Class III Peroxidase Activity in the Scutellum as an Indicator of the Final Germination Phase to the Post-Germination in Maize Embryos of the Conic Complex
Mexico is the place of origin of maize. Currently, fifty-nine races of maize have been described, classified into seven groups, and for this study, maize grains from the Conical group were used. The main components of the grain are the pericarp, aleurone, starchy endosperm and embryo; the embryo comprises the scutellum and embryonic axis. The scutellum is essential for germination; its metabolism is associated with the generation of reactive oxygen species; thus, it is protected by various antioxidants, including class III peroxidases (POX). Accordingly, the objectives of this research are to demonstrate that POX is a biochemical indicator of germination, and to relate the germination morphometric parameters with POX activity in the scutellum that was subjected to imbibition using phosphate solutions at different concentrations and pH. The results revealed that POX is inducible and is an indicator of the embryo germination/postgermination phase. Morphometric changes during germination and their relationship with POX activity are similar in embryos of the Conic group from different locations and harvest dates; therefore, this parameter can be used as a marker between grains from the same maize group.
References
[1]
UNICEF (2022) The State of Food Security and Nutrition in the World 2022.
[2]
The World Bank (2025) Food Security Update. https://thedocs.worldbank.org/en/doc/40ebbf38f5a6b68bfc11e5273e1405d4-0090012022/related/Food-Security-Update-115-April-25-2025.pdf
[3]
Chura, J., Mendoza-Cortez, J. and de la Cruz, J. (2019) Doses and Splitting of Nitrogen in Two Sowing Densities of the Flint Yellow Maize Hybrid. Scientia Agropecuaria, 10, 241-248. https://doi.org/10.17268/sci.agropecu.2019.02.09
[4]
Chang, A., Rodríguez, A. and Pile, E. (2018) Evaluación productiva de cinco híbridos de maíz en estado tierno en Villa Darién, Darién. Revista Colón Ciencias, Tecnología y Negocios, 5, 48-54.
[5]
Chamba, M., Cordero, F. and Vásquez, E. (2017) Implicaciones sociales, técnicas y económicas de la comercialización de Zea mays L. (maíz) en el cantón Espíndola, provincia de Loja. Bosques Latitud Cero, 7, 55-70.
[6]
FAO Food and Agriculture Organization (2009) How to Feed the World in 2050. https://www.fao.org/fileadmin/templates/wsfs/docs/expert_paper/How_to_Feed_the_World_in_2050.pdf
[7]
FAO (2025) Crop Prospects and Food Situation. https://doi.org/10.4060/cd4597en
Goodman, M.M. and Bird, R.M. (1977) The Races of Maize IV: Tentative Grouping of 219 Latin American Races. Economic Botany, 31, 204-221. https://doi.org/10.1007/bf02866591
[10]
Anderson, E. (1946) Maize in Mexico a Preliminary Survey. Annals of the Missouri Botanical Garden, 33, 147-247. https://doi.org/10.2307/2394428
[11]
Wellhausen, E.J., Roberts, L.M., Hernández, X. and Mangelsdorf, P.C. (1951) Razas de Maíz En México: Su Origen, Características y Distribución; Folleto técnico No. 5. Oficina de Estudios Especiales, Secretaría de Agricultura y Ganadería de México.
[12]
Hernández, X.E. and Alanís, F. (1970) Estudio morfológico de cinco razas de maíz de la Sierra Madre Occidental de México: Implicaciones filogenéticos y fitogeográficas. Agrociencia, 5, 3-30.
