Loading…

Application of anodized aluminium oxide as a biochip substrate for a Fabry-Perot interferometer

BACKGROUND: Non‐uniform distribution of pore size and depth of porous Si chip for a Fabry–Perot interferometer, in a previous study, led to relatively low sensitivity with poor reproducibility when its surface was immobilized with calyx crown derivative (Prolinker A). In this study, porous anodized...

Full description

Saved in:
Bibliographic Details
Published in:Journal of chemical technology and biotechnology (1986) 2007-11, Vol.82 (11), p.1045-1052
Main Authors: Lee, Jung-Chul, An, Jin Young, Kim, Byung-Woo
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c3999-dcbe91afa4fac870ea8872552527868c4a8625513611eedcfad2cf935d277d923
cites cdi_FETCH-LOGICAL-c3999-dcbe91afa4fac870ea8872552527868c4a8625513611eedcfad2cf935d277d923
container_end_page 1052
container_issue 11
container_start_page 1045
container_title Journal of chemical technology and biotechnology (1986)
container_volume 82
creator Lee, Jung-Chul
An, Jin Young
Kim, Byung-Woo
description BACKGROUND: Non‐uniform distribution of pore size and depth of porous Si chip for a Fabry–Perot interferometer, in a previous study, led to relatively low sensitivity with poor reproducibility when its surface was immobilized with calyx crown derivative (Prolinker A). In this study, porous anodized aluminium oxide (AAO) was used as an alternative biochip substrate for detecting β‐galactosidase, and chip fabrication and surface functionalization methods were optimized. RESULTS: According to structural and spectral analysis of the AAO surface, an optimal operating voltage for anodization was determined as 40 V, which gave the best uniformity in pore size (about 30 nm) and fringe pattern. The ΔEOT (difference in effective optical thickness) showed a linear relationship (R2 = 0.9932) with β‐galactosidase concentration in the range 0.05–5 units enzyme mL−1, corresponding to 0.07–7.0 µg protein mL−1. CONCLUSIONS: With uniformly porous AAO immobilized with Prolinker A, sensitivity was enhanced about 200 times compared with the lowest detection concentration of 10 units mL−1 with the porous Si chip used in the previous study. Copyright © 2007 Society of Chemical Industry
doi_str_mv 10.1002/jctb.1729
format article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_30968714</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>30968714</sourcerecordid><originalsourceid>FETCH-LOGICAL-c3999-dcbe91afa4fac870ea8872552527868c4a8625513611eedcfad2cf935d277d923</originalsourceid><addsrcrecordid>eNqFkMtu1DAYhS0EEkNhwRt4QyUWaX0Z35btQFuq3hZDWVp_HFu4TeJgJ6LD05PRjMoKdfVf9J1vcRD6SMkRJYQdP7ixPqKKmVdoQYlR1VJK8hotCJO6YkKJt-hdKQ-EEKmZXCB7MgxtdDDG1OMUMPSpiX98g6GdutjHqcPpKTYeQ8GA65jczzjgMtVlzDB6HFKe_2dQ501153MacexHn8O8dn5e3qM3AdriP-znAfp-9nW9uqiubs-_rU6uKseNMVXjam8oBFgGcFoRD1orJgQTTGmp3RK0nE_KJaXeNy5Aw1wwXDRMqcYwfoAOd94hp1-TL6PtYnG-baH3aSqWEyO1ossXQUaY4ISrGfy8A11OpWQf7JBjB3ljKbHbru22a7vtemY_7aVQHLQhQ-9i-Rcw1Aih6cwd77jfsfWb_wvt5Wp9ujdXu0Qso396TkB-tFJxJeyPm3N7fX-9FvdfTu0F_wsw-Z39</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>20253037</pqid></control><display><type>article</type><title>Application of anodized aluminium oxide as a biochip substrate for a Fabry-Perot interferometer</title><source>Wiley-Blackwell Read &amp; Publish Collection</source><creator>Lee, Jung-Chul ; An, Jin Young ; Kim, Byung-Woo</creator><creatorcontrib>Lee, Jung-Chul ; An, Jin Young ; Kim, Byung-Woo</creatorcontrib><description>BACKGROUND: Non‐uniform distribution of pore size and depth of porous Si chip for a Fabry–Perot interferometer, in a previous study, led to relatively low sensitivity with poor reproducibility when its surface was immobilized with calyx crown derivative (Prolinker A). In this study, porous anodized aluminium oxide (AAO) was used as an alternative biochip substrate for detecting β‐galactosidase, and chip fabrication and surface functionalization methods were optimized. RESULTS: According to structural and spectral analysis of the AAO surface, an optimal operating voltage for anodization was determined as 40 V, which gave the best uniformity in pore size (about 30 nm) and fringe pattern. The ΔEOT (difference in effective optical thickness) showed a linear relationship (R2 = 0.9932) with β‐galactosidase concentration in the range 0.05–5 units enzyme mL−1, corresponding to 