Yashuang Hei , Lisi Ba , Ling Yu , Bingxiao Zheng , Sisi Wen , Nan Ma , Zhiju Zhao
{"title":"一种将辣根过氧化物酶和乳酸氧化酶共同固定在甘蔗基三维碳纳米球交联碳气凝胶上的双酶乳酸生物传感器","authors":"Yashuang Hei , Lisi Ba , Ling Yu , Bingxiao Zheng , Sisi Wen , Nan Ma , Zhiju Zhao","doi":"10.1016/j.snr.2025.100383","DOIUrl":null,"url":null,"abstract":"<div><div>In this work, a novel bienzymatic lactate biosensor was developed by co-immobilization of lactate oxidase (LOD) and horseradish peroxidase (HRP) onto the screen-printed electrode (SPE) modified by the three-dimensional (3D) carbon nanoballs cross-linked carbon aerogels (3D-CNCAs), which is derived from the biomass of sugarcane. The 3D-CNCAs, with large surface area and porous structure, play a crucial role in facilitating direct electron transfer between the electroactive center of HRP and the biosensor electrode. The experimental parameters including the amount of 3D-CNCAs suspension, the ratio of the two enzymes, the buffer pH and the operation potential were optimized. The bienzymatic lactate biosensor exhibits linear current response for lactate in the concentration ranges of 1-1690 μM, with a detection limit of 0.23 μM (S/N = 3), which is superior to the one based on monotypic enzyme of LOD. The bienzymatic lactate biosensor also exhibits a high level of selectivity, reproducibility, repeatability and long-term stability (87% of the original value after storage for 30 days), and was further applied in lactate detection in diluted real samples of lactic acid cream and commercial beverage. The outstanding analytical performance of the bienzymatic lactate biosensor demonstrates the preponderance of the bienzymatic over the one based on monotypic enzyme, and holds broad application prospects in the future.</div></div>","PeriodicalId":426,"journal":{"name":"Sensors and Actuators Reports","volume":"10 ","pages":"Article 100383"},"PeriodicalIF":7.6000,"publicationDate":"2025-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"A bienzymatic lactate biosensor with co-immobilization of horseradish peroxidase and lactate oxidase on sugarcane-derived three-dimensional carbon nanoballs cross-linked carbon aerogels\",\"authors\":\"Yashuang Hei , Lisi Ba , Ling Yu , Bingxiao Zheng , Sisi Wen , Nan Ma , Zhiju Zhao\",\"doi\":\"10.1016/j.snr.2025.100383\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>In this work, a novel bienzymatic lactate biosensor was developed by co-immobilization of lactate oxidase (LOD) and horseradish peroxidase (HRP) onto the screen-printed electrode (SPE) modified by the three-dimensional (3D) carbon nanoballs cross-linked carbon aerogels (3D-CNCAs), which is derived from the biomass of sugarcane. The 3D-CNCAs, with large surface area and porous structure, play a crucial role in facilitating direct electron transfer between the electroactive center of HRP and the biosensor electrode. The experimental parameters including the amount of 3D-CNCAs suspension, the ratio of the two enzymes, the buffer pH and the operation potential were optimized. The bienzymatic lactate biosensor exhibits linear current response for lactate in the concentration ranges of 1-1690 μM, with a detection limit of 0.23 μM (S/N = 3), which is superior to the one based on monotypic enzyme of LOD. The bienzymatic lactate biosensor also exhibits a high level of selectivity, reproducibility, repeatability and long-term stability (87% of the original value after storage for 30 days), and was further applied in lactate detection in diluted real samples of lactic acid cream and commercial beverage. The outstanding analytical performance of the bienzymatic lactate biosensor demonstrates the preponderance of the bienzymatic over the one based on monotypic enzyme, and holds broad application prospects in the future.</div></div>\",\"PeriodicalId\":426,\"journal\":{\"name\":\"Sensors and Actuators Reports\",\"volume\":\"10 \",\"pages\":\"Article 100383\"},\"PeriodicalIF\":7.6000,\"publicationDate\":\"2025-09-17\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Sensors and Actuators Reports\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S2666053925001018\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"BIOTECHNOLOGY & APPLIED MICROBIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Sensors and Actuators Reports","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S2666053925001018","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"BIOTECHNOLOGY & APPLIED MICROBIOLOGY","Score":null,"Total":0}
A bienzymatic lactate biosensor with co-immobilization of horseradish peroxidase and lactate oxidase on sugarcane-derived three-dimensional carbon nanoballs cross-linked carbon aerogels
In this work, a novel bienzymatic lactate biosensor was developed by co-immobilization of lactate oxidase (LOD) and horseradish peroxidase (HRP) onto the screen-printed electrode (SPE) modified by the three-dimensional (3D) carbon nanoballs cross-linked carbon aerogels (3D-CNCAs), which is derived from the biomass of sugarcane. The 3D-CNCAs, with large surface area and porous structure, play a crucial role in facilitating direct electron transfer between the electroactive center of HRP and the biosensor electrode. The experimental parameters including the amount of 3D-CNCAs suspension, the ratio of the two enzymes, the buffer pH and the operation potential were optimized. The bienzymatic lactate biosensor exhibits linear current response for lactate in the concentration ranges of 1-1690 μM, with a detection limit of 0.23 μM (S/N = 3), which is superior to the one based on monotypic enzyme of LOD. The bienzymatic lactate biosensor also exhibits a high level of selectivity, reproducibility, repeatability and long-term stability (87% of the original value after storage for 30 days), and was further applied in lactate detection in diluted real samples of lactic acid cream and commercial beverage. The outstanding analytical performance of the bienzymatic lactate biosensor demonstrates the preponderance of the bienzymatic over the one based on monotypic enzyme, and holds broad application prospects in the future.
期刊介绍:
Sensors and Actuators Reports is a peer-reviewed open access journal launched out from the Sensors and Actuators journal family. Sensors and Actuators Reports is dedicated to publishing new and original works in the field of all type of sensors and actuators, including bio-, chemical-, physical-, and nano- sensors and actuators, which demonstrates significant progress beyond the current state of the art. The journal regularly publishes original research papers, reviews, and short communications.
For research papers and short communications, the journal aims to publish the new and original work supported by experimental results and as such purely theoretical works are not accepted.