CoChat
Sign Up
Cited by 124

Modifying the structure, physicochemical properties, and foaming ability of amaranth protein by dual pH-shifting and ultrasound treatments

Figueroa-González, Juan J., Lobato-Calleros, Consuelo, Vernon-Carter, E. Jaime, Aguirre-Mandujano, Eleazar, Alvarez-Ramirez, Jose, Martínez-Velasco, Alejandro·2022·LWT
DOI 10.1016/j.lwt.2021.112561
Open this paper in CoChat — free account

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1016/j.lwt.2021.112561

Cites

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • At the colloidal scale, DLS at neutral pH often reports broad micron-scale distributions (1.1-1.2 μm), which can be disassociated into submicron particles (0.4-0.6 μm) by dual pH-shift combined with ultrasound.

    “At the colloidal scale, DLS at neutral pH often reports broad micron-scale distributions (1.1-1.2 μ m), which can be disassociated into submicron particles (0.4-0.6 μ m) by dual pH-shift combined with ultrasound”

    From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Figueroa-González et al., 2022

  • Dual pH-shift combined with ultrasound markedly reduces the contents of α-helices and β-turns while increasing those of β-sheets and random coils, accompanied by intrinsic-fluorescence red-shifts and quenching that indicate tryptophan exposure and partial loss of tertiary packing.

    “Dual pH-shift combined with ultrasound markedly re­ duces the contents of α -helices and β -turns while increasing those of β -sheets and random coils, accompanied by intrinsic-fluorescence red-­ shifts and quenching that indicate tryptophan exposure and partial loss of tertiary packing”

    From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Figueroa-González et al., 2022

  • For amaranth, dual pH-shift combined with ultrasound can disintegrate loose aggregates (1.1-1.2 μm) into submicron particles (0.4-0.6 μm), increase ζ-potential and surface hydrophobicity, and redistribute secondary-structure assignments toward higher β-sheet and random coil.

    “For amaranth, dual pH-shift combined with ultrasound can disintegrate loose aggregates (1.1-1.2 μ m) into submicron particles (0.4-0.6 μ m), increase ζ -potential and surface hydrophobicity, and redistribute secondary-structure assignments toward higher β -sheet and random coil”

    From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Figueroa-González et al., 2022

  • pH-shift combined with ultrasound can further increase apparent solubility by breaking micron flocs into submicron dispersions and increasing charge magnitude.

    “pH-shift combined with ultrasound can further increase apparent solubility by breaking micron flocs into submicron dispersions and increasing charge magnitude”

    From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Figueroa-González et al., 2022

  • For amaranth, pH-shift combined with ultrasonication reduced loose flocs from 1.1-1.2 μm to 0.4-0.6 μm, with higher ζ-magnitude and increased surface hydrophobicity, typical of a move toward submicron particle stabilization.

    “For amaranth, pH-shift combined with ultrasonication reduced loose flocs from 1.1-1.2 μ m to 0.4-0.6 μ m, with higher ζ -magnitude and increased surface hydrophobicity, which is typical of a move toward submicron particle stabilization (Figueroa-Gonz ´ alez et al., 2022).”

    From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Figueroa-Gonzalez et al., 2022

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

No references could be resolved yet.

