{"title":"海藻酸盐基复合微球脲酶的固定化","authors":"Demet Baybaş","doi":"10.1016/j.ab.2025.115867","DOIUrl":null,"url":null,"abstract":"<div><div>The aim of this research is to investigate the contribution of incorporating Aloe Vera (<em>Aloe barbadensis</em>) (Av), sepiolite (Sp) and carrageenan (Cr) to alginate beads in immobilizing urease enzyme. For this purpose, only alginate (A), AAv, ASp and ACr composite beads were synthesized. Simultaneously, the enzyme-immobilized beads (A-U, AAv-U, ASp-U and ACr-U) were formed by co-synthesis in the presence of urease. All prepared beads were characterized by FTIR analysis and SEM images. The optimum pH and temperature values of the immobilized enzyme activity were determined and compared with those of the free enzyme. The optimum pHs were 7 for free enzyme, AAv-U, Asp-U enzymes, 8 for ACr, and 4.5 for A-U. While the optimum temperature for free enzyme was around 20 °C, immobilized enzymes showed high activity at higher temperatures. In addition, the re-usability and storage stability of the enzyme-immobilized beads were investigated at two different temperatures and in two different environments. Michaelis-Menten constants were determined by studying the variation of enzyme activity with substrate concentration.</div></div>","PeriodicalId":7830,"journal":{"name":"Analytical biochemistry","volume":"703 ","pages":"Article 115867"},"PeriodicalIF":2.6000,"publicationDate":"2025-04-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Urease immobilization on alginate-based composite micro-beads\",\"authors\":\"Demet Baybaş\",\"doi\":\"10.1016/j.ab.2025.115867\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>The aim of this research is to investigate the contribution of incorporating Aloe Vera (<em>Aloe barbadensis</em>) (Av), sepiolite (Sp) and carrageenan (Cr) to alginate beads in immobilizing urease enzyme. For this purpose, only alginate (A), AAv, ASp and ACr composite beads were synthesized. Simultaneously, the enzyme-immobilized beads (A-U, AAv-U, ASp-U and ACr-U) were formed by co-synthesis in the presence of urease. All prepared beads were characterized by FTIR analysis and SEM images. The optimum pH and temperature values of the immobilized enzyme activity were determined and compared with those of the free enzyme. The optimum pHs were 7 for free enzyme, AAv-U, Asp-U enzymes, 8 for ACr, and 4.5 for A-U. While the optimum temperature for free enzyme was around 20 °C, immobilized enzymes showed high activity at higher temperatures. In addition, the re-usability and storage stability of the enzyme-immobilized beads were investigated at two different temperatures and in two different environments. Michaelis-Menten constants were determined by studying the variation of enzyme activity with substrate concentration.</div></div>\",\"PeriodicalId\":7830,\"journal\":{\"name\":\"Analytical biochemistry\",\"volume\":\"703 \",\"pages\":\"Article 115867\"},\"PeriodicalIF\":2.6000,\"publicationDate\":\"2025-04-14\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Analytical biochemistry\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0003269725001058\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"BIOCHEMICAL RESEARCH METHODS\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Analytical biochemistry","FirstCategoryId":"99","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0003269725001058","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"BIOCHEMICAL RESEARCH METHODS","Score":null,"Total":0}
Urease immobilization on alginate-based composite micro-beads
The aim of this research is to investigate the contribution of incorporating Aloe Vera (Aloe barbadensis) (Av), sepiolite (Sp) and carrageenan (Cr) to alginate beads in immobilizing urease enzyme. For this purpose, only alginate (A), AAv, ASp and ACr composite beads were synthesized. Simultaneously, the enzyme-immobilized beads (A-U, AAv-U, ASp-U and ACr-U) were formed by co-synthesis in the presence of urease. All prepared beads were characterized by FTIR analysis and SEM images. The optimum pH and temperature values of the immobilized enzyme activity were determined and compared with those of the free enzyme. The optimum pHs were 7 for free enzyme, AAv-U, Asp-U enzymes, 8 for ACr, and 4.5 for A-U. While the optimum temperature for free enzyme was around 20 °C, immobilized enzymes showed high activity at higher temperatures. In addition, the re-usability and storage stability of the enzyme-immobilized beads were investigated at two different temperatures and in two different environments. Michaelis-Menten constants were determined by studying the variation of enzyme activity with substrate concentration.
期刊介绍:
The journal''s title Analytical Biochemistry: Methods in the Biological Sciences declares its broad scope: methods for the basic biological sciences that include biochemistry, molecular genetics, cell biology, proteomics, immunology, bioinformatics and wherever the frontiers of research take the field.
The emphasis is on methods from the strictly analytical to the more preparative that would include novel approaches to protein purification as well as improvements in cell and organ culture. The actual techniques are equally inclusive ranging from aptamers to zymology.
The journal has been particularly active in:
-Analytical techniques for biological molecules-
Aptamer selection and utilization-
Biosensors-
Chromatography-
Cloning, sequencing and mutagenesis-
Electrochemical methods-
Electrophoresis-
Enzyme characterization methods-
Immunological approaches-
Mass spectrometry of proteins and nucleic acids-
Metabolomics-
Nano level techniques-
Optical spectroscopy in all its forms.
The journal is reluctant to include most drug and strictly clinical studies as there are more suitable publication platforms for these types of papers.