Magnetically separable biocatalysts based on glucose oxidase for d-glucose oxidation
Biocatalytic systems based on glucose oxidase immobilized on the surface of magnetically separable oxides SiO 2 and Al 2 O 3 were studied. Silicon and aluminum oxides acquired magnetic properties due to the introduction of magnetic nanoparticles Fe 3 O 4 into their pores. The support surface was mod...
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| Veröffentlicht in: | Russian chemical bulletin 2022-03, Vol.71 (3), p.524-530 |
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| container_title | Russian chemical bulletin |
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| creator | Grebennikova, O. V. Sulman, A. M. Sidorov, A. I. Sulman, M. G. Molchanov, V. P. Tikhonov, B. B. Matveeva, V. G. |
| description | Biocatalytic systems based on glucose oxidase immobilized on the surface of magnetically separable oxides SiO
2
and Al
2
O
3
were studied. Silicon and aluminum oxides acquired magnetic properties due to the introduction of magnetic nanoparticles Fe
3
O
4
into their pores. The support surface was modified with reactive amino groups using (3-aminopropyl)triethoxysilane and was activated using glutaraldehyde to achieve covalent bonding of the enzyme to the magnetically separable supports. Glucose oxidase was immobilized on the modified and activated magnetically separable supports. These biocatalytic systems were studied using low-temperature nitrogen adsorption, transmission electron microscopy, and X-ray photoelectron spectroscopy. All the biocatalytic systems were tested in the reaction of oxidation of
d
-glucose to
d
-gluconic acid. The highest relative activity (95%) was demonstrated by the biocatalyst based on glucose oxidase immobilized on the surface of magnetically separable silica. |
| doi_str_mv | 10.1007/s11172-022-3443-0 |
| format | Article |
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2
and Al
2
O
3
were studied. Silicon and aluminum oxides acquired magnetic properties due to the introduction of magnetic nanoparticles Fe
3
O
4
into their pores. The support surface was modified with reactive amino groups using (3-aminopropyl)triethoxysilane and was activated using glutaraldehyde to achieve covalent bonding of the enzyme to the magnetically separable supports. Glucose oxidase was immobilized on the modified and activated magnetically separable supports. These biocatalytic systems were studied using low-temperature nitrogen adsorption, transmission electron microscopy, and X-ray photoelectron spectroscopy. All the biocatalytic systems were tested in the reaction of oxidation of
d
-glucose to
d
-gluconic acid. The highest relative activity (95%) was demonstrated by the biocatalyst based on glucose oxidase immobilized on the surface of magnetically separable silica.</description><identifier>ISSN: 1066-5285</identifier><identifier>EISSN: 1573-9171</identifier><identifier>DOI: 10.1007/s11172-022-3443-0</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Aluminum oxide ; Aminopropyltriethoxysilane ; Chemistry ; Chemistry and Materials Science ; Chemistry/Food Science ; Full Articles ; Gluconic acid ; Glucose ; Glucose oxidase ; Inorganic Chemistry ; Iron oxides ; Low temperature ; Magnetic properties ; Nanoparticles ; Organic Chemistry ; Oxidation ; Photoelectrons ; Silicon dioxide</subject><ispartof>Russian chemical bulletin, 2022-03, Vol.71 (3), p.524-530</ispartof><rights>Springer Science+Business Media LLC 2022</rights><rights>Springer Science+Business Media LLC 2022.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c198t-4383b6c3528ca8b4aee49dedb82621f354a4c854114a99aaeb55eeaa6d665f4b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s11172-022-3443-0$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s11172-022-3443-0$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,777,781,27905,27906,41469,42538,51300</link.rule.ids></links><search><creatorcontrib>Grebennikova, O. V.</creatorcontrib><creatorcontrib>Sulman, A. M.</creatorcontrib><creatorcontrib>Sidorov, A. I.</creatorcontrib><creatorcontrib>Sulman, M. G.</creatorcontrib><creatorcontrib>Molchanov, V. P.</creatorcontrib><creatorcontrib>Tikhonov, B. B.</creatorcontrib><creatorcontrib>Matveeva, V. G.</creatorcontrib><title>Magnetically separable biocatalysts based on glucose oxidase for d-glucose oxidation</title><title>Russian chemical bulletin</title><addtitle>Russ Chem Bull</addtitle><description>Biocatalytic systems based on glucose oxidase immobilized on the surface of magnetically separable oxides SiO