Research works printed but not linked: 61

  1. AOAC. (1996). Official methods of analysis of AOAC international (16th ed.). AOAC International.
  2. Avanza, M. V., & Añon, M. C. (2017). Effect of thermal treatment on the proteins of amaranth isolates. Journal of the Science of Food and Agriculture, 87(4), 616-623. https://doi.org/10.1002/jsfa.2751 · DOI
  3. Barba de la Rosa, A. P., Fomsgaard, I. S., Laursen, B., Mortensen, A. G., Olvera- Martínez, L., Silva-Sánchez, C., et al. (2009). Amaranth (Amaranthus hypochondriacus) as an alternative crop for sustainable food production: Phenolic acids and flavonoids with potential impact on its nutraceutical quality. Journal of Cereal Science, 49, 117-121. https://doi.org/10.1016/j.jcs.2008.07.012 · DOI
  4. Bolontrade, A. J., Scilingo, A. A., & Añón, M. C. (2013). Amaranth proteins foaming properties: Adsorption kinetics and foam formation-part 1. Colloids and Surfaces B: Biointerfaces, 105, 319-327. https://doi.org/10.1016/j.colsurfb.2012.12.039 · DOI
  5. Bolontrade, A. J., Scilingo, A. A., & Añón, M. C. (2016). Amaranth proteins foaming properties: Film rheology and foam stability-Part 2. Colloids and Surfaces B: Biointerfaces, 141, 643-650. https://doi.org/10.1016/j.colsurfb.2014.10.061 · DOI
  6. Carbonaro, M., & Nucara, A. (2010). Secondary structure of food proteins by Fourier transform spectroscopy in the mid-infrared region. Amino Acids, 38(3), 679-690. https://doi.org/10.1007/s00726-009-0274-3 · DOI
  7. Chen, W., Wang, W., Ma, X., Lv, R., Watharkar, R. B., Ding, T., et al. (2019). Effect of pH- shifting treatment on structural and functional properties of whey protein isolate and its interaction with (-)-epigallocatechin-3-gallate. Food Chemistry, 274, 234-241. https://doi.org/10.1016/j.foodchem.2018. · DOI
  8. Condés, M. C., Scilingo, A. A., & Añón, M. C. (2009). Characterization of amaranth proteins modified by trypsin proteolysis. Structural and functional changes. LWT- Food Science and Technology, 42(5), 963-970. https://doi.org/10.1016/j. lwt.2008.12.00 · DOI
  9. Constantino, A. B. T., & Garcia-Rojas, E. E. (2020). Modifications of physicochemical and functional properties of amaranth protein isolate (Amaranthus cruentus BRS Alegria) treated with high-intensity ultrasound. Journal of Cereal Science, 95, 103076. https:// doi.org/10.1016/j.jcs.2020.103076 · DOI · Paper page
  10. Cordero-de-Los-Santos, M. Y., Osuna-Castro, J. A., Borodanenko, A., & Paredes-López, O. (2005). Physicochemical and functional characterisation of amaranth (Amaranthus hypochondriacus) protein isolates obtained by isoelectric precipitation and micellisation. Food Science and Technology International, 11(4), 269-280, 10.1177% 2F1082013205056491.
  11. Corke, H., Cai, Y. Z., & Wu, H. X. (2016). Amaranth: Overview. In C. Wrigley, H. Corke, K. Seetharaman, & J. Faubion (Eds.), Encyclopedia of food grains (2nd ed., Vol. 1, pp. 287-296). Elsevier, 10.1016/B978-0-12-394437-5.00032-2. · DOI
  12. Das, D., Mir, N. A., Chandla, N. K., & Singh, S. (2021). Combined effect of pH treatment and the extraction pH on the physicochemical, functional and rheological characteristics of amaranth (Amaranthus hypochondriacus) seed protein isolates. Food Chemistry, 353, 129466. https://doi.org/10.1016/j.foodchem.2021.129466 · DOI
  13. Elsohaimy, S. A., Refaay, T. M., & Zaytoun, M. A. M. (2015). Physicochemical and functional properties of quinoa protein isolate. Annals of Agricultural Science, 60(2), 297-305. https://doi.org/10.1016/j.aoas.2015.10.007 · DOI
