glucose (A4), 1% AH + 0.5 M D-glucose (A5), three% AH + 0.5 M D-glucose (A6); B. chymotrypsin hydrolysate (CH), 1% CH + 0.i Grand D-glucose (C1), 3% CH + 0.1 G D-glucose (C2), iii% CH + 0.two M D-glucose (C3), iii% CH + 0.3 M D-glucose (C4), iii% CH + 0.4 M D-glucose (C5), 3% CH + 0.five Chiliad D-glucose (C6). Confined with different messages have significantly dissimilar (p < 0.05) mean values as determined from Duncan Multiple Range tests while error bars represent standard deviation. ΔRFU: changes in relative fluorescence unit (test cells minus control cells).
4. Discussion
Glycation is a common method used to modify proteins, and the properties and characteristics of the resulting AGEs are closely related to the caste of glycation [25,26], which is influenced past many factors including temperature, time, h2o activeness and the reactants molar ratio [12,27]. Previous studies reported that calculation 500–g Da and thou–5000 Da fractions of wheat gluten hydrolysates enhanced umami taste and improved the yield of AGEs [26,27,28]. However, cereals are rich in asparagines [29], which produce acrylamide, a known carcinogenic gene during the Maillard reaction [30]. Thus, meat protein hydrolysate is a better selection for producing safer AGEs. Given the same saccharide and same reacting weather, the differences in DG could have been due to variations in the blazon of peptides inside the enzymatic hydrolysates. BPCH had significantly (p < 0.05) lower DG than that of BPAH, suggesting that in add-on to peptide size, the blazon and system of amino acids on the peptides may be important in determining the degree of glycation. Li et al. [25] reported that the content of lysine and arginine decreased significantly in AGEs, implying that peptides with more lysine and arginine may accept college DG. In this instance, we previously reported that BPAH and BPCH had similar contents of these 2 amino acids [21]. Still, the higher DG of BPAH could exist attributed to the presence of more of the brusk-chain peptides, which will mean a greater number of free amino groups bachelor for the Maillard reaction. This is because our previous work showed that BPAH contained a higher level of short-chain peptides (boilerplate of 450 Da) when compared to the i.8 kDa for BPCH [21]. Glycation is believed to be an of import way of reducing bitter taste and generating aroma gustation because the attachment of sugars can dramatically reduce the surface hydrophobicity of peptides and increment solubility [27,31]. Thus, the AGEs with higher DG may have a better taste and have higher potential for masking biting taste.
Bitter scores of BPAH-AGEs and BPCH-AGEs were estimated by the electronic tongue. The ability of the AGEs to suppress quinine bitterness was stronger when three% BPCH hydrolysate concentration was used but not BPAH. The greater bitter taste-suppressing action of BPAH-AGEs from 0.3 M or 0.4 M glucose suggested the presence of circuitous glycosylated peptides with structures that promote better interactions with the T2R4 receptor when compared to the other AGEs. However, the BPCH-AGEs did not show a like effect on glucose concentration. Therefore, it is possible that the peptide composition differed betwixt BPAH and BPCH, which would explicate the variation in the bitter taste-suppressing ability of the AGEs fifty-fifty when the aforementioned concentration of peptides was reacted with glucose. Still, most chiefly, the results suggest that these AGEs could serve as useful agents in blocking biting awareness in the human mouth. The results are reliable indications of the potential employ of the AGEs as bitter gustation blockers. This is because the use of this instrumental approach was based on a previous study that showed the prediction of biting taste of dairy protein hydrolysates had a R2 value of 0.94 when the electronic natural language data were plotted against the human sensory panel [32]. Although sensory tests are unremarkably performed past human being panelists through physical tasting of samples, this method has some disadvantages, such as low objectivity and reproducibility, especially when large numbers of samples are involved [33,34]. Notwithstanding, homo sensory tests have the advantage of representing the diverse gustatory modality preferences inside the population, which cannot be measured past the electronic tongue instrument. The diversity in taste preferences and loftier variability may be useful for food product development that meets consumer demands. However, in social club to solve some of the issues associated with human sensory tests, electronic-tongue instrumentation has been adult to enable the rapid assay of a multiple number of samples within a short catamenia of time and without the fatigue associated with human being tasting. In the electronic tongue organization, in that location is one Ag/AgCl electrode and seven sensors coated with lipid/polymer membranes, which govern the sensitivity and selectivity of an individual sensor by interacting with tastants to produce an electric potential [34,35]. This arrangement can not merely detect the bitter taste of samples, but can also determine the suppression power of bitter taste modifiers, such as high potency sweeteners that suppress bitter gustation of quinine hydrochloride, and acesulfame Thou and citric acid suppressing the bitter taste of epinephrine [36,37]. This written report aimed to find highly efficient bitter gustatory modality modifiers, which were expected to be able to function at the taste receptor level. The results obtained in this work are similar to those we reported for various beef protein hydrolysates and peptides that also suppressed quinine bitterness intensity as measured by the electronic tongue [21]. In order to verify the results of bitter gustation that were measured by the electronic tongue and further explore the mechanism of bitterness masking of AGEs, the AGEs with lower bitter gustatory modality scores were selected to conduct a calcium assay based on HEK 293 cells. Because the diversity and complexity of 25 human bitter taste receptors, the T2R4 whose chemical structure and binding sites of its agonist quinine have been extensively studied, was selected as a future target receptor; quinine and BCML were selected as a bitter agonist and adversary, respectively [ii].
