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Enzyme-based amperometric galactose biosensors: a review
This review (with 35 references) summarizes the various strategies used in biosensors for galactose, and their analytical performance. A brief comparison of the enzyme immobilization methods employed and the analytical performance characteristics of a range of galactose biosensors are first summariz...
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| Published in: | Mikrochimica acta (1966) 2017-10, Vol.184 (10), p.3663-3671 |
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| Main Authors: | , , , |
| Format: | Article |
| Language: | English |
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| cited_by | cdi_FETCH-LOGICAL-c537t-8f022ad5188269f410a5ff8579631d507ef7d4edc22217f06a030e41219231603 |
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| cites | cdi_FETCH-LOGICAL-c537t-8f022ad5188269f410a5ff8579631d507ef7d4edc22217f06a030e41219231603 |
| container_end_page | 3671 |
| container_issue | 10 |
| container_start_page | 3663 |
| container_title | Mikrochimica acta (1966) |
| container_volume | 184 |
| creator | Kanyong, Prosper Krampa, Francis D. Aniweh, Yaw Awandare, Gordon A. |
| description | This review (with 35 references) summarizes the various strategies used in biosensors for galactose, and their analytical performance. A brief comparison of the enzyme immobilization methods employed and the analytical performance characteristics of a range of galactose biosensors are first summarized in tabular form and then described in detail. Selected examples have been included to demonstrate the various applications of these biosensors to real samples. Following an introduction into the field that covers the significance of sensing galactose in various fields, the review covers biosensors based on the use of galactose oxidase, with a discussion of methods for their immobilization (via cross-linking, adsorption, covalent bonding and entrapment). This is followed by a short section on biosensors based on the use of galactose dehydrogenase. The conclusion section summarizes the state of the art and addresses current challenges.
Graphical abstract
Fabrication of a disposable screen-printed (a) electrochemical galactose biosensor (b) for real sample analysis and a dummy biosensor (c) for compensating the effect of interferences |
| doi_str_mv | 10.1007/s00604-017-2465-z |
| format | article |
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Graphical abstract
Fabrication of a disposable screen-printed (a) electrochemical galactose biosensor (b) for real sample analysis and a dummy biosensor (c) for compensating the effect of interferences</description><identifier>ISSN: 0026-3672</identifier><identifier>EISSN: 1436-5073</identifier><identifier>DOI: 10.1007/s00604-017-2465-z</identifier><identifier>PMID: 28979051</identifier><language>eng</language><publisher>Vienna: Springer Vienna</publisher><subject>Analytical Chemistry ; Biosensing Techniques - methods ; Biosensors ; Characterization and Evaluation of Materials ; Chemical bonds ; Chemistry ; Chemistry and Materials Science ; Comparative analysis ; Crosslinking ; Electrical measurement ; Electrochemical Techniques - methods ; Entrapment ; Enzymes ; Enzymes, Immobilized - chemistry ; Galactose ; Galactose - blood ; Galactose - chemistry ; Galactose Dehydrogenases - chemistry ; Galactose Oxidase - chemistry ; Humans ; Immobilization ; Medical equipment ; Microengineering ; Nanochemistry ; Nanotechnology ; Oxidase ; Oxidases ; Physiological apparatus ; Review ; Review Article</subject><ispartof>Mikrochimica acta (1966), 2017-10, Vol.184 (10), p.3663-3671</ispartof><rights>The Author(s) 2017</rights><rights>(c) for compensating the effect of interferences.</rights><rights>COPYRIGHT 2017 Springer</rights><rights>Microchimica Acta is a copyright of Springer, 2017.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c537t-8f022ad5188269f410a5ff8579631d507ef7d4edc22217f06a030e41219231603</citedby><cites>FETCH-LOGICAL-c537t-8f022ad5188269f410a5ff8579631d507ef7d4edc22217f06a030e41219231603</cites><orcidid>0000-0003-2414-6197</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28979051$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kanyong, Prosper</creatorcontrib><creatorcontrib>Krampa, Francis D.</creatorcontrib><creatorcontrib>Aniweh, Yaw</creatorcontrib><creatorcontrib>Awandare, Gordon A.</creatorcontrib><title>Enzyme-based amperometric galactose biosensors: a review</title><title>Mikrochimica acta (1966)</title><addtitle>Microchim Acta</addtitle><addtitle>Mikrochim Acta</addtitle><description>This review (with 35 references) summarizes the various strategies used in biosensors for galactose, and their analytical performance. A brief comparison of the enzyme immobilization methods employed and the analytical performance characteristics of a range of galactose biosensors are first summarized in tabular form and then described in detail. Selected examples have been included to demonstrate the various applications of these biosensors to real samples. Following an introduction into the field that covers the significance of sensing galactose in various fields, the review covers biosensors based on the use of galactose oxidase, with a discussion of methods for their immobilization (via cross-linking, adsorption, covalent bonding and entrapment). This is followed by a short section on biosensors based on the use of galactose dehydrogenase. The conclusion section summarizes the state of the art and addresses current challenges.
Graphical abstract
Fabrication of a disposable screen-printed (a) electrochemical galactose biosensor (b) for real sample analysis and a dummy biosensor (c) for compensating the effect of interferences</description><subject>Analytical Chemistry</subject><subject>Biosensing Techniques - methods</subject><subject>Biosensors</subject><subject>Characterization and Evaluation of Materials</subject><subject>Chemical bonds</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Comparative analysis</subject><subject>Crosslinking</subject><subject>Electrical measurement</subject><subject>Electrochemical Techniques - methods</subject><subject>Entrapment</subject><subject>Enzymes</subject><subject>Enzymes, Immobilized - chemistry</subject><subject>Galactose</subject><subject>Galactose - blood</subject><subject>Galactose - chemistry</subject><subject>Galactose Dehydrogenases - chemistry</subject><subject>Galactose Oxidase - chemistry</subject><subject>Humans</subject><subject>Immobilization</subject><subject>Medical equipment</subject><subject>Microengineering</subject><subject>Nanochemistry</subject><subject>Nanotechnology</subject><subject>Oxidase</subject><subject>Oxidases</subject><subject>Physiological apparatus</subject><subject>Review</subject><subject>Review Article</subject><issn>0026-3672</issn><issn>1436-5073</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><recordid>eNp1kV9rHCEUxaW0NNu0H6AvZaAvfTG96qhjHwohpE0g0Jf0WdyZ69Ywo1udTcl--rps_tMiKHh_51yvh5D3DI4YgP5cABS0FJimvFWSbl-QBWuFohK0eEkWAFxRoTQ_IG9KuYIKKt6-Jge8M9qAZAvSncbtzYR06QoOjZvWmNOEcw59s3Kj6-dUsFmGuseScvnSuCbjdcA_b8kr78aC727PQ_Lz2-nlyRm9-PH9_OT4gvZS6Jl2Hjh3g2Rdx5XxLQMnve-kNkqwob4TvR5aHHrOOdMelAMB2DLODBdMgTgkX_e-681yqhzGObvRrnOYXL6xyQX7tBLDL7tK11ZKo1W3M_h0a5DT7w2W2U6h9DiOLmLaFMtMqxXTnJuKfnyGXqVNjnW8SolOGG50-0DVD0Ibok-1b78ztceaSah9Na_U0T-ougacQp8i-lDvnwjYXtDnVEpGfz8jA7uL2-7jtjVFu4vbbqvmw-PPuVfc5VsBvgdKLcUV5kcT_df1L9eesxI</recordid><startdate>20171001</startdate><enddate>20171001</enddate><creator>Kanyong, Prosper</creator><creator>Krampa, Francis D.</creator><creator>Aniweh, Yaw</creator><creator>Awandare, Gordon A.</creator><general>Springer Vienna</general><general>Springer</general><general>Springer Nature B.V</general><scope>C6C</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FE</scope><scope>8FG</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>M0S</scope><scope>M1P</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-2414-6197</orcidid></search><sort><creationdate>20171001</creationdate><title>Enzyme-based amperometric galactose biosensors: a review</title><author>Kanyong, Prosper ; 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Graphical abstract
Fabrication of a disposable screen-printed (a) electrochemical galactose biosensor (b) for real sample analysis and a dummy biosensor (c) for compensating the effect of interferences</abstract><cop>Vienna</cop><pub>Springer Vienna</pub><pmid>28979051</pmid><doi>10.1007/s00604-017-2465-z</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0003-2414-6197</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | Mikrochimica acta (1966), 2017-10, Vol.184 (10), p.3663-3671 |
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| source | Springer Nature:Jisc Collections:Springer Nature Read and Publish 2023-2025: Springer Reading List |
| subjects | Analytical Chemistry Biosensing Techniques - methods Biosensors Characterization and Evaluation of Materials Chemical bonds Chemistry Chemistry and Materials Science Comparative analysis Crosslinking Electrical measurement Electrochemical Techniques - methods Entrapment Enzymes Enzymes, Immobilized - chemistry Galactose Galactose - blood Galactose - chemistry Galactose Dehydrogenases - chemistry Galactose Oxidase - chemistry Humans Immobilization Medical equipment Microengineering Nanochemistry Nanotechnology Oxidase Oxidases Physiological apparatus Review Review Article |
| title | Enzyme-based amperometric galactose biosensors: a review |
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