  14. Fang, Z., Cai, X., Wu, J., Zhang, L., Fang, Y., & Wang, S. (2021). Effect of simultaneous treatment combining ultrasonication and pH-shifting on SPI in the formation of nanoparticles and encapsulating resveratrol. Food Hydrocolloids, 111, 106250. https://doi.org/10.1016/j.foodhyd.2020.106250 · DOI
  15. Fasolin, L. H., Pereira, R. N., Pinheiro, A. C., Martins, J. T., Andrade, C. C. P., Ramos, O. L., et al. (2019). Emergent food proteins-Towards sustainability, health and innovation. Food Research International, 125, 108586. https://doi.org/10.1016/ j.foodres.2019.108586 · DOI
  16. Gürbüz, G., Kauntola, V., Diaz, J. M. R., Jouppila, K., & Heinonen, M. (2018). Oxidative and physical stability of oil-in-water emulsions prepared with quinoa and amaranth proteins. European Food Research and Technology, 244(3), 469-479. https://doi.org/ 10.1007/s00217-017-2973-4 · DOI
  17. He, S., Zhao, J., Cao, X., Ye, Y., Wu, Z., Yue, J., et al. (2020). Low pH-shifting treatment would improve functional properties of black turtle bean (Phaseolus vulgaris L.) protein isolate with immunoreactivity reduction. Food Chemistry, 330, 127217. https://doi.org/10.1016/j.foodchem.2020.127217 · DOI
  18. Hsu, H. W., Vavak, D. L., Satterlee, L., & Miller, G. A. (1977). A multienzyme technique for estimating protein digestibility. Journal of Food Science, 42(5), 1269-1273. https://doi.org/10.1111/j.1365-2621.1977.tb14476.x · DOI · Paper page
  19. Hu, Y., Wang, L., & Li, Z. (2017). Modification of protein structure and dough rheological properties of wheat flour through superheated steam treatment. Journal of Cereal Science, 76, 222-228. https://doi.org/10.1016/j.jcs.2017.06.013 · DOI
  20. Hu, H., Wu, J., Li-Chan, E. C., Zhu, L., Zhang, F., Xu, X., et al. (2013). Effects of ultrasound on structural and physical properties of soy protein isolate (SPI) dispersions. Food Hydrocolloids, 30(2), 647-655. https://doi.org/10.1016/j. foodhyd.2013.01.016 · DOI
  21. Ismail, B. P., Senaratne-Lenagala, L., Stube, A., & Brackenridge, A. (2020). Protein demand: Review of plant and animal proteins used in alternative protein product development and production. Animal Frontiers, 10(4), 53-63. https://doi.org/ 10.1093/af/vfaa040 · DOI
  22. Jiang, J., Chen, J., & Xiong, Y. L. (2009). Structural and emulsifying properties of soy protein isolate subjected to acid and alkaline pH-shifting processes. Journal of Agricultural and Food Chemistry, 57, 7576-7583. https://doi.org/10.1021/jf901585n · DOI
  23. Jiang, S., Ding, J., Andrade, J., Rababah, T. M., Almajwal, A., Abulmeaty, M. M., et al. (2017). Modifying the physicochemical properties of pea protein by pH-shifting and ultrasound combined treatments. Ultrasonics Sonochemistry, 38, 835-842. https:// doi.org/10.1016/j.ultsonch.2017.03.046 · DOI
  24. Jiang, L., Ren, Y., Shen, M., Zhang, J., Yu, Q., Chen, Y., et al. (2021). Effect of acid/alkali shifting on function, gelation properties, and microstructure of Mesona chinensis polysaccharide-whey protein isolate gels. Food Hydrocolloids, 117, 106699. https:// doi.org/10.1016/j.foodhyd.2021.106699 · DOI
  25. Jiang, J., Wang, Q., & Xiong, Y. L. (2018). A pH shift approach to the improvement of interfacial properties of plant seed proteins. Current Opinion in Food Science, 19, 50-56. https://doi.org/10.1016/j.cofs.2018.01.002 · DOI