[13]
Sanchez G., J.J. and Goodman, M.M. (1992) Relationships among the Mexican Races of Maize. Economic Botany, 46, 72-85. https://doi.org/10.1007/bf02985256
[14]
Sanchez G., J.J., Goodman, M.M. and Stuber, C.W. (2000) Isozymatic and Morphological Diversity in the Races of Maize of Mexico. Economic Botany, 54, 43-59. https://doi.org/10.1007/bf02866599
[15]
Ruiz Corral, J.A., Durán Puga, N., Sánchez González, J.d.J., Ron Parra, J., González Eguiarte, D.R., Holland, J.B., et al. (2008) Climatic Adaptation and Ecological Descriptors of 42 Mexican Maize Races. Crop Science, 48, 1502-1512. https://doi.org/10.2135/cropsci2007.09.0518
[16]
Lombi, E., Smith, E., Hansen, T.H., Paterson, D., de Jonge, M.D., Howard, D.L., et al. (2010) Megapixel Imaging of (Micro)nutrients in Mature Barley Grains. Journal of Experimental Botany, 62, 273-282. https://doi.org/10.1093/jxb/erq270
[17]
Sánchez-Linares, L., Gavilanes-Ruíz, M., Díaz-Pontones, D., Guzmán-Chávez, F., Calzada-Alejo, V., Zurita-Villegas, V., et al. (2012) Early Carbon Mobilization and Radicle Protrusion in Maize Germination. Journal of Experimental Botany, 63, 4513-4526. https://doi.org/10.1093/jxb/ers130
[18]
Lu, L., Tian, S., Liao, H., Zhang, J., Yang, X., Labavitch, J.M., et al. (2013) Analysis of Metal Element Distributions in Rice (Oryza sativa L.) Seeds and Relocation during Germination Based on X-Ray Fluorescence Imaging of Zn, Fe, K, Ca, and Mn. PLOS ONE, 8, e57360. https://doi.org/10.1371/journal.pone.0057360
[19]
Corona-Carrillo, J.I., González, S., Chávez Nájera, G. and Díaz-Pontones, D. (2024) Antioxidant System of Scutellum during Germination and Early Growth of Maize Seedlings. Agriculture, 14, Article No. 2025. https://doi.org/10.3390/agriculture14112025
[20]
Macleod, A.M. and Palmer, G.H. (1967) Gibberellin from Barley Embryos. Nature, 216, 1342-1343. https://doi.org/10.1038/2161342a0
[21]
Radley, M. (1967) Site of Production of Gibberellin-Like Substances in Germinating Barley Embryos. Planta, 75, 164-171. https://doi.org/10.1007/bf00387132
[22]
Stoddart, J.L., Thomas, H. and Robertson, A. (1973) Protein Synthesis Patterns in Barley Embryos during Germination. Planta, 112, 309-321. https://doi.org/10.1007/bf00390304
[23]
Corona-Carrillo, J.I., Flores-Ponce, M., Chávez-Nájera, G. and Díaz-Pontones, D.M. (2014) Peroxidase Activity in Scutella of Maize in Association with Anatomical Changes during Germination and Grain Storage. SpringerPlus, 3, Article No. 399. https://doi.org/10.1186/2193-1801-3-399
[24]
Mittler, R. (2017) ROS Are Good. Trends in Plant Science, 22, 11-19. https://doi.org/10.1016/j.tplants.2016.08.002
[25]
K？rk？nen, A. and Kuchitsu, K. (2015) Reactive Oxygen Species in Cell Wall Metabolism and Development in Plants. Phytochemistry, 112, 22-32. https://doi.org/10.1016/j.phytochem.2014.09.016
[26]
Wang, P., Liu, W., Han, C., Wang, S., Bai, M. and Song, C. (2024) Reactive Oxygen Species: Multidimensional Regulators of Plant Adaptation to Abiotic Stress and Development. Journal of Integrative Plant Biology, 66, 330-367. https://doi.org/10.1111/jipb.13601
[27]
Welinder, K.G. (1992) Superfamily of Plant, Fungal and Bacterial Peroxidases. Current Opinion in Structural Biology, 2, 388-393. https://doi.org/10.1016/0959-440x(92)90230-5
[28]
Li, S., Zheng, H., Sui, N. and Zhang, F. (2024) Class III Peroxidase: An Essential Enzyme for Enhancing Plant Physiological and Developmental Process by Maintaining the ROS Level: A Review. International Journal of Biological Macromolecules, 283, Article ID: 137331. https://doi.org/10.1016/j.ijbiomac.2024.137331