0.07–7.0 µg protein mL−1. CONCLUSIONS: With uniformly porous AAO immobilized with Prolinker A, sensitivity was enhanced about 200 times compared with the lowest detection concentration of 10 units mL−1 with the porous Si chip used in the previous study. Copyright © 2007 Society of Chemical Industry</description><identifier>ISSN: 0268-2575</identifier><identifier>EISSN: 1097-4660</identifier><identifier>DOI: 10.1002/jctb.1729</identifier><identifier>CODEN: JCTBDC</identifier><language>eng</language><publisher>Chichester, UK: John Wiley &amp; Sons, Ltd</publisher><subject>anodized aluminium oxide (AAO) ; anodized aluminium oxide (AAO), β‐galactosidase ; Applied sciences ; biosensor ; Chemical engineering ; Exact sciences and technology ; interferometry ; surface functionalization ; β-galactosidase</subject><ispartof>Journal of chemical technology and biotechnology (1986), 2007-11, Vol.82 (11), p.1045-1052</ispartof><rights>Copyright © 2007 Society of Chemical Industry</rights><rights>2008 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3999-dcbe91afa4fac870ea8872552527868c4a8625513611eedcfad2cf935d277d923</citedby><cites>FETCH-LOGICAL-c3999-dcbe91afa4fac870ea8872552527868c4a8625513611eedcfad2cf935d277d923</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=19195581$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Lee, Jung-Chul</creatorcontrib><creatorcontrib>An, Jin Young</creatorcontrib><creatorcontrib>Kim, Byung-Woo</creatorcontrib><title>Application of anodized aluminium oxide as a biochip substrate for a Fabry-Perot interferometer</title><title>Journal of chemical technology and biotechnology (1986)</title><addtitle>J. Chem. Technol. Biotechnol</addtitle><description>BACKGROUND: Non‐uniform distribution of pore size and depth of porous Si chip for a Fabry–Perot interferometer, in a previous study, led to relatively low sensitivity with poor reproducibility when its surface was immobilized with calyx crown derivative (Prolinker A). In this study, porous anodized aluminium oxide (AAO) was used as an alternative biochip substrate for detecting β‐galactosidase, and chip fabrication and surface functionalization methods were optimized. RESULTS: According to structural and spectral analysis of the AAO surface, an optimal operating voltage for anodization was determined as 40 V, which gave the best uniformity in pore size (about 30 nm) and fringe pattern. The ΔEOT (difference in effective optical thickness) showed a linear relationship (R2 = 0.9932) with β‐galactosidase concentration in the range 0.05–5 units enzyme mL−1, corresponding to 0.07–7.0 µg protein mL−1. CONCLUSIONS: With uniformly porous AAO immobilized with Prolinker A, sensitivity was enhanced about 200 times compared with the lowest detection concentration of 10 units mL−1 with the porous Si chip used in the previous study. Copyright © 2007 Society of Chemical Industry</description><subject>anodized aluminium oxide (AAO)</subject><subject>anodized aluminium oxide (AAO), β‐galactosidase</subject><subject>Applied sciences</subject><subject>biosensor</subject><subject>Chemical engineering</subject><subject>Exact sciences and technology</subject><subject>interferometry</subject><subject>surface functionalization</subject><subject>β-galactosidase</subject><issn>0268-2575</issn><issn>1097-4660</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><recordid>eNqFkMtu1DAYhS0EEkNhwRt4QyUWaX0Z35btQFuq3hZDWVp_HFu4TeJgJ6LD05PRjMoKdfVf9J1vcRD6SMkRJYQdP7ixPqKKmVdoQYlR1VJK8hotCJO6YkKJt-hdKQ-EEKmZXCB7MgxtdDDG1OMUMPSpiX98g6GdutjHqcPpKTYeQ8GA65jczzjgMtVlzDB6HFKe_2dQ501153MacexHn8O8dn5e3qM3AdriP-znAfp-9nW9uqiubs-_rU6uKseNMVXjam8oBFgGcFoRD1orJgQTTGmp3RK0nE_KJaXeNy5Aw1wwXDRMqcYwfoAOd94hp1-TL6PtYnG-baH3aSqWEyO1ossXQUaY4ISrGfy8A11OpWQf7JBjB3ljKbHbru22a7vtemY_7aVQHLQhQ-9i-Rcw1Aih6cwd77jfsfWb_wvt5Wp9ujdXu0Qso396TkB-tFJxJeyPm3N7fX-9FvdfTu0F_wsw-Z39</recordid><startdate>200711</startdate><enddate>200711</enddate><creator>Lee, Jung-Chul</creator><creator>An, Jin Young</creator><creator>Kim, Byung-Woo</creator><general>John Wiley &amp; Sons, Ltd</general><general>Wiley</general><scope>BSCLL</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7QF</scope><scope>7U5</scope><scope>F28</scope><scope>JG9</scope><scope>L7M</scope></search><sort><creationdate>200711</creationdate><title>Application of anodized aluminium oxide as a biochip substrate for a