Immobilization of β-galactosidase on surface modified cobalt/multiwalled carbon nanotube nanocomposite improves enzyme stability and resistance to inhibitor
[Display omitted] •High yield procedure for immobilization of β-galactosidase has been described.•Both physical adsorption and covalent method of binding have been employed.•Polyaniline/cobalt/multiwalled carbon nanotube nanocomposite have been used.•Covalently attached enzyme exhibited greater stab...
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| Veröffentlicht in: | International journal of biological macromolecules 2017-12, Vol.105 (Pt 1), p.693-701 |
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| container_title | International journal of biological macromolecules |
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| creator | Khan, Maryam Husain, Qayyum Bushra, Rani |
| description | [Display omitted]
•High yield procedure for immobilization of β-galactosidase has been described.•Both physical adsorption and covalent method of binding have been employed.•Polyaniline/cobalt/multiwalled carbon nanotube nanocomposite have been used.•Covalently attached enzyme exhibited greater stability and reusability.
The present study aimed to work out a high yield procedure for immobilization of Aspergillus oryzae β-galactosidase on polyaniline cobalt multiwalled carbon nanotubes nanocomposite (PANI/Co/MWCNTNC) by physical adsorption and covalent attachment via glutaraldehyde. The binding was confirmed by scanning and transmission electron microscopy along with Fourier transform-infrared spectroscopy. The immobilization yields obtained for adsorbed and cross-linked enzymes were 93% and 97%, respectively. The covalently immobilized enzyme was remarkably more stable at extremes of pH and temperature compared to native and adsorbed enzymes. The Ki values were found to increase ten-folds for covalently immobilized β-galactosidase indicating that this immobilized enzyme was markedly more resistant to galactose inhibition. The covalently attached enzyme retained 92% activity after its 10th successive reuse compared to the adsorbed β-galactosidase which exhibited 74% of its initial activity. Furthermore, no significant change was noticed in the band intensity of pBR322 plasmid when exposed to free and bound nanocomposite. The covalently bound enzyme exhibited superiority in terms of stability and reusability when compared to the adsorbed and native β-galactosidase. The results, presented here demonstrate an efficient method of immobilization of β-galactosidase on PANI/Co/MWCNTNC in order to construct a convenient and novel biosensor for the detection of lactose concentration. |
| doi_str_mv | 10.1016/j.ijbiomac.2017.07.088 |
| format | Article |
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•High yield procedure for immobilization of β-galactosidase has been described.•Both physical adsorption and covalent method of binding have been employed.•Polyaniline/cobalt/multiwalled carbon nanotube nanocomposite have been used.•Covalently attached enzyme exhibited greater stability and reusability.
The present study aimed to work out a high yield procedure for immobilization of Aspergillus oryzae β-galactosidase on polyaniline cobalt multiwalled carbon nanotubes nanocomposite (PANI/Co/MWCNTNC) by physical adsorption and covalent attachment via glutaraldehyde. The binding was confirmed by scanning and transmission electron microscopy along with Fourier transform-infrared spectroscopy. The immobilization yields obtained for adsorbed and cross-linked enzymes were 93% and 97%, respectively. The covalently immobilized enzyme was remarkably more stable at extremes of pH and temperature compared to native and adsorbed enzymes. The Ki values were found to increase ten-folds for covalently immobilized β-galactosidase indicating that this immobilized enzyme was markedly more resistant to galactose inhibition. The covalently attached enzyme retained 92% activity after its 10th successive reuse compared to the adsorbed β-galactosidase which exhibited 74% of its initial activity. Furthermore, no significant change was noticed in the band intensity of pBR322 plasmid when exposed to free and bound nanocomposite. The covalently bound enzyme exhibited superiority in terms of stability and reusability when compared to the adsorbed and native β-galactosidase. The results, presented here demonstrate an efficient method of immobilization of β-galactosidase on PANI/Co/MWCNTNC in order to construct a convenient and novel biosensor for the detection of lactose concentration.</description><identifier>ISSN: 0141-8130</identifier><identifier>EISSN: 1879-0003</identifier><identifier>DOI: 10.1016/j.ijbiomac.2017.07.088</identifier><identifier>PMID: 28735002</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Aniline Compounds - chemistry ; Aspergillus oryzae - enzymology ; beta-Galactosidase - antagonists & inhibitors ; beta-Galactosidase - chemistry ; Carbon nanotubes ; Cobalt - chemistry ; Enzyme Stability ; Enzymes, Immobilized - antagonists & inhibitors ; Enzymes, Immobilized - chemistry ; Galactose - pharmacology ; Glycoside Hydrolase Inhibitors - pharmacology ; Hydrogen-Ion Concentration ; Kinetics ; Models, Molecular ; Molecular Conformation ; Nanocomposites ; Nanocomposites - chemistry ; Nanocomposites - toxicity ; Nanotubes, Carbon - chemistry ; Surface Properties ; Temperature ; β-Galactosidase</subject><ispartof>International journal of biological macromolecules, 2017-12, Vol.105 (Pt 1), p.693-701</ispartof><rights>2017 Elsevier B.V.</rights><rights>Copyright © 2017 Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c368t-b03ff877acb4ebf93be434139e5bde529e576d78a683b2572999d28465ecb8dd3</citedby><cites>FETCH-LOGICAL-c368t-b03ff877acb4ebf93be434139e5bde529e576d78a683b2572999d28465ecb8dd3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.ijbiomac.2017.07.088$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,781,785,3551,27929,27930,46000</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28735002$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Khan, Maryam</creatorcontrib><creatorcontrib>Husain, Qayyum</creatorcontrib><creatorcontrib>Bushra, Rani</creatorcontrib><title>Immobilization of β-galactosidase on surface modified cobalt/multiwalled carbon nanotube nanocomposite improves enzyme stability and resistance to inhibitor</title><title>International journal of biological macromolecules</title><addtitle>Int J Biol Macromol</addtitle><description>[Display omitted]
•High yield procedure for immobilization of β-galactosidase has been described.•Both physical adsorption and covalent method of binding have been employed.•Polyaniline/cobalt/multiwalled carbon nanotube nanocomposite have been used.•Covalently attached enzyme exhibited greater stability and reusability.