[29]
Cosio, C. and Dunand, C. (2009) Specific Functions of Individual Class III Peroxidase Genes. Journal of Experimental Botany, 60, 391-408. https://doi.org/10.1093/jxb/ern318
[30]
Kidwai, M., Dhar, Y.V., Gautam, N., Tiwari, M., Ahmad, I.Z., Asif, M.H., et al. (2019) Oryza sativa Class III Peroxidase (OsPRX38) Overexpression in Arabidopsis Thaliana Reduces Arsenic Accumulation Due to Apoplastic Lignification. Journal of Hazardous Materials, 362, 383-393. https://doi.org/10.1016/j.jhazmat.2018.09.029
[31]
Lüthje, S., Meisrimler, C.N., Hopff, D. and M？ller, B. (2011) Phylogeny, Topology, Structure and Functions of Membrane-Bound Class III Peroxidases in Vascular Plants. Phytochemistry, 72, 1124-1135. https://doi.org/10.1016/j.phytochem.2010.11.023
[32]
Lüthje, S. and Martinez-Cortes, T. (2018) Membrane-Bound Class III Peroxidases: Unexpected Enzymes with Exciting Functions. International Journal of Molecular Sciences, 19, Article No. 2876. https://doi.org/10.3390/ijms19102876
[33]
Kis, M. (2004) An N-Terminal Peptide Extension Results in Efficient Expression, but Not Secretion, of a Synthetic Horseradish Peroxidase Gene in Transgenic Tobacco. Annals of Botany, 93, 303-310. https://doi.org/10.1093/aob/mch045
[34]
Costa, M.M.R., Hilliou, F., Duarte, P., Pereira, L.G., Almeida, I., Leech, M., et al. (2008) Molecular Cloning and Characterization of a Vacuolar Class III Peroxidase Involved in the Metabolism of Anticancer Alkaloids in Catharanthus roseus. Plant Physiology, 146, 403-417. https://doi.org/10.1104/pp.107.107060
[35]
Francoz, E., Ranocha, P., Nguyen-Kim, H., Jamet, E., Burlat, V. and Dunand, C. (2015) Roles of Cell Wall Peroxidases in Plant Development. Phytochemistry, 112, 15-21. https://doi.org/10.1016/j.phytochem.2014.07.020
[36]
Veljovi？ Jovanovi？, S., Kukavica, B., Vidovi？, M., Morina, F. and Menckhoff, L. (2018) Class III Peroxidases: Functions, Localization and Redox Regulation of Isoenzymes. In: Gupta, D.K., Palma, J.M. and Corpas, F.J., Eds., Antioxidants and Antioxidant Enzymes in Higher Plants, Springer International Publishing, 269-300. https://doi.org/10.1007/978-3-319-75088-0_13
[37]
Wang, Y., Wang, Q., Zhao, Y., Han, G. and Zhu, S. (2015) Systematic Analysis of Maize Class III Peroxidase Gene Family Reveals a Conserved Subfamily Involved in Abiotic Stress Response. Gene, 566, 95-108. https://doi.org/10.1016/j.gene.2015.04.041
[38]
Hernández-Ruiz, J., Arnao, M.B., Hiner, A.N.P., García-Cánovas, F. and Acosta, M. (2001) Catalase-Like Activity of Horseradish Peroxidase: Relationship to Enzyme Inactivation by H2O2. Biochemical Journal, 354, 107-114. https://doi.org/10.1042/bj3540107
[39]
Barceló, A.R., Ros, L.V.G. and Carrasco, A.E. (2007) Looking for Syringyl Peroxidases. Trends in Plant Science, 12, 486-491. https://doi.org/10.1016/j.tplants.2007.09.002
[40]
Shigeto, J. and Tsutsumi, Y. (2016) Diverse Functions and Reactions of Class III Peroxidases. New Phytologist, 209, 1395-1402. https://doi.org/10.1111/nph.13738
[41]
Passardi, F., Cosio, C., Penel, C. and Dunand, C. (2005) Peroxidases Have More Functions than a Swiss Army Knife. Plant Cell Reports, 24, 255-265. https://doi.org/10.1007/s00299-005-0972-6
[42]
Amaya, I., Botella, M.A., de la Calle, M., Medina, M.I., Heredia, A., Bressan, R.A., et al. (1999) Improved Germination under Osmotic Stress of Tobacco Plants Overexpressing a Cell Wall Peroxidase. FEBS Letters, 457, 80-84. https://doi.org/10.1016/s0014-5793(99)01011-x
[43]
Jemmat, A.M., Ranocha, P., Le Ru, A., Neel, M., Jauneau, A., Raggi, S., et al. (2020) Coordination of Five Class III Peroxidase-Encoding Genes for Early Germination Events of Arabidopsis Thaliana. Plant Science, 298, Article ID: 110565. https://doi.org/10.1016/j.plantsci.2020.110565
[44]
Hofmann, A., Wienkoop, S., Harder, S., Bartlog, F. and Lüthje, S. (2020) Hypoxia-responsive Class III Peroxidases in Maize Roots: Soluble and Membrane-Bound Isoenzymes. International Journal of Molecular Sciences, 21, Article No. 8872. https://doi.org/10.3390/ijms21228872
[45]
Cosio, C., Vuillemin, L., De Meyer, M., Kevers, C., Penel, C. and Dunand, C. (2009) An Anionic Class III Peroxidase from Zucchini May Regulate Hypocotyl Elongation through Its Auxin Oxidase Activity. Planta, 229, 823-836. https://doi.org/10.1007/s00425-008-0876-0
[46]
Schopfer, P. (2001) Hydroxyl Radical-induced Cell-wall Loosening in Vitro and in Vivo : Implications for the Control of Elongation Growth. The Plant Journal, 28, 679-688. https://doi.org/10.1046/j.1365-313x.2001.01187.x
[47]
Schopfer, P., Plachy, C. and Frahry, G. (2001) Release of Reactive Oxygen Intermediates (Superoxide Radicals, Hydrogen Peroxide, and Hydroxyl Radicals) and Peroxidase in Germinating Radish Seeds Controlled by Light, Gibberellin, and Abscisic Acid. Plant Physiology, 125, 1591-1602. https://doi.org/10.1104/pp.125.4.1591
[48]
Liszkay, A., Kenk, B. and Schopfer, P. (2003) Evidence for the Involvement of Cell Wall Peroxidase in the Generation of Hydroxyl Radicals Mediating Extension Growth. Planta, 217, 658-667. https://doi.org/10.1007/s00425-003-1028-1
[49]
Passardi, F., Penel, C. and Dunand, C. (2004) Performing the Paradoxical: How Plant Peroxidases Modify the Cell Wall. Trends in Plant Science, 9, 534-540. https://doi.org/10.1016/j.tplants.2004.09.002
[50]
Passardi, F., Tognolli, M., De Meyer, M., Penel, C. and Dunand, C. (2006) Two Cell Wall Associated Peroxidases from Arabidopsis Influence Root Elongation. Planta, 223, 965-974. https://doi.org/10.1007/s00425-005-0153-4
[51]
Jin, J., Hewezi, T. and Baum, T.J. (2011) Arabidopsis Peroxidase AtPRX53 Influences Cell Elongation and Susceptibility to Heterodera schachtii. Plant Signaling & Behavior, 6, 1778-1786. https://doi.org/10.4161/psb.6.11.17684
[52]
Kunieda, T., Shimada, T., Kondo, M., Nishimura, M., Nishitani, K. and Hara-Nishimura, I. (2013) Spatiotemporal Secretion of PEROXIDASE36 Is Required for Seed Coat Mucilage Extrusion in Arabidopsis. The Plant Cell, 25, 1355-1367. https://doi.org/10.1105/tpc.113.110072
[53]
Mishler-Elmore, J.W., Zhou, Y., Sukul, A., Oblak, M., Tan, L., Faik, A., et al. (2021) Extensins: Self-Assembly, Crosslinking, and the Role of Peroxidases. Frontiers in Plant Science, 12, Article ID: 664738. https://doi.org/10.3389/fpls.2021.664738
[54]
Brownleader, M.D., Hopkins, J., Mobasheri, A., Dey, P.M., Jackson, P. and Trevan, M. (2000) Role of Extensin Peroxidase in Tomato (Lycopersicon esculentum Mill.) Seedling Growth. Planta, 210, 668-676. https://doi.org/10.1007/s004250050058
[55]
Fry, S.C. (2004) Oxidative Coupling of Tyrosine and Ferulic Acid Residues: Intra-and Extra-Protoplasmic Occurrence, Predominance of Trimers and Larger Products, and Possible Role in Inter-Polymeric Cross-Linking. Phytochemistry Reviews, 3, 97-111. https://doi.org/10.1023/b:phyt.0000047808.74647.43
[56]