  26. Jiang, J., Xiong, Y. L., & Chen, J. (2011). Role of β-conglycinin and glycinin subunits in the pH-shifting-induced structural and physicochemical changes of soy protein isolate. Journal of Food Science, 76(2), C293-C302. https://doi.org/10.1111/j.1750- 3841.2010.02035.x · DOI
  27. Jiang, J., Zhu, B., Liu, Y., & Xiong, Y. (2014). Interfacial structural role of pH-shifting processed pea protein in the oxidative stability of oil/water emulsions. Journal of Agricultural and Food Chemistry, 62(7), 1683-1691. https://doi.org/10.1021/ jf405190h · DOI
  28. Jin, J., Okagu, O. D., Yagoub, A. E. A., & Udenigwe, C. C. (2021). Effects of sonication on the in vitro digestibility and structural properties of buckwheat protein isolates. Ultrasonics Sonochemistry, 70, 105348. https://doi.org/10.1016/j. ultsonch.2020.105348 · DOI · Paper page
  29. Kong, J., & Yu, S. (2007). Fourier transform infrared spectroscopic analysis of protein secondary structures. Acta Biochimica et Biophysica Sinica, 39(8), 549-559. https:// doi.org/10.1111/j.1745-7270.2007.00320.x · DOI
  30. Lado, M. B., Burini, J., Rinaldi, G., Añón, M. C., & Tironi, V. A. (2015). Effects of the dietary addition of Amaranth (Amaranthus mantegazzianus) protein isolate on antioxidant status, lipid profiles and blood pressure of rats. Plant Foods for Human Nutrition, 70(4), 371-379. https://doi.org/10.1007/s11130-015-0516-3. · DOI
  31. Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227(5259), 680-685. https://doi.org/10.1038/227680a0 · DOI · Paper page
  32. Lee, H., Yildiz, G., Dos Santos, L. C., Jiang, S., Andrade, J. E., Engeseth, N. J., et al. (2016). Soy protein nano-aggregates with improved functional properties prepared by sequential pH treatment and ultrasonication. Food Hydrocolloids, 55, 200-209. https://doi.org/10.1016/j.foodhyd.2015.11.022 · DOI
  33. Lin, H., Bean, S. R., Tilley, M., Peiris, K. H. S., & Brabec, D. (2021). Qualitative and quantitative analysis of sorghum grain composition including protein and tannins using ATR-FTIR spectroscopy. Food Analytical Methods, 14(2), 268-279. https://doi. org/10.1007/s12161-020-01874-5 · DOI
  34. Li, J., Wu, M., Wang, Y., Li, K., Du, J., & Bai, Y. (2020). Effect of pH-shifting treatment on structural and heat induced gel properties of peanut protein isolate. Food Chemistry, 325, 126921. https://doi.org/10.1016/j.foodchem.2020.126921 · DOI
  35. López-Monterrubio, D. I., Lobato-Calleros, C., Alvarez-Ramirez, J., & Vernon-Carter, E. J. (2020). Huauzontle (Chenopodium nuttalliae Saff.) protein: Composition, structure, physicochemical and functional properties. Food Hydrocolloids, 108, 106043. https://doi.org/10.1016/j.foodhyd.2020.106043 · DOI
  36. López, D. N., Galante, M., Robson, M., Boeris, V., & Spelzini, D. (2018). Amaranth, quinoa and chia protein isolates: Physicochemical and structural properties. International Journal of Biological Macromolecules, 109, 152-159. https://doi.org/ 10.1016/j.ijbiomac.2017.12.080 · DOI
  37. Marcone, M. F., & Kakuda, Y. (1999). A comparative study of the functional properties of amaranth and soybean globulin isolates. Food, 43(6), 368-373. doi.org/10.1002/ (SICI)1521-3803(19991201)43:6%3C368::AID-FOOD368%3E3.0.CO;2-R. Martinez-Lopez, A., Millan-Linares, M. C., Rodriguez-Martin, N. M., Millan, F., & Montserrat-de la Paz, S. (2020). Nutraceutical value of kiwicha (Amaranthus caudatus L.). Journal of Functional Foods, 65, 103735. https://doi.org/10.1016/j. jff.2019.103735 · DOI