Fabry-Perot interferometer</title><author>Lee, Jung-Chul ; An, Jin Young ; Kim, Byung-Woo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3999-dcbe91afa4fac870ea8872552527868c4a8625513611eedcfad2cf935d277d923</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>anodized aluminium oxide (AAO)</topic><topic>anodized aluminium oxide (AAO), β‐galactosidase</topic><topic>Applied sciences</topic><topic>biosensor</topic><topic>Chemical engineering</topic><topic>Exact sciences and technology</topic><topic>interferometry</topic><topic>surface functionalization</topic><topic>β-galactosidase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lee, Jung-Chul</creatorcontrib><creatorcontrib>An, Jin Young</creatorcontrib><creatorcontrib>Kim, Byung-Woo</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Aluminium Industry Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>ANTE: Abstracts in New Technology &amp; Engineering</collection><collection>Materials Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Journal of chemical technology and biotechnology (1986)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lee, Jung-Chul</au><au>An, Jin Young</au><au>Kim, Byung-Woo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Application of anodized aluminium oxide as a biochip substrate for a Fabry-Perot interferometer</atitle><jtitle>Journal of chemical technology and biotechnology (1986)</jtitle><addtitle>J. Chem. Technol. Biotechnol</addtitle><date>2007-11</date><risdate>2007</risdate><volume>82</volume><issue>11</issue><spage>1045</spage><epage>1052</epage><pages>1045-1052</pages><issn>0268-2575</issn><eissn>1097-4660</eissn><coden>JCTBDC</coden><abstract>BACKGROUND: Non‐uniform distribution of pore size and depth of porous Si chip for a Fabry–Perot interferometer, in a previous study, led to relatively low sensitivity with poor reproducibility when its surface was immobilized with calyx crown derivative (Prolinker A). In this study, porous anodized aluminium oxide (AAO) was used as an alternative biochip substrate for detecting β‐galactosidase, and chip fabrication and surface functionalization methods were optimized. RESULTS: According to structural and spectral analysis of the AAO surface, an optimal operating voltage for anodization was determined as 40 V, which gave the best uniformity in pore size (about 30 nm) and fringe pattern. The ΔEOT (difference in effective optical thickness) showed a linear relationship (R2 = 0.9932) with β‐galactosidase concentration in the range 0.05–5 units enzyme mL−1, corresponding to 0.07–7.0 µg protein mL−1. CONCLUSIONS: With uniformly porous AAO immobilized with Prolinker A, sensitivity was enhanced about 200 times compared with the lowest detection concentration of 10 units mL−1 with the porous Si chip used in the previous study. Copyright © 2007 Society of Chemical Industry</abstract><cop>Chichester, UK</cop><pub>John Wiley &amp; Sons, Ltd</pub><doi>10.1002/jctb.1729</doi><tpages>8</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0268-2575
ispartof Journal of chemical technology and biotechnology (1986), 2007-11, Vol.82 (11), p.1045-1052
issn 0268-2575
1097-4660
language eng
recordid cdi_proquest_miscellaneous_30968714
source Wiley-Blackwell Read & Publish Collection
subjects anodized aluminium oxide (AAO)
anodized aluminium oxide (AAO), β‐galactosidase
Applied sciences
biosensor
Chemical engineering
Exact sciences and technology
interferometry
surface functionalization
β-galactosidase
title Application of anodized aluminium oxide as a biochip substrate for a Fabry-Perot interferometer
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-02T09%3A39%3A33IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Application%20of%20anodized%20aluminium%20oxide%20as%20a%20biochip%20substrate%20for%20a%20Fabry-Perot%20interferometer&rft.jtitle=Journal%20of%20chemical%20technology%20and%20biotechnology%20(1986)&rft.au=Lee,%20Jung-Chul&rft.date=2007-11&rft.volume=82&rft.issue=11&rft.spage=1045&rft.epage=1052&rft.pages=1045-1052&rft.issn=0268-2575&rft.eissn=1097-4660&rft.coden=JCTBDC&rft_id=info:doi/10.1002/jctb.1729&rft_dat=%3Cproquest_cross%3E30968714%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c3999-dcbe91afa4fac870ea8872552527868c4a8625513611eedcfad2cf935d277d923%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=20253037&rft_id=info:pmid/&rfr_iscdi=true