Based on the mechanism of the bitter taste transduction pathway, the activation of T2Rs will stimulate calcium release from intracellular stores, hence the calcium assay is used to identify bitter gustatory modality agonists and antagonists of T2Rs [two,38]. Furthermore, HEK293T prison cell-based heterologous expression is a robust assay method to measure G-protein coupled receptor activation and is wildly used for T2Rs and other human membrane proteins. About of the T2R inhibitors including GABA, BCML, probenecid and 6-methoxyflavanones were discovered using the above HEK293T heterologous expression system and calcium assay method [1,ii,iii]. The results showed that some of the glycated peptides had a college bitter taste blocking efficiency (reduced calcium release) than the hydrolysates. For example, glycated peptides like A1–A4 and A6 every bit well as C1, C3, and C4 had stronger effects in limiting calcium release than their corresponding not-glycated hydrolysates. For these samples, it is possible that glycation led to structural changes such as increased hydrophilicity, which reduced hydrophobic interactions with the T2R4 protein. In dissimilarity, the AGEs with a weaker bitter gustation blocking effect might accept assumed structural changes that increased effective interactions (activation) with the T2R4 protein. The results are consistent with our previous report that showed a wide range of structural properties of beef protein-derived peptides that blocked quinine-dependent T2R4 activation [21]. However, nosotros observed that in that location was no directly relationship betwixt DG and quinine bitter taste-suppression, which suggested that the intrinsic structural properties of the AGEs may accept had a stronger influence than simply the concentration of glucose used for the Maillard reaction.
5. Conclusions
This written report showed that the Maillard reaction efficiently reduced the bitterness of beef protein hydrolysates, which may be attributed to increased electrophilic properties of the glycated peptides. The increased electrophilic properties may exist responsible for the decreased intrinsic bitterness of the glycated peptides and their enhanced ability to reduce quinine bitterness intensity every bit measured by the electronic tongue. The higher charged country of the glycated peptides could have reduced hydrophobic interactions with the T2R4 protein, hence the weak activation that was measured as a poor receptor response to quinine-induced calcium release (a measure of reduced bitterness intensity). The stronger ability of BPAH-AGEs to block quinine-dependent bitterness intensity may exist due to the high state of glycation and poorer hydrophobic interactions with T2R4 (reduced receptor activation) when compared to the less glycated BPCH-AGEs. Hereafter studies that are focused on structural elucidation of the AGEs will be required to determine the structural ground for the bitter gustatory modality-blocking ability. The use of human taste evaluation panels will be necessary to confirm the potential role of peptide AGEs equally biting sense of taste-blocking ingredients in food and nutraceutical products development.
Author Contributions
Conceptualization, P.C. and R.E.A.; formal analysis, C.Z. and A.M.A.; funding acquisition, P.C. and R.E.A.; methodology, C.Z., A.M.A., N.South. and P.C.; projection administration, P.C. and R.E.A.; resources, P.C. and R.E.A.; supervision, A.1000.A., Northward.S. and P.C.; writing–original draft, C.Z.; writing–review and editing, P.C. and R.E.A.
Funding
The authors are grateful for the financial back up provided by Alberta Agriculture and Forestry funding reference number 2015P002R, Edmonton, Alberta, Canada. We acknowledge support of the Natural Sciences and Engineering Research Council of Canada (NSERC), funding reference numbers RGPIN 249890-13 and RGPIN 2014-04099. Cette recherche a été financée par le Conseil de recherches en sciences naturelles et en génie du Canada (CRSNG), numéro de référence RGPIN 249890-thirteen et RGPIN 2014-04099.
Conflicts of Involvement
The authors declare no conflicts of interest. The funders had no part in the design of the study; in the collection, analyses, or estimation of data; in the writing of the manuscript, or in the decision to publish the results.
References
i. Greene T.A., Alarcon S., Thomas A., Berdougo E., Doranz B.J., Breslin P.A.South., Rucker J.B. Probenecid inhibits the human bitter taste receptor TAS2R16 and suppresses bitter perception of salicin. PLoS 1. 2011;6:e20123. doi: ten.1371/periodical.pone.0020123. [PMC free commodity] [PubMed] [CrossRef] [Google Scholar]
2. Pydi S.P., Sobotkiewicz T., Billakanti R., Bhullar R.P., Loewen Chiliad.C., Chelikani P. Amino acrid derivatives equally biting taste receptor (T2R) blockers. J. Biol. Chem. 2014;289:25054–25066. doi: ten.1074/jbc.M114.576975. [PMC gratuitous article] [PubMed] [CrossRef] [Google Scholar]
three. Roland West.S.U., Gouka R.J., Gruppen H., Driesse G., Van Buren 50., Smit K., Vincken J.P. half dozen-Methoxyflavanones as bitter gustatory modality receptor blockers for hTAS2R39. PLoS 1. 2014;ix:e94451. doi: 10.1371/journal.pone.0094451. [PMC gratuitous article] [PubMed] [CrossRef] [Google Scholar]
4. Jaggupilli A., Howard R., Upadhyaya J.D., Bhullar R.P., Chelikani P. Bitter sense of taste receptors: Novel insights into the biochemistry and pharmacology. Int. J. Biochem. Cell Biol. 2016;77:184–196. doi: 10.1016/j.biocel.2016.03.005. [PubMed] [CrossRef] [Google Scholar]
five. Ley J.P. Masking bitter taste past molecules. Chemosens. Percept. 2008;i:58–77. doi: 10.1007/s12078-008-9008-2. [CrossRef] [Google Scholar]
6. Slack J.P., Brockhoff A., Batram C., Menzel S., Sonnabend C., Born S., Meyerhof W. Modulation of bitter taste perception past a small molecule hTAS2R adversary. Curr. Biol. 2010;20:1104–1109. doi: 10.1016/j.cub.2010.04.043. [PMC costless article] [PubMed] [CrossRef] [Google Scholar]
vii. Jaggupilli A., Howard R., Aluko R.E., Chelikani P. Advanced glycation terminate-products can activate or cake bitter taste receptors. Nutrients. 2019;11:1317. doi: 10.3390/nu11061317. [PMC free commodity] [PubMed] [CrossRef] [Google Scholar]
8. Wu C.-H., Huang S.-M., Lin J.A., Yen One thousand.-C. Inhibition of advanced glycation endproduct formation by foodstuffs. Food Funct. 2011;2:224–234. doi: 10.1039/c1fo10026b. [PubMed] [CrossRef] [Google Scholar]
9. Chen X.U.E., Pyzik R., Yong A., Striker G.E. Advanced glycation end products in foods and a practical guide to their reduction in the diet. J. Am. Diet. Assoc. 2013;110:911–916. [PMC gratis article] [PubMed] [Google Scholar]
x. Uribarri J., Dolores M., Pía Yard., Maza D., Filip R., Gugliucci A., Wrobel Chiliad. Dietary advanced glycation end products and their role in health and disease. Adv. Nutr. 2015;6:461–473. doi: 10.3945/an.115.008433. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
eleven. Liu P., Huang M., Song S., Hayat K., Zhang X., Xia S., Jia C. Sensory characteristics and antioxidant activities of Maillard reaction products from soy protein hydrolysates with different molecular weight distribution. Food Bioprocess Tech. 2012;5:1775–1789. doi: 10.1007/s11947-010-0440-3. [CrossRef] [Google Scholar]
12. Oh Due north.S., Lee H.A., Lee J.Y., Joung J.Y., Lee Thousand.B., Kim Y., Kim S.H. The dual effects of Maillard reaction and enzymatic hydrolysis on the antioxidant activity of milk proteins. J. Dairy Sci. 2013;96:4899–4911. doi: x.3168/jds.2013-6613. [PubMed] [CrossRef] [Google Scholar]
13. Namiki T., Nakamura T. Enhancement of Sugar Sugariness past Furanones and/or Cyclotene. JP 04008264. Japanese Patent. 1992
14. Ottinger H., Soldo T., Hofmann T. Discovery and structure decision of a novel Maillard-derived sweet enhancer by application of the comparative gustatory modality dilution analysis (cTDA) J. Agric. Food Chem. 2003;51:1035–1041. doi: 10.1021/jf020977i. [PubMed] [CrossRef] [Google Scholar]
15. Dong S., Wei B., Chen B., McClements D.J., Decker E.A. Chemical and antioxidant properties of casein peptide and its glucose Maillard reaction products in fish oil-in-h2o emulsions. J. Agric. Nutrient Chem. 2011;59:13311–13317. doi: x.1021/jf203778z. [PubMed] [CrossRef] [Google Scholar]
16. Williams P.G. Nutritional composition of red meat. Nutr. Diet. 2007;64(Suppl. iv):S113–S119. doi: x.1111/j.1747-0080.2007.00197.10. [CrossRef] [Google Scholar]
17. Guerard F., Dufosse 50., De La Broise D., Binet A. Enzymatic hydrolysis of proteins from yellowfin tuna (Thunnus albacares) wastes using Alcalase. J. Mol. Catal. B. 2001;11:1051–1059. doi: x.1016/S1381-1177(00)00031-X. [CrossRef] [Google Scholar]
18. Feng 50., Qiao Y., Zou Y., Huang Chiliad., Kang Z., Zhou Grand. Result of Flavourzyme on proteolysis, antioxidant chapters and sensory attributes of Chinese sausage. Meat Sci. 2014;98:34–40. doi: 10.1016/j.meatsci.2014.04.001. [PubMed] [CrossRef] [Google Scholar]
xix. Meinlschmidt P., Sussmann D., Schweiggert-Weisz U., Eisner P. Enzymatic treatment of soy protein isolates: Furnishings on the potential allergenicity, technofunctionality, and sensory backdrop. Food Sci. Nutr. 2016;4:11–23. doi: x.1002/fsn3.253. [PMC gratis commodity] [PubMed] [CrossRef] [Google Scholar]
twenty. O'Meara M.M., Munro P.A. Hydrolysis of the sarcoplasmic, myofibrillar and connective tissue proteins of lean beef by alcalase and its relationship to whole meat hydrolysis. Meat Sci. 1985;12:91–103. doi: 10.1016/0309-1740(85)90018-X. [PubMed] [CrossRef] [Google Scholar]
21. Zhang C., Alashi A.Thousand., Singh N., Liu K., Chelikani P., Aluko R.E. Beefiness poly peptide-derived peptides every bit biting taste receptor T2R4 blockers. J. Agric. Food Chem. 2018;66:4902–4912. doi: 10.1021/acs.jafc.8b00830. [PubMed] [CrossRef] [Google Scholar]
22. Charoenphun N., Cheirsilp B., Sirinupong N., Youravong W. Calcium-binding peptides derived from tilapia (Oreochromis niloticus) protein hydrolysate. Eur. Food Res. Technol. 2013;236:57–63. doi: ten.1007/s00217-012-1860-2. [CrossRef] [Google Scholar]
23. Nielsen P.Chiliad., Petersen D., Dambmann C. Improved method for determining nutrient protein degree of hydrolysis. J. Food Sci. 2001;66:642–646. doi: x.1111/j.1365-2621.2001.tb04614.10. [CrossRef] [Google Scholar]
24. Alpha MOS . Astree Electrochemical Sensor Technology—Technical Annotation: T-SAS-04. Alpha MOS; Toulouse, France: 2004. [Google Scholar]
25. Li Y., Zhong F., Ji Westward., Yokoyama West., Shoemaker C.F., Zhu S., Xia W. Functional properties of Maillard reaction products of rice protein hydrolysates with mono-, oligo- and polysaccharides. Nutrient Hydrocoll. 2013;thirty:53–60. doi: x.1016/j.foodhyd.2012.04.013. [CrossRef] [Google Scholar]
26. Song N., Tan C., Huang M., Liu P., Eric K., Zhang X., Jia C. Transglutaminase cantankerous-linking upshot on sensory characteristics and antioxidant activities of Maillard reaction products from soybean protein hydrolysates. Food Chem. 2013;136:144–151. doi: x.1016/j.foodchem.2012.07.100. [PubMed] [CrossRef] [Google Scholar]
27. Garcia-Amezquita Fifty.E., Martinez-Alvarenga K.Southward., Olivas Thou.I., Zamudio-Flores P.B., Acosta-Muñiz C.H., Sepulveda D.R. Event of Maillard reaction conditions on the degree of glycation and functional properties of whey poly peptide isolate-Maltodextrin conjugates. Food Hydrocoll. 2014;38:110–118. [Google Scholar]
28. Ogasawara K., Katsumata T., Egi Thou. Taste backdrop of Maillard-reaction products prepared from 1000 to 5000 Da peptide. Nutrient Chem. 2006;99:600–604. doi: 10.1016/j.foodchem.2005.08.040. [CrossRef] [Google Scholar]
29. Friedman Grand. Chemistry, biochemistry, and rubber of acrylamide. A review. J. Agric. Food Chem. 2003;51:4504–4526. doi: ten.1021/jf030204+. [PubMed] [CrossRef] [Google Scholar]
30. Vattem D.A., Shetty K. Acrylamide in food: A model for mechanism of formation and its reduction. Innov. Food Sci. Emerg. Technol. 2003;4:331–338. doi: ten.1016/S1466-8564(03)00033-X. [CrossRef] [Google Scholar]
31. Li Westward., Zhao H., He Z., Zeng Grand., Qin F., Chen J. Modification of soy protein hydrolysates by Maillard reaction: Furnishings of sugar concatenation length on structural and interfacial backdrop. Colloids Surf. B. 2016;138:70–77. doi: x.1016/j.colsurfb.2015.xi.038. [PubMed] [CrossRef] [Google Scholar]
32. Newman J., Harbourne N., O'Riordan D., Jacquier J.C., O'Sullivan Yard. Comparing of a trained sensory console and an electronic natural language in the assessment of biting dairy poly peptide hydrolysates. J. Food Eng. 2014;128:127–131. doi: 10.1016/j.jfoodeng.2013.12.019. [CrossRef] [Google Scholar]
33. Akitomi H., Tahara Y., Yasuura M., Kobayashi Y., Ikezaki H., Toko K. Quantification of tastes of amino acids using taste sensors. Sens. Actuators B. 2013;179:276–281. doi: 10.1016/j.snb.2012.09.014. [CrossRef] [Google Scholar]
34. Choi D.H., Kim N.A., Nam T.Due south., Lee Due south., Jeong S.H. Evaluation of gustation-masking furnishings of pharmaceutical sweeteners with an electronic natural language system. Drug Dev. Ind. Pharm. 2014;40:308–317. doi: ten.3109/03639045.2012.758636. [PubMed] [CrossRef] [Google Scholar]
35. Miyanaga Y., Tanigake A., Nakamura T., Kobayashi Y., Ikezaki H., Taniguchi A., Uchida T. Prediction of the bitterness of single, binary- and multiple-component amino acid solutions using a taste sensor. Int. J. Pharm. 2002;248:207–218. doi: 10.1016/S0378-5173(02)00456-eight. [PubMed] [CrossRef] [Google Scholar]
36. Rachid O., Simons F.E.R., Rawas-Qalaji M., Simons K.J. An electronic natural language: Evaluation of the masking efficacy of sweetening and/or flavoring agents on the bitter taste of epinephrine. AAPS PharmSciTech. 2010;11:550–557. doi: 10.1208/s12249-010-9402-3. [PMC free commodity] [PubMed] [CrossRef] [Google Scholar]
37. Wu X., Onitake H., Haraguchi T., Tahara Y., Yatabe R., Yoshida M., Toko 1000. Quantitative prediction of bitterness masking effect of high-potency sweeteners using taste sensor. Sens. Actuators B. 2016;235:xi–17. doi: 10.1016/j.snb.2016.05.009. [CrossRef] [Google Scholar]
38. Behrens G., Meyerhof W. Bitter taste receptors and human bitter taste perception. Jail cell. Mol. Life Sci. 2006;63:1501–1509. doi: 10.1007/s00018-006-6113-8. [PubMed] [CrossRef] [Google Scholar]
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