Luis Ramiro Caso Vargas, Norma Angélica Caballero Concha, Leslie Susana Arcila Lozano, Raúl Delgado-Macuil, Efraín Rubio-Rosas, Alma Delia Luna González, Melisa Carmona López, Andrea Lizbeth Cortés Noriega, Xquenda Ríos Aguilar, Erick Saúl González Méndez
{"title":"基于二胺氧化酶的生物胺检测传感器的表征,该传感器使用脂肪和芳香二醛作为交联剂组装在功能化的二氧化硅底物上","authors":"Luis Ramiro Caso Vargas, Norma Angélica Caballero Concha, Leslie Susana Arcila Lozano, Raúl Delgado-Macuil, Efraín Rubio-Rosas, Alma Delia Luna González, Melisa Carmona López, Andrea Lizbeth Cortés Noriega, Xquenda Ríos Aguilar, Erick Saúl González Méndez","doi":"10.1080/19476337.2023.2256820","DOIUrl":null,"url":null,"abstract":"Development of two biosensors to detect biogenic amines was carried out using immobilized diamine oxidase from Pisum sativum on 3-APTMS-functionalized SiO2 substrates with either glutaraldehyde or terephthalaldehyde as crosslinkers. The assembly process was validated by FT-IR, SEM-EDX, and AFM. Biosensor responses to biogenic amines were c.a. 3-fold lower compared to the free enzyme kinetics as assessed by UV/VIS spectrophotometry. The calculated initial velocities (ΔAbs·min-1) for glutaraldehyde and terephthalaldehyde biosensors in the given order were (3.2 ± 0.68) × 10–2, (0.48 ± 0.09) × 10–2 for putrescine; (4.6 ± 1.2) × 10–2, (0.35 ± 0.47) × 10–2 for cadaverine; (5.8 ± 2.4) × 10–3, (19.0 ± 155) × 10–3 for spermidine, and (3.0 ± 2.0) × 10–4, (0.0 ± 7) × 10–4for histamine. The 2-way t-tests indicated that the crosslinker type affected the catalytic activity of immobilized diamine oxidase as the responses of glutaraldehyde biosensors to putrescine and cadaverine were significantly higher than those of the terephthalaldehyde. Molecular Docking simulations showed that glutaraldehyde has a stronger affinity for DAO’s lysine and arginine residues while terephthalaldehyde to phenylalanine.","PeriodicalId":49084,"journal":{"name":"Cyta-Journal of Food","volume":null,"pages":null},"PeriodicalIF":2.1000,"publicationDate":"2023-09-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Characterization of diamine oxidase-based biosensors for biogenic amines detection assembled onto functionalized SiO₂ substrates using aliphatic and aromatic di-aldehydes as crosslinkers\",\"authors\":\"Luis Ramiro Caso Vargas, Norma Angélica Caballero Concha, Leslie Susana Arcila Lozano, Raúl Delgado-Macuil, Efraín Rubio-Rosas, Alma Delia Luna González, Melisa Carmona López, Andrea Lizbeth Cortés Noriega, Xquenda Ríos Aguilar, Erick Saúl González Méndez\",\"doi\":\"10.1080/19476337.2023.2256820\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Development of two biosensors to detect biogenic amines was carried out using immobilized diamine oxidase from Pisum sativum on 3-APTMS-functionalized SiO2 substrates with either glutaraldehyde or terephthalaldehyde as crosslinkers. The assembly process was validated by FT-IR, SEM-EDX, and AFM. Biosensor responses to biogenic amines were c.a. 3-fold lower compared to the free enzyme kinetics as assessed by UV/VIS spectrophotometry. The calculated initial velocities (ΔAbs·min-1) for glutaraldehyde and terephthalaldehyde biosensors in the given order were (3.2 ± 0.68) × 10–2, (0.48 ± 0.09) × 10–2 for putrescine; (4.6 ± 1.2) × 10–2, (0.35 ± 0.47) × 10–2 for cadaverine; (5.8 ± 2.4) × 10–3, (19.0 ± 155) × 10–3 for spermidine, and (3.0 ± 2.0) × 10–4, (0.0 ± 7) × 10–4for histamine. The 2-way t-tests indicated that the crosslinker type affected the catalytic activity of immobilized diamine oxidase as the responses of glutaraldehyde biosensors to putrescine and cadaverine were significantly higher than those of the terephthalaldehyde. Molecular Docking simulations showed that glutaraldehyde has a stronger affinity for DAO’s lysine and arginine residues while terephthalaldehyde to phenylalanine.\",\"PeriodicalId\":49084,\"journal\":{\"name\":\"Cyta-Journal of Food\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":2.1000,\"publicationDate\":\"2023-09-20\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Cyta-Journal of Food\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1080/19476337.2023.2256820\",\"RegionNum\":4,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Cyta-Journal of Food","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1080/19476337.2023.2256820","RegionNum":4,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Characterization of diamine oxidase-based biosensors for biogenic amines detection assembled onto functionalized SiO₂ substrates using aliphatic and aromatic di-aldehydes as crosslinkers
Development of two biosensors to detect biogenic amines was carried out using immobilized diamine oxidase from Pisum sativum on 3-APTMS-functionalized SiO2 substrates with either glutaraldehyde or terephthalaldehyde as crosslinkers. The assembly process was validated by FT-IR, SEM-EDX, and AFM. Biosensor responses to biogenic amines were c.a. 3-fold lower compared to the free enzyme kinetics as assessed by UV/VIS spectrophotometry. The calculated initial velocities (ΔAbs·min-1) for glutaraldehyde and terephthalaldehyde biosensors in the given order were (3.2 ± 0.68) × 10–2, (0.48 ± 0.09) × 10–2 for putrescine; (4.6 ± 1.2) × 10–2, (0.35 ± 0.47) × 10–2 for cadaverine; (5.8 ± 2.4) × 10–3, (19.0 ± 155) × 10–3 for spermidine, and (3.0 ± 2.0) × 10–4, (0.0 ± 7) × 10–4for histamine. The 2-way t-tests indicated that the crosslinker type affected the catalytic activity of immobilized diamine oxidase as the responses of glutaraldehyde biosensors to putrescine and cadaverine were significantly higher than those of the terephthalaldehyde. Molecular Docking simulations showed that glutaraldehyde has a stronger affinity for DAO’s lysine and arginine residues while terephthalaldehyde to phenylalanine.
期刊介绍:
CyTA – Journal of Food is an Open Access journal that publishes original peer-reviewed research papers dealing with a wide range of subjects which are essential to the food scientist and technologist. Topics include: chemical analysis of food; additives and toxins in food; sensory, nutritional and physiological aspects of food; food microbiology and biotechnology; changes during the processing and storage of foods; effect of the use of agrochemicals in foods; quality control in food; and food engineering and technology.