2
and Al
2
O
3
were studied. Silicon and aluminum oxides acquired magnetic properties due to the introduction of magnetic nanoparticles Fe
3
O
4
into their pores. The support surface was modified with reactive amino groups using (3-aminopropyl)triethoxysilane and was activated using glutaraldehyde to achieve covalent bonding of the enzyme to the magnetically separable supports. Glucose oxidase was immobilized on the modified and activated magnetically separable supports. These biocatalytic systems were studied using low-temperature nitrogen adsorption, transmission electron microscopy, and X-ray photoelectron spectroscopy. All the biocatalytic systems were tested in the reaction of oxidation of
d
-glucose to
d
-gluconic acid. The highest relative activity (95%) was demonstrated by the biocatalyst based on glucose oxidase immobilized on the surface of magnetically separable silica.</description><subject>Aluminum oxide</subject><subject>Aminopropyltriethoxysilane</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Chemistry/Food Science</subject><subject>Full Articles</subject><subject>Gluconic acid</subject><subject>Glucose</subject><subject>Glucose oxidase</subject><subject>Inorganic Chemistry</subject><subject>Iron oxides</subject><subject>Low temperature</subject><subject>Magnetic properties</subject><subject>Nanoparticles</subject><subject>Organic Chemistry</subject><subject>Oxidation</subject><subject>Photoelectrons</subject><subject>Silicon dioxide</subject><issn>1066-5285</issn><issn>1573-9171</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><recordid>eNp1kEtLxDAUhYMoOI7-AHcB19G8my5l8AUjbsZ1uEnToUNtxqQF59-boYK4cHUvh3POvXwIXTN6yyit7jJjrOKEck6ElILQE7RgqhKkZhU7LTvVmihu1Dm6yHlHKeXGmAXavMJ2CGPnoe8POIc9JHB9wK6LHkboD3nM2EEODY4D3vaTjzng-NU1RcNtTLghf9Sxi8MlOmuhz-HqZy7R--PDZvVM1m9PL6v7NfGsNiORwginvShveTBOQgiybkLjDNectUJJkN4oyZiEugYITqkQAHSjtWqlE0t0M_fuU_ycQh7tLk5pKCct10qx0kx5cbHZ5VPMOYXW7lP3AelgGbVHeHaGZws8e4RnacnwOZOLd9iG9Nv8f-gbAbdy1w</recordid><startdate>20220301</startdate><enddate>20220301</enddate><creator>Grebennikova, O. V.</creator><creator>Sulman, A. M.</creator><creator>Sidorov, A. I.</creator><creator>Sulman, M. G.</creator><creator>Molchanov, V. P.</creator><creator>Tikhonov, B. B.</creator><creator>Matveeva, V. G.</creator><general>Springer US</general><general>Springer Nature B.V</general><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>20220301</creationdate><title>Magnetically separable biocatalysts based on glucose oxidase for d-glucose oxidation</title><author>Grebennikova, O. V. ; Sulman, A. M. ; Sidorov, A. I. ; Sulman, M. G. ; Molchanov, V. P. ; Tikhonov, B. B. ; Matveeva, V. G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c198t-4383b6c3528ca8b4aee49dedb82621f354a4c854114a99aaeb55eeaa6d665f4b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Aluminum oxide</topic><topic>Aminopropyltriethoxysilane</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Chemistry/Food Science</topic><topic>Full Articles</topic><topic>Gluconic acid</topic><topic>Glucose</topic><topic>Glucose oxidase</topic><topic>Inorganic Chemistry</topic><topic>Iron oxides</topic><topic>Low temperature</topic><topic>Magnetic properties</topic><topic>Nanoparticles</topic><topic>Organic Chemistry</topic><topic>Oxidation</topic><topic>Photoelectrons</topic><topic>Silicon dioxide</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Grebennikova, O. V.</creatorcontrib><creatorcontrