Loading…
Electrospun Zein Fibers as Carriers to Stabilize (-)-Epigallocatechin Gallate
In this study, a method was developed for continuous electrospinning of ultrafine corn zein protein fibers with diameters ranging from 150 to 600 nm. Fiber-forming solutions with various zein concentrations (10% to 30%, w/w) and aqueous ethanol concentrations (60% to 90%, w/w) were electrospun at 15...
Saved in:
Published in: | Journal of food science 2009-04, Vol.74 (3), p.C233-C240 |
---|---|
Main Authors: | , , |
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-c5183-f71ed3055e5382e10f2b5c9e94f87229631dc035c6c857a22bc33c66851f7c7e3 |
---|---|
cites | cdi_FETCH-LOGICAL-c5183-f71ed3055e5382e10f2b5c9e94f87229631dc035c6c857a22bc33c66851f7c7e3 |
container_end_page | C240 |
container_issue | 3 |
container_start_page | C233 |
container_title | Journal of food science |
container_volume | 74 |
creator | Li, Y Lim, L.-T Kakuda, Y |
description | In this study, a method was developed for continuous electrospinning of ultrafine corn zein protein fibers with diameters ranging from 150 to 600 nm. Fiber-forming solutions with various zein concentrations (10% to 30%, w/w) and aqueous ethanol concentrations (60% to 90%, w/w) were electrospun at 15 and 20 kV. Scanning electron microscopy results showed that the morphology of zein fibers was affected by aqueous ethanol concentration, zein concentration, and the applied voltage. The optimal condition for forming bead-less fibers was found to be 20% protein, 70% alcohol, and 15 kV. The zein fibers resisted solubilization in water, although swelling and plasticization were apparent after the water treatment. The efficacy of zein fibers was tested for stabilization of a green tea polyphenol, (-)-epigallocatechin gallate (EGCG), by incorporating the EGCG in zein fiber-forming solutions. Freshly spun fibers were less effective at immobilizing the EGCG upon immersion in water (82% recovery) as compared to fibers that were aged at 0% relative humidity for at least 1 d (>98% recovery) before water immersion. Fourier transform infrared spectroscopy studies demonstrated that hydrogen bonding, hydrophobic interactions, and physical encapsulation are the major contributors to the stabilization of EGCG in zein fibers in water. |
doi_str_mv | 10.1111/j.1750-3841.2009.01093.x |
format | article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_67167156</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>34230840</sourcerecordid><originalsourceid>FETCH-LOGICAL-c5183-f71ed3055e5382e10f2b5c9e94f87229631dc035c6c857a22bc33c66851f7c7e3</originalsourceid><addsrcrecordid>eNqNkV-L1DAUxYMo7uzqV9AiuOhD671J06Qvgo4zo7L-Y1wEX0Imk66Z7bRj0uKsn97UDiP4oiGQG_K7h5tzCEkQMozr2SZDwSFlMseMApQZIJQs298ik-PDbTIBoDRFzMUJOQ1hA8OdFXfJCZasFALkhLyb1dZ0vg27vkm-Wtckc7eyPiQ6JFPtvRvqrk2WnV652v20yZP0aTrbuStd163RnTXfYtMi3mJ9j9ypdB3s_cN5Ri7ns8_T1-nFh8Wb6YuL1HCULK0E2jUDzi1nklqEiq64KW2ZV1JQWhYM1wYYN4WRXGhKV4YxUxSSYyWMsOyMnI-6O99-723o1NYFY-MMjW37oAqBcfPinyDLKQOZQwQf_QVu2t438RMKyzyneQEDJEfIRMOCt5XaebfV_kYhqCEYtVGD_2rwXw3BqN_BqH1sfXDQ71dbu_7TeEgiAo8PgA5G15XXjXHhyFHMIWdy4J6P3A9X25v_HkC9nb9aDmUUSEcBFzq7Pwpofx1tY4KrL-8X6iPMuVwsP6mXkX848pVulb7ycajLJQVkgAVSUSD7BXjovlo</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>194424600</pqid></control><display><type>article</type><title>Electrospun Zein Fibers as Carriers to Stabilize (-)-Epigallocatechin Gallate</title><source>Wiley:Jisc Collections:Wiley Read and Publish Open Access 2024-2025 (reading list)</source><creator>Li, Y ; Lim, L.-T ; Kakuda, Y</creator><creatorcontrib>Li, Y ; Lim, L.-T ; Kakuda, Y</creatorcontrib><description>In this study, a method was developed for continuous electrospinning of ultrafine corn zein protein fibers with diameters ranging from 150 to 600 nm. Fiber-forming solutions with various zein concentrations (10% to 30%, w/w) and aqueous ethanol concentrations (60% to 90%, w/w) were electrospun at 15 and 20 kV. Scanning electron microscopy results showed that the morphology of zein fibers was affected by aqueous ethanol concentration, zein concentration, and the applied voltage. The optimal condition for forming bead-less fibers was found to be 20% protein, 70% alcohol, and 15 kV. The zein fibers resisted solubilization in water, although swelling and plasticization were apparent after the water treatment. The efficacy of zein fibers was tested for stabilization of a green tea polyphenol, (-)-epigallocatechin gallate (EGCG), by incorporating the EGCG in zein fiber-forming solutions. Freshly spun fibers were less effective at immobilizing the EGCG upon immersion in water (82% recovery) as compared to fibers that were aged at 0% relative humidity for at least 1 d (>98% recovery) before water immersion. Fourier transform infrared spectroscopy studies demonstrated that hydrogen bonding, hydrophobic interactions, and physical encapsulation are the major contributors to the stabilization of EGCG in zein fibers in water.</description><identifier>ISSN: 0022-1147</identifier><identifier>EISSN: 1750-3841</identifier><identifier>DOI: 10.1111/j.1750-3841.2009.01093.x</identifier><identifier>PMID: 19397708</identifier><identifier>CODEN: JFDSAZ</identifier><language>eng</language><publisher>Malden, USA: Blackwell Publishing Inc</publisher><subject>(−)-epigallocatechin gallate ; Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts ; aqueous solutions ; Biological and medical sciences ; catechin ; Catechin - analogs & derivatives ; Catechin - chemistry ; chemical concentration ; Corn ; diameter ; Drug Stability ; electrical treatment ; Electricity ; electrospun ultrafine fibers ; encapsulation ; epigallocatechin ; Ethanol ; fiber aging ; Food industries ; Food science ; Fourier transform infrared spectroscopy ; Fourier transforms ; Fundamental and applied biological sciences. Psychology ; green tea ; Hydrogen Bonding ; Hydrogen bonds ; Hydrophobic and Hydrophilic Interactions ; hydrophobicity ; Microscopy, Electron, Scanning ; physicochemical properties ; phytochemicals ; plant products ; plasticization ; polyphenols ; protein products ; Proteins ; Scanning electron microscopy ; solubility ; solubilization ; Solutions ; Spectroscopy, Fourier Transform Infrared ; Spectrum analysis ; storage quality ; Studies ; swelling (materials) ; Tea - chemistry ; Water ; water treatment ; zein ; Zein - analysis ; Zein - chemistry ; Zein - ultrastructure ; zein protein</subject><ispartof>Journal of food science, 2009-04, Vol.74 (3), p.C233-C240</ispartof><rights>2009 Institute of Food Technologists</rights><rights>2009 INIST-CNRS</rights><rights>Copyright Institute of Food Technologists Apr 2009</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5183-f71ed3055e5382e10f2b5c9e94f87229631dc035c6c857a22bc33c66851f7c7e3</citedby><cites>FETCH-LOGICAL-c5183-f71ed3055e5382e10f2b5c9e94f87229631dc035c6c857a22bc33c66851f7c7e3</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&idt=21404388$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19397708$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Li, Y</creatorcontrib><creatorcontrib>Lim, L.