{"title":"探索酶固定化系统中的非线性反应-扩散:整数阶和分数阶建模。","authors":"R Rajaraman","doi":"10.1007/s12010-024-05050-x","DOIUrl":null,"url":null,"abstract":"<p><p>This paper presented a kinetic model of the Langmuir-Hinshelwood-Hougen-Watson (LHHW) type for porous catalysts with simple one-dimensional geometry, including spheres, infinite cylinders, and flat pellets. The model was applied to systems involving immobilized enzymes, where enzymes are attached to porous support materials to enhance stability and reusability. The LHHW model provided a tool for understanding and modeling reaction kinetics in heterogeneous porous catalysts and immobilized enzymes. A nonlinear reaction-diffusion equation was generated using finite-range Fickian diffusion and nonlinear reaction kinetics, crucial for accurately modeling the behavior of immobilized enzymes. This research addressed a gap in the existing literature by introducing fractional derivatives to investigate enzyme reaction kinetics, capturing the complex dynamics of substrate interaction and reaction rates within the porous matrix. An approximation method based on Lucas wavelets was employed to find solutions for substrate concentration and effectiveness factors across various parameter values. The analytical solutions derived from the Lucas wavelet method (LWM) were evaluated against the fourth-order Runge-Kutta method, showing great agreement between the LWM solutions and numerical counterparts. These results optimized diffusion and reaction kinetics, paving the way for advancements in biocatalysis and efficient enzyme reactor design.</p>","PeriodicalId":465,"journal":{"name":"Applied Biochemistry and Biotechnology","volume":null,"pages":null},"PeriodicalIF":3.1000,"publicationDate":"2024-09-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Exploring Nonlinear Reaction-Diffusion in Enzyme Immobilized Systems: Integer and Fractional Order Modeling.\",\"authors\":\"R Rajaraman\",\"doi\":\"10.1007/s12010-024-05050-x\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>This paper presented a kinetic model of the Langmuir-Hinshelwood-Hougen-Watson (LHHW) type for porous catalysts with simple one-dimensional geometry, including spheres, infinite cylinders, and flat pellets. The model was applied to systems involving immobilized enzymes, where enzymes are attached to porous support materials to enhance stability and reusability. The LHHW model provided a tool for understanding and modeling reaction kinetics in heterogeneous porous catalysts and immobilized enzymes. A nonlinear reaction-diffusion equation was generated using finite-range Fickian diffusion and nonlinear reaction kinetics, crucial for accurately modeling the behavior of immobilized enzymes. This research addressed a gap in the existing literature by introducing fractional derivatives to investigate enzyme reaction kinetics, capturing the complex dynamics of substrate interaction and reaction rates within the porous matrix. An approximation method based on Lucas wavelets was employed to find solutions for substrate concentration and effectiveness factors across various parameter values. The analytical solutions derived from the Lucas wavelet method (LWM) were evaluated against the fourth-order Runge-Kutta method, showing great agreement between the LWM solutions and numerical counterparts. These results optimized diffusion and reaction kinetics, paving the way for advancements in biocatalysis and efficient enzyme reactor design.</p>\",\"PeriodicalId\":465,\"journal\":{\"name\":\"Applied Biochemistry and Biotechnology\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":3.1000,\"publicationDate\":\"2024-09-06\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Applied Biochemistry and Biotechnology\",\"FirstCategoryId\":\"5\",\"ListUrlMain\":\"https://doi.org/10.1007/s12010-024-05050-x\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Applied Biochemistry and Biotechnology","FirstCategoryId":"5","ListUrlMain":"https://doi.org/10.1007/s12010-024-05050-x","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
Exploring Nonlinear Reaction-Diffusion in Enzyme Immobilized Systems: Integer and Fractional Order Modeling.
This paper presented a kinetic model of the Langmuir-Hinshelwood-Hougen-Watson (LHHW) type for porous catalysts with simple one-dimensional geometry, including spheres, infinite cylinders, and flat pellets. The model was applied to systems involving immobilized enzymes, where enzymes are attached to porous support materials to enhance stability and reusability. The LHHW model provided a tool for understanding and modeling reaction kinetics in heterogeneous porous catalysts and immobilized enzymes. A nonlinear reaction-diffusion equation was generated using finite-range Fickian diffusion and nonlinear reaction kinetics, crucial for accurately modeling the behavior of immobilized enzymes. This research addressed a gap in the existing literature by introducing fractional derivatives to investigate enzyme reaction kinetics, capturing the complex dynamics of substrate interaction and reaction rates within the porous matrix. An approximation method based on Lucas wavelets was employed to find solutions for substrate concentration and effectiveness factors across various parameter values. The analytical solutions derived from the Lucas wavelet method (LWM) were evaluated against the fourth-order Runge-Kutta method, showing great agreement between the LWM solutions and numerical counterparts. These results optimized diffusion and reaction kinetics, paving the way for advancements in biocatalysis and efficient enzyme reactor design.
期刊介绍:
This journal is devoted to publishing the highest quality innovative papers in the fields of biochemistry and biotechnology. The typical focus of the journal is to report applications of novel scientific and technological breakthroughs, as well as technological subjects that are still in the proof-of-concept stage. Applied Biochemistry and Biotechnology provides a forum for case studies and practical concepts of biotechnology, utilization, including controls, statistical data analysis, problem descriptions unique to a particular application, and bioprocess economic analyses. The journal publishes reviews deemed of interest to readers, as well as book reviews, meeting and symposia notices, and news items relating to biotechnology in both the industrial and academic communities.
In addition, Applied Biochemistry and Biotechnology often publishes lists of patents and publications of special interest to readers.