  38. Martínez-Velasco, A., Lobato-Calleros, C., Hernández-Rodríguez, B. E., Román- Guerrero, A., Alvarez-Ramirez, J., & Vernon-Carter, E. J. (2018). High intensity ultrasound treatment of faba bean (Vicia faba L.) protein: Effect on surface properties, foaming ability and structural changes. Ultrasonics Sonochemistry, 44, 97-105. https://doi.org/10.1016/j.ultsonch.2018.02.007 · DOI
  39. Mir, N. A., Riar, C. S., & Singh, S. (2019a). Structural modification of quinoa seed protein isolates (QPIs) by variable time sonification for improving its physicochemical and functional characteristics. Ultrasonics Sonochemistry, 58, 104700. https://doi.org/ 10.1016/j.ultsonch.2019.104700 · DOI
  40. Mir, N. A., Riar, C. S., & Singh, S. (2019b). Physicochemical, molecular and thermal properties of high-intensity ultrasound (HIUS) treated protein isolates from album (Chenopodium album) seed. Food Hydrocolloids, 96, 433-441. https://doi.org/ 10.1016/j.foodhyd.2019.05.052 · DOI
  41. Mir, N. A., Riar, C. S., & Singh, S. (2020). Structural modification in album (Chenopodium album) protein isolates due to controlled thermal modification and its relationship with protein digestibility and functionality. Food Hydrocolloids, 103, 105708. https://doi.org/10.1016/j.foodhyd.2020.105708 · DOI
  42. Nazari, B., Mohammadifar, M. A., Shojaee-Aliabadi, S., Feizollahi, E., & Mirmoghtadaie, L. (2018). Effect of ultrasound treatments on functional properties and structure of millet protein concentrate. Ultrasonics Sonochemistry, 41, 382-388. https://doi.org/10.1016/j.ultsonch.2017.10.002 · DOI
  43. Paredes-López, O. (2018). Amaranth biology, chemistry and technology. CRC Press.
  44. Pezeshk, S., Rezaei, M., Hosseini, H., & Abdollahi, M. (2021). Impact of pH-shift processing combined with ultrasonication on structural and functional properties of proteins isolated from rainbow trout by-products. Food Hydrocolloids, 118, 106768. https://doi.org/10.1016/j.foodhyd.2021.106768 · DOI
  45. Pojić, M., Mišan, A., & Tiwari, B. (2018). Eco-innovative technologies for extraction of proteins for human consumption from renewable protein sources of plant origin. Trends in Food Science & Technology, 75, 93-104. https://doi.org/10.1016/j. tifs.2018.03.010 · DOI
  46. Rastogi, A., & Shukla, S. (2013). Amaranth: A new millennium crop of nutraceutical values. Critical Reviews in Food Science and Nutrition, 53(2), 109-125. https://doi. org/10.1080/10408398.2010.517876 · DOI
  47. Shapiro, A. L., Viñuela, E., & Maizel, J. V. (1967). Molecular weight estimation of polypeptide chains by electrophoresis in SDS polyacrylamide gels. Biochemical and Biophysical Research Communications, 28(5), 815-820.
  48. Shevkani, K., Singh, N., Rana, J. C., & Kaur, A. (2014). Relationship between physicochemical and functional properties of amaranth (Amaranthus hypochondriacus) protein isolates. International Journal of Food Science and Technology, 49(2), 541-550. https://doi.org/10.1111/ijfs.12335 · DOI
  49. Silva-Sánchez, C., González-Castañeda, J., De León-Rodríguez, A., & De La Rosa, A. B. (2004). Functional and rheological properties of amaranth albumins extracted from two Mexican varieties. Plant Foods for Human Nutrition, 59(4), 169-174. https://doi. org/10.1007/s11130-004-0021-6 · DOI
  50. Singh, T. P., Siddiqi, R. A., & Sogi, D. S. (2021). Enzymatic modification of rice bran protein: Impact on structural, antioxidant and functional properties. LWT-Food Science and Technology, 138, 110648. https://doi.org/10.1016/j.lwt.2020.110648 · DOI
  51. Sullivan, A. C., Pangloli, P., & Dia, V. P. (2018). Impact of ultrasonication on the physicochemical properties of sorghum kafirin and in vitro pepsin-pancreatin digestibility of sorghum gluten-like flour. Food Chemistry, 240, 1121-1130. https:// doi.org/10.1016/j.foodchem.2017.08.046 · DOI
  52. Valenzuela, C., Abugoch, L., Tapia, C., & Gamboa, A. (2013). Effect of alkaline extraction on the structure of the protein of quinoa (Chenopodium quinoa Willd.) and its influence on film formation. International Journal of Food Science and Technology, 48 (4), 843-849. https://doi.org/10.1111/ijfs.12035 · DOI
  53. Van der Plancken, I., Van Loey, A., & Hendrickx, M. E. (2007). Foaming properties of egg white proteins affected by heat or high pressure treatment. Journal of Food Engineering, 78, 1410-1426. https://doi.org/10.1016/j.jfoodeng.2006.01.013 · DOI
  54. Ventureira, J. L., Martínez, E. N., & Añon, M. C. (2012). Effect of acid treatment on structural and foaming properties of soy amaranth protein mixtures. Food Hydrocolloids, 29(2), 272-279. https://doi.org/10.1016/j.foodhyd.2012.03.013 · DOI
  55. Vera, A., Valenzuela, M. A., Yazdani-Pedram, M., Tapia, C., & Abugoch, L. (2019). Conformational and physicochemical properties of quinoa proteins affected by different conditions of high-intensity ultrasound treatments. Ultrasonics Sonochemistry, 51, 186-196. https://doi.org/10.1016/j.ultsonch.2018.10.026 · DOI
  56. Wang, H., Wu, J., & Betti, M. (2013). Chemical, rheological and surface morphologic characterisation of spent hen proteins extracted by pH-shift processing with or without the presence of cryoprotectants. Food Chemistry, 139(1-4), 710-719. https://doi.org/10.1016/j.foodchem.2013.01.123 · DOI
  57. Westermeier, R. (2016). Electrophoresis in practice: A guide to methods and applications of DNA and protein separations (5th ed.). Wiley-VCH Verlag GmbH & Co. KGaA. https:// doi.org/10.1002/9783527695188 (Chapter 1). · DOI
  58. Xu, L., Xia, Q., Cao, J., He, J., Zhou, C., Guo, Y., et al. (2021). Ultrasonic effects on the headspace volatilome and protein isolate microstructure of duck liver, as well as their potential correlation mechanism. Ultrasonics Sonochemistry, 71, 105358. https://doi.org/10.1016/j.ultsonch.2020.105358 · DOI
  59. Yildiz, G., Andrade, J., Engeseth, N. E., & Feng, H. (2017). Functionalizing soy protein nano-aggregates with pH-shifting and mano-thermo-sonication. Journal of Colloid and Interface Science, 505, 836-846. https://doi.org/10.1016/j.jcis.2017.06.088 · DOI
  60. Zhao, C., Yin, H., Yan, J., Niu, X., Qi, B., & Liu, J. (2021). Structure and acid-induced gelation properties of soy protein isolate-maltodextrin glycation conjugates with ultrasonic pretreatment. Food Hydrocolloids, 112, 106278. https://doi.org/10.1016/ j.foodhyd.2020.106278 · DOI
  61. Zou, Y., Yang, H., Li, P. P., Zhang, M. H., Zhang, X. X., Xu, W. M., et al. (2019). Effect of different time of ultrasound treatment on physicochemical, thermal, and antioxidant properties of chicken plasma protein. Poultry Science, 98(4), 1925-1933. https://doi. org/10.3382/ps/ · DOI

Cited by

Sorted by citations

Authors
Figueroa-González, J. J., Lobato-Calleros, C., Vernon-Carter, E. J., Aguirre-Mandujano, E., Alvarez-Ramirez, J., & Martínez-Velasco, A.
ORCID
Venue
LWT
Publisher
Elsevier BV
Published
2022-01
Volume
153
Pages
112561
ISSN
0023-6438
DOI
10.1016/j.lwt.2021.112561
Cited by
124
References
0
Language
en
Licence
Funders
Consejo Nacional de Ciencia y Tecnología

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review