-T</creatorcontrib><creatorcontrib>Kakuda, Y</creatorcontrib><title>Electrospun Zein Fibers as Carriers to Stabilize (-)-Epigallocatechin Gallate</title><title>Journal of food science</title><addtitle>J Food Sci</addtitle><description>In this study, a method was developed for continuous electrospinning of ultrafine corn zein protein fibers with diameters ranging from 150 to 600 nm. Fiber-forming solutions with various zein concentrations (10% to 30%, w/w) and aqueous ethanol concentrations (60% to 90%, w/w) were electrospun at 15 and 20 kV. Scanning electron microscopy results showed that the morphology of zein fibers was affected by aqueous ethanol concentration, zein concentration, and the applied voltage. The optimal condition for forming bead-less fibers was found to be 20% protein, 70% alcohol, and 15 kV. The zein fibers resisted solubilization in water, although swelling and plasticization were apparent after the water treatment. The efficacy of zein fibers was tested for stabilization of a green tea polyphenol, (-)-epigallocatechin gallate (EGCG), by incorporating the EGCG in zein fiber-forming solutions. Freshly spun fibers were less effective at immobilizing the EGCG upon immersion in water (82% recovery) as compared to fibers that were aged at 0% relative humidity for at least 1 d (>98% recovery) before water immersion. Fourier transform infrared spectroscopy studies demonstrated that hydrogen bonding, hydrophobic interactions, and physical encapsulation are the major contributors to the stabilization of EGCG in zein fibers in water.</description><subject>(−)-epigallocatechin gallate</subject><subject>Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts</subject><subject>aqueous solutions</subject><subject>Biological and medical sciences</subject><subject>catechin</subject><subject>Catechin - analogs & derivatives</subject><subject>Catechin - chemistry</subject><subject>chemical concentration</subject><subject>Corn</subject><subject>diameter</subject><subject>Drug Stability</subject><subject>electrical treatment</subject><subject>Electricity</subject><subject>electrospun ultrafine fibers</subject><subject>encapsulation</subject><subject>epigallocatechin</subject><subject>Ethanol</subject><subject>fiber aging</subject><subject>Food industries</subject><subject>Food science</subject><subject>Fourier transform infrared spectroscopy</subject><subject>Fourier transforms</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>green tea</subject><subject>Hydrogen Bonding</subject><subject>Hydrogen bonds</subject><subject>Hydrophobic and Hydrophilic Interactions</subject><subject>hydrophobicity</subject><subject>Microscopy, Electron, Scanning</subject><subject>physicochemical properties</subject><subject>phytochemicals</subject><subject>plant products</subject><subject>plasticization</subject><subject>polyphenols</subject><subject>protein products</subject><subject>Proteins</subject><subject>Scanning electron microscopy</subject><subject>solubility</subject><subject>solubilization</subject><subject>Solutions</subject><subject>Spectroscopy, Fourier Transform Infrared</subject><subject>Spectrum analysis</subject><subject>storage quality</subject><subject>Studies</subject><subject>swelling (materials)</subject><subject>Tea - chemistry</subject><subject>Water</subject><subject>water treatment</subject><subject>zein</subject><subject>Zein - analysis</subject><subject>Zein - chemistry</subject><subject>Zein - ultrastructure</subject><subject>zein protein</subject><issn>0022-1147</issn><issn>1750-3841</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><recordid>eNqNkV-L1DAUxYMo7uzqV9AiuOhD671J06Qvgo4zo7L-Y1wEX0Imk66Z7bRj0uKsn97UDiP4oiGQG_K7h5tzCEkQMozr2SZDwSFlMseMApQZIJQs298ik-PDbTIBoDRFzMUJOQ1hA8OdFXfJCZasFALkhLyb1dZ0vg27vkm-Wtckc7eyPiQ6JFPtvRvqrk2WnV652v20yZP0aTrbuStd163RnTXfYtMi3mJ9j9ypdB3s_cN5Ri7ns8_T1-nFh8Wb6YuL1HCULK0E2jUDzi1nklqEiq64KW2ZV1JQWhYM1wYYN4WRXGhKV4YxUxSSYyWMsOyMnI-6O99-723o1NYFY-MMjW37oAqBcfPinyDLKQOZQwQf_QVu2t438RMKyzyneQEDJEfIRMOCt5XaebfV_kYhqCEYtVGD_2rwXw3BqN_BqH1sfXDQ71dbu_7TeEgiAo8PgA5G15XXjXHhyFHMIWdy4J6P3A9X25v_HkC9nb9aDmUUSEcBFzq7Pwpofx1tY4KrL-8X6iPMuVwsP6mXkX848pVulb7ycajLJQVkgAVSUSD7BXjovlo</recordid><startdate>200904</startdate><enddate>200904</enddate><creator>Li, Y</creator><creator>Lim, L.