Pedreira, J., Herrera, M.T., Zarra, I. and Revilla, G. (2011) The Overexpression of AtPrx37, an Apoplastic Peroxidase, Reduces Growth in Arabidopsis. Physiologia Plantarum, 141, 177-187. https://doi.org/10.1111/j.1399-3054.2010.01427.x
[57]
Herrero, J., Fernández-Pérez, F., Yebra, T., Novo-Uzal, E., Pomar, F., Pedre？o, M.á., et al. (2013) Bioinformatic and Functional Characterization of the Basic Peroxidase 72 from Arabidopsis Thaliana Involved in Lignin Biosynthesis. Planta, 237, 1599-1612. https://doi.org/10.1007/s00425-013-1865-5
[58]
Lee, Y., Rubio, M.C., Alassimone, J. and Geldner, N.A. (2013) A Mechanism for Localized Lignin Deposition in the Endodermis. Cell, 153, 402-412. https://doi.org/10.1016/j.cell.2013.02.045
[59]
Shigeto, J., Kiyonaga, Y., Fujita, K., Kondo, R. and Tsutsumi, Y. (2013) Putative Cationic Cell-Wall-Bound Peroxidase Homologues in Arabidopsis, AtPrx2, AtPrx25, and AtPrx71, Are Involved in Lignification. Journal of Agricultural and Food Chemistry, 61, 3781-3788. https://doi.org/10.1021/jf400426g
[60]
？stergaard, L., Teilum, K., Mirza, O., Mattsson, O., Petersen, M., Welinder, K.G., et al. (2000) Arabidopsis ATP A2 Peroxidase. Expression and High-Resolution Structure of a Plant Peroxidase with Implications for Lignification. Plant Molecular Biology, 44, 231-243. https://doi.org/10.1023/a:1006442618860
[61]
Chen, Y.-A., Shin, J.-W. and Liu, Z.-H. (2002) Effect of Light on Peroxidase and Lignin Synthesis in Mungbean Hypocotyls. Plant Physiology and Biochemistry, 40, 33-39. https://doi.org/10.1016/s0981-9428(01)01345-6
[62]
Sim？es, M.S., Carvalho, G.G., Ferreira, S.S. and Cesarino, I. (2023) Toward the Identification of Class III Peroxidases Potentially Involved in Lignification in the Model C4 Grass Setaria viridis. Theoretical and Experimental Plant Physiology, 35, 111-131. https://doi.org/10.1007/s40626-023-00273-5
[63]
Delmer, D., Dixon, R.A., Keegstra, K. and Mohnen, D. (2024) The Plant Cell Wall—Dynamic, Strong, and Adaptable—Is a Natural Shapeshifter. The Plant Cell, 36, 1257-1311. https://doi.org/10.1093/plcell/koad325
[64]
Aleem, M., Riaz, A., Raza, Q., Aleem, M., Aslam, M., Kong, K., et al. (2022) Genome-wide Characterization and Functional Analysis of Class III Peroxidase Gene Family in Soybean Reveal Regulatory Roles of GsPOD40 in Drought Tolerance. Genomics, 114, 45-60. https://doi.org/10.1016/j.ygeno.2021.11.016
[65]
Zhang, H., Wang, Z., Li, X., Gao, X., Dai, Z., Cui, Y., et al. (2021) The IbBBX24-IbTOE3-IbPRX17 Module Enhances Abiotic Stress Tolerance by Scavenging Reactive Oxygen Species in Sweet Potato. New Phytologist, 233, 1133-1152. https://doi.org/10.1111/nph.17860
Su, P., Yan, J., Li, W., Wang, L., Zhao, J., Ma, X., et al. (2020) A Member of Wheat Class III Peroxidase Gene Family, TaPRX-2A, Enhanced the Tolerance of Salt Stress. BMC Plant Biology, 20, Article No. 392. https://doi.org/10.1186/s12870-020-02602-1
[68]
Kumar, S., Jaggi, M. and Sinha, A.K. (2012) Ectopic Overexpression of Vacuolar and Apoplastic Catharanthus Roseus Peroxidases Confers Differential Tolerance to Salt and Dehydration Stress in Transgenic Tobacco. Protoplasma, 249, 423-432. https://doi.org/10.1007/s00709-011-0294-1
[69]
Li, Q., Qin, X., Qi, J., Dou, W., Dunand, C., Chen, S. and He, Y. (2020) CsPrx25, a Class III Peroxidase in Citrus Sinensis, Confers Resistance to Citrus Bacterial Canker through the Maintenance of ROS Homeostasis and Cell Wall Lignification. Horticulture Research, 7, Article No. 192.