The present study aimed to work out a high yield procedure for immobilization of Aspergillus oryzae β-galactosidase on polyaniline cobalt multiwalled carbon nanotubes nanocomposite (PANI/Co/MWCNTNC) by physical adsorption and covalent attachment via glutaraldehyde. The binding was confirmed by scanning and transmission electron microscopy along with Fourier transform-infrared spectroscopy. The immobilization yields obtained for adsorbed and cross-linked enzymes were 93% and 97%, respectively. The covalently immobilized enzyme was remarkably more stable at extremes of pH and temperature compared to native and adsorbed enzymes. The Ki values were found to increase ten-folds for covalently immobilized β-galactosidase indicating that this immobilized enzyme was markedly more resistant to galactose inhibition. The covalently attached enzyme retained 92% activity after its 10th successive reuse compared to the adsorbed β-galactosidase which exhibited 74% of its initial activity. Furthermore, no significant change was noticed in the band intensity of pBR322 plasmid when exposed to free and bound nanocomposite. The covalently bound enzyme exhibited superiority in terms of stability and reusability when compared to the adsorbed and native β-galactosidase. The results, presented here demonstrate an efficient method of immobilization of β-galactosidase on PANI/Co/MWCNTNC in order to construct a convenient and novel biosensor for the detection of lactose concentration.</description><subject>Aniline Compounds - chemistry</subject><subject>Aspergillus oryzae - enzymology</subject><subject>beta-Galactosidase - antagonists & inhibitors</subject><subject>beta-Galactosidase - chemistry</subject><subject>Carbon nanotubes</subject><subject>Cobalt - chemistry</subject><subject>Enzyme Stability</subject><subject>Enzymes, Immobilized - antagonists & inhibitors</subject><subject>Enzymes, Immobilized - chemistry</subject><subject>Galactose - pharmacology</subject><subject>Glycoside Hydrolase Inhibitors - pharmacology</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Models, Molecular</subject><subject>Molecular Conformation</subject><subject>Nanocomposites</subject><subject>Nanocomposites - chemistry</subject><subject>Nanocomposites - toxicity</subject><subject>Nanotubes, Carbon - chemistry</subject><subject>Surface Properties</subject><subject>Temperature</subject><subject>β-Galactosidase</subject><issn>0141-8130</issn><issn>1879-0003</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1uFDEQhS0EIkPgCpGXbHpit_vHvQNFkESKxAbWln-qoUZ2e7DdQZO7cAkOwpnwMAlbpJLKevqqnu1HyAVnW874cLnb4s5gDNpuW8bHLasl5TOy4XKcGsaYeE42jHe8kVywM_Iq511Vh57Ll-SslaPoGWs35OdtCNGgxwddMC40zvT3r-ar9tqWmNHpDLTKeU2ztkBDdDgjOGqj0b5chtUX_KG9P0o6mYoueollNfD3YGPY1zUFKIZ9iveQKSwPhwA0F320LQeqF0cTZKzKUi1KpLh8Q4Mlptfkxax9hjeP_Zx8-fjh89VNc_fp-vbq_V1jxSBLY5iYZzmO2poOzDwJA53ouJigNw76tvZxcKPUgxSm7cd2mibXym7owRrpnDgnb0976x2_r5CLCpgteK8XiGtWfGoF51yMXUWHE2pTzDnBrPYJg04HxZk6RqN26ikadYxGsVpS1sGLR4_VBHD_xp6yqMC7EwD1pfcISWWLUL_EYQJblIv4P48_zXapVA</recordid><startdate>201712</startdate><enddate>201712</enddate><creator>Khan, Maryam</creator><creator>Husain, Qayyum</creator><creator>Bushra, Rani</creator><general>Elsevier B.V</general><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>7X8</scope></search><sort><creationdate>201712</creationdate><title>Immobilization of β-galactosidase on surface modified cobalt/multiwalled carbon nanotube nanocomposite improves enzyme stability and resistance to inhibitor</title><author>Khan, Maryam ; Husain, Qayyum ; Bushra, Rani</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c368t-b03ff877acb4ebf93be434139e5bde529e576d78a683b2572999d28465ecb8dd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Aniline Compounds - chemistry</topic><topic>Aspergillus oryzae - enzymology</topic><topic>beta-Galactosidase - antagonists & inhibitors</topic><topic>beta-Galactosidase - chemistry</topic><topic>Carbon nanotubes</topic><topic>Cobalt - chemistry</topic><topic>Enzyme Stability</topic><topic>Enzymes, Immobilized - antagonists & inhibitors</topic><topic>Enzymes, Immobilized - chemistry</topic><topic>Galactose - pharmacology</topic><topic>Glycoside Hydrolase Inhibitors - pharmacology</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Models, Molecular</topic><topic>Molecular Conformation</topic><topic>Nanocomposites</topic><topic>Nanocomposites - chemistry</topic><topic>Nanocomposites - toxicity</topic><topic>Nanotubes, Carbon - chemistry</topic><topic>Surface Properties</topic><topic>Temperature</topic><topic>β-Galactosidase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Khan, Maryam</creatorcontrib><creatorcontrib>Husain, Qayyum</creatorcontrib><creatorcontrib>Bushra, Rani</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>International journal of biological macromolecules</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Khan, Maryam</au><au>Husain, Qayyum</au><au>Bushra, Rani</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Immobilization of β-galactosidase on surface modified cobalt/multiwalled carbon nanotube nanocomposite improves enzyme stability and resistance to inhibitor</atitle><jtitle>International journal of biological macromolecules</jtitle><addtitle>Int J Biol Macromol</addtitle><date>2017-12</date><risdate>2017</risdate><volume>105</volume><issue>Pt 1</issue><spage>693</spage><epage>701</epage><pages>693-701</pages><issn>0141-8130</issn><eissn>1879-0003</eissn><abstract>[Display omitted]
•High yield procedure for immobilization of β-galactosidase has been described.•Both physical adsorption and covalent method of binding have been employed.•Polyaniline/cobalt/multiwalled carbon nanotube nanocomposite have been used.•Covalently attached enzyme exhibited greater stability and reusability.
The present study aimed to work out a high yield procedure for immobilization of Aspergillus oryzae β-galactosidase on polyaniline cobalt multiwalled carbon nanotubes nanocomposite (PANI/Co/MWCNTNC) by physical adsorption and covalent attachment via glutaraldehyde. The binding was confirmed by scanning and transmission electron microscopy along with Fourier transform-infrared spectroscopy. The immobilization yields obtained for adsorbed and cross-linked enzymes were 93% and 97%, respectively. The covalently immobilized enzyme was remarkably more stable at extremes of pH and temperature compared to native and adsorbed enzymes. The Ki values were found to increase ten-folds for covalently immobilized β-galactosidase indicating that this immobilized enzyme was markedly more resistant to galactose inhibition. The covalently attached enzyme retained 92% activity after its 10th successive reuse compared to the adsorbed β-galactosidase which exhibited 74% of its initial activity. Furthermore, no significant change was noticed in the band intensity of pBR322 plasmid when exposed to free and bound nanocomposite. The covalently bound enzyme exhibited superiority in terms of stability and reusability when compared to the adsorbed and native β-galactosidase. The results, presented here demonstrate an efficient method of immobilization of β-galactosidase on PANI/Co/MWCNTNC in order to construct a convenient and novel biosensor for the detection of lactose concentration.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>28735002</pmid><doi>10.1016/j.ijbiomac.2017.07.088</doi><tpages>9</tpages></addata></record> |
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| subjects | Aniline Compounds - chemistry Aspergillus oryzae - enzymology beta-Galactosidase - antagonists & inhibitors beta-Galactosidase - chemistry Carbon nanotubes Cobalt - chemistry Enzyme Stability Enzymes, Immobilized - antagonists & inhibitors Enzymes, Immobilized - chemistry Galactose - pharmacology Glycoside Hydrolase Inhibitors - pharmacology Hydrogen-Ion Concentration Kinetics Models, Molecular Molecular Conformation Nanocomposites Nanocomposites - chemistry Nanocomposites - toxicity Nanotubes, Carbon - chemistry Surface Properties Temperature β-Galactosidase |
| title | Immobilization of β-galactosidase on surface modified cobalt/multiwalled carbon nanotube nanocomposite improves enzyme stability and resistance to inhibitor |
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