-T</creator><creator>Kakuda, Y</creator><general>Blackwell Publishing Inc</general><general>Wiley</general><general>Wiley Subscription Services, Inc</general><scope>FBQ</scope><scope>BSCLL</scope><scope>IQODW</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>7QO</scope><scope>7QR</scope><scope>7ST</scope><scope>7T7</scope><scope>7U7</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>SOI</scope><scope>7X8</scope></search><sort><creationdate>200904</creationdate><title>Electrospun Zein Fibers as Carriers to Stabilize (-)-Epigallocatechin Gallate</title><author>Li, Y ; Lim, L.-T ; Kakuda, Y</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5183-f71ed3055e5382e10f2b5c9e94f87229631dc035c6c857a22bc33c66851f7c7e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>(−)-epigallocatechin gallate</topic><topic>Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts</topic><topic>aqueous solutions</topic><topic>Biological and medical sciences</topic><topic>catechin</topic><topic>Catechin - analogs & derivatives</topic><topic>Catechin - chemistry</topic><topic>chemical concentration</topic><topic>Corn</topic><topic>diameter</topic><topic>Drug Stability</topic><topic>electrical treatment</topic><topic>Electricity</topic><topic>electrospun ultrafine fibers</topic><topic>encapsulation</topic><topic>epigallocatechin</topic><topic>Ethanol</topic><topic>fiber aging</topic><topic>Food industries</topic><topic>Food science</topic><topic>Fourier transform infrared spectroscopy</topic><topic>Fourier transforms</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>green tea</topic><topic>Hydrogen Bonding</topic><topic>Hydrogen bonds</topic><topic>Hydrophobic and Hydrophilic Interactions</topic><topic>hydrophobicity</topic><topic>Microscopy, Electron, Scanning</topic><topic>physicochemical properties</topic><topic>phytochemicals</topic><topic>plant products</topic><topic>plasticization</topic><topic>polyphenols</topic><topic>protein products</topic><topic>Proteins</topic><topic>Scanning electron microscopy</topic><topic>solubility</topic><topic>solubilization</topic><topic>Solutions</topic><topic>Spectroscopy, Fourier Transform Infrared</topic><topic>Spectrum analysis</topic><topic>storage quality</topic><topic>Studies</topic><topic>swelling (materials)</topic><topic>Tea - chemistry</topic><topic>Water</topic><topic>water treatment</topic><topic>zein</topic><topic>Zein - analysis</topic><topic>Zein - chemistry</topic><topic>Zein - ultrastructure</topic><topic>zein protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Li, Y</creatorcontrib><creatorcontrib>Lim, L.-T</creatorcontrib><creatorcontrib>Kakuda, Y</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Environment Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Toxicology Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>Environment Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of food science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Li, Y</au><au>Lim, L.-T</au><au>Kakuda, Y</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Electrospun Zein Fibers as Carriers to Stabilize (-)-Epigallocatechin Gallate</atitle><jtitle>Journal of food science</jtitle><addtitle>J Food Sci</addtitle><date>2009-04</date><risdate>2009</risdate><volume>74</volume><issue>3</issue><spage>C233</spage><epage>C240</epage><pages>C233-C240</pages><issn>0022-1147</issn><eissn>1750-3841</eissn><coden>JFDSAZ</coden><abstract>In this study, a method was developed for continuous electrospinning of ultrafine corn zein protein fibers with diameters ranging from 150 to 600 nm. Fiber-forming solutions with various zein concentrations (10% to 30%, w/w) and aqueous ethanol concentrations (60% to 90%, w/w) were electrospun at 15 and 20 kV. Scanning electron microscopy results showed that the morphology of zein fibers was affected by aqueous ethanol concentration, zein concentration, and the applied voltage. The optimal condition for forming bead-less fibers was found to be 20% protein, 70% alcohol, and 15 kV. The zein fibers resisted solubilization in water, although swelling and plasticization were apparent after the water treatment. The efficacy of zein fibers was tested for stabilization of a green tea polyphenol, (-)-epigallocatechin gallate (EGCG), by incorporating the EGCG in zein fiber-forming solutions. Freshly spun fibers were less effective at immobilizing the EGCG upon immersion in water (82% recovery) as compared to fibers that were aged at 0% relative humidity for at least 1 d (>98% recovery) before water immersion. Fourier transform infrared spectroscopy studies demonstrated that hydrogen bonding, hydrophobic interactions, and physical encapsulation are the major contributors to the stabilization of EGCG in zein fibers in water.</abstract><cop>Malden, USA</cop><pub>Blackwell Publishing Inc</pub><pmid>19397708</pmid><doi>10.1111/j.1750-3841.2009.01093.x</doi><tpages>8</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0022-1147 |
ispartof | Journal of food science, 2009-04, Vol.74 (3), p.C233-C240 |
issn | 0022-1147 1750-3841 |
language | eng |
recordid | cdi_proquest_miscellaneous_67167156 |
source | Wiley:Jisc Collections:Wiley Read and Publish Open Access 2024-2025 (reading list) |
subjects | (−)-epigallocatechin gallate Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts aqueous solutions Biological and medical sciences catechin Catechin - analogs & derivatives Catechin - chemistry chemical concentration Corn diameter Drug Stability electrical treatment Electricity electrospun ultrafine fibers encapsulation epigallocatechin Ethanol fiber aging Food industries Food science Fourier transform infrared spectroscopy Fourier transforms Fundamental and applied biological sciences. Psychology green tea Hydrogen Bonding Hydrogen bonds Hydrophobic and Hydrophilic Interactions hydrophobicity Microscopy, Electron, Scanning physicochemical properties phytochemicals plant products plasticization polyphenols protein products Proteins Scanning electron microscopy solubility solubilization Solutions Spectroscopy, Fourier Transform Infrared Spectrum analysis storage quality Studies swelling (materials) Tea - chemistry Water water treatment zein Zein - analysis Zein - chemistry Zein - ultrastructure zein protein |
title | Electrospun Zein Fibers as Carriers to Stabilize (-)-Epigallocatechin Gallate |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-24T23%3A36%3A15IST&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=Electrospun%20Zein%20Fibers%20as%20Carriers%20to%20Stabilize%20(-)-Epigallocatechin%20Gallate&rft.jtitle=Journal%20of%20food%20science&rft.au=Li,%20Y&rft.date=2009-04&rft.volume=74&rft.issue=3&rft.spage=C233&rft.epage=C240&rft.pages=C233-C240&rft.issn=0022-1147&rft.eissn=1750-3841&rft.coden=JFDSAZ&rft_id=info:doi/10.1111/j.1750-3841.2009.01093.x&rft_dat=%3Cproquest_cross%3E34230840%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c5183-f71ed3055e5382e10f2b5c9e94f87229631dc035c6c857a22bc33c66851f7c7e3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=194424600&rft_id=info:pmid/19397708&rfr_iscdi=true |