[70]
Wang, C.-J., Chan, Y.-L., Shien, C.H. and Yeh, K.-W. (2015) Molecular Characterization of Fruit-Specific Class III Peroxidase Genes in Tomato (Solanum lycopersicum). Journal of Plant Physiology, 177, 83-92. https://doi.org/10.1016/j.jplph.2015.01.011
[71]
Kim, Y.-H., Kim, C.Y., Song, W.-K., Park, D.-S., Kwon, S.-Y., Lee, H.-S., et al. (2008) Overexpression of Sweetpotato Swpa4 Peroxidase Results in Increased Hydrogen Peroxide Production and Enhances Stress Tolerance in Tobacco. Planta, 227, 867-881. https://doi.org/10.1007/s00425-007-0663-3
[72]
Coego, A., Ramirez, V., Gil, M.J., Flors, V., Mauch-Mani, B. and Vera, P. (2005) An Arabidopsis Homeodomain Transcription Factor, Overexpressor of Cationic Peroxidase 3, Mediates Resistance to Infection by Necrotrophic Pathogens. The Plant Cell, 17, 2123-2137. https://doi.org/10.1105/tpc.105.032375
[73]
Liszkay, A., van der Zalm, E. and Schopfer, P. (2004) Production of Reactive Oxygen Intermediates (O？ 2, H2O2, and OH) by Maize Roots and Their Role in Wall Loosening and Elongation Growth. Plant Physiology, 136, 3114-3123. https://doi.org/10.1104/pp.104.044784
[74]
García-Lara, S., Arnason, J.T., Díaz-Pontones, D., Gonzalez, E. and Bergvinson, D.J. (2007) Soluble Peroxidase Activity in Maize Endosperm Associated with Maize Weevil Resistance. Crop Science, 47, 1125-1130. https://doi.org/10.2135/cropsci2006.10.0687
[75]
Lefebvre, D.D., Duff, S.M.G., Fife, C.A., Julien-Inalsingh, C. and Plaxton, W.C. (1990) Response to Phosphate Deprivation in Brassica nigra Suspension Cells: Enhancement of Intracellular, Cell Surface, and Secreted Phosphatase Activities Compared to Increases in Pi-Absorption Rate. Plant Physiology, 93, 504-511. https://doi.org/10.1104/pp.93.2.504
[76]
Taiz, L., Zeiger, E. and Murphy, A. (2015) Plant Physiology and Development. 6th Edition, Sinauer Associates.
[77]
Ferreira, C.V., Taga, E.M. and Aoyama, H. (2000) Inhibition of Acid Phosphatase Isoforms Purified from Mature Soybean (Glyczne MAX) Seeds. Journal of Enzyme Inhibition, 15, 403-410. https://doi.org/10.1080/14756360009040696
[78]
Mohamed, N.G., Ahmed, M., Mohammed, E., Emad, B., Mohamed, M., Mostafa, A., et al. (2026) Seed Priming Enhances Physiological and Biochemical Adaptation of Food Crops to Abiotic and Biotic Stresses under Global Warming. Discover Plants, 3, Article No. 120. https://doi.org/10.1007/s44372-026-00580-6
[79]
Díaz-Pontones, D.M., Corona-Carrillo, J.I., Herrera-Miranda, C. and González, S. (2021) Excess Zinc Alters Cell Wall Class III Peroxidase Activity and Flavonoid Content in the Maize Scutellum. Plants, 10, Article No. 197. https://doi.org/10.3390/plants10020197
[80]
Caramori, S.S., Ramalho, R.P.R.S. and Scalize, P.S. (2016) Peroxidase de gramínea de Cerrado como alternativa no tratamento de efluentes agroindustriais. Ambiente e Agua—An Interdisciplinary Journal of Applied Science, 11, 50-59. https://doi.org/10.4136/ambi-agua.1735
[81]
Fernandes, M., Souza, D.H., Henriques, R.O., Alves, M.V., Skoronski, E. and Junior, A.F. (2020) Obtaining Soybean Peroxidase from Soybean Hulls and Its Application for Detoxification of 2,4-Dichlorophenol Contaminated Water. Journal of Environmental Chemical Engineering, 8, Article ID: 103786. https://doi.org/10.1016/j.jece.2020.103786
[82]
Maehly, A.C. (1954) The Assay of Catalases and Peroxidases. In: Glick, D., Ed., Methods of Bio-Chemical Analysis, Vol. 1, Wiley, 357-424.
[83]
Zeraik, A.E., Souza, F.S.d., Fatibello-Filho, O. and Leite, O.D. (2008) Desenvolvimento de um spot test para o monitoramento da atividade da peroxidase em um procedimento de purifica？？o. Química Nova, 31, 731-734. https://doi.org/10.1590/s0100-40422008000400003
[84]
Oh, J., Kim, B.C. and Lee, J. (2014) Colorimetric Detection of Acetylcholine with Plasmonic Nanomaterials Signaling. Analytical and Bioanalytical Chemistry, 406, 7591-7600. https://doi.org/10.1007/s00216-014-8199-4
[85]
de Oliveira, F.K., Santos, L.O. and Buffon, J.G. (2021) Mechanism of Action, Sources, and Application of Peroxidases. Food Research International, 143, Article ID: 110266. https://doi.org/10.1016/j.foodres.2021.110266
[86]
López-Serrano, M. and Barceló, A.R. (1997) Kinetic Properties of (+)-Catechin Oxidation by a Basic Peroxidase Isoenzyme from Strawberries. Journal of Food Science, 62, 676-723. https://doi.org/10.1111/j.1365-2621.1997.tb15433.x
[87]
López-Serrano, M. and Ros Barceló, A. (2001) Reversed-Phase and Size-Exclusion Chromatography as Useful Tools in the Resolution of Peroxidase-Mediated (+)-Catechin Oxidation Products. Journal of Chromatography A, 919, 267-273. https://doi.org/10.1016/s0021-9673(01)00817-2
[88]
López-Serrano, M. and Ros Barceló, A. (2002) Comparative Study of the Products of the Peroxidase-Catalyzed and the Polyphenoloxidase-Catalyzed (+)-Catechin Oxidation. Their Possible Implications in Strawberry (Fragaria × ananassa) Browning Reactions. Journal of Agricultural and Food Chemistry, 50, 1218-1224. https://doi.org/10.1021/jf010902z
[89]
Herrera-Cabrera, B.E., Castillo-González, F., Sánchez-González, J.d.J., Ortega-Paczka, R. and M.-Goodman, M. (2022) Caracteres morfológicos para valorar la diversidad entre poblaciones de maíz en una región: Caso la raza Chalque？o. Revista Fitotecnia Mexicana, 23, 335-354. https://doi.org/10.35196/rfm.2000.2.335
[90]
Herrera Cabrera, B.E., Castillo González, F., de Sánchez González, J.J., Hérnandez-Casillas J.M., Ortega Paczka, R. and Goodman, M.M. (2004) Diversity of Chalque？o Maize. Agrociencia, 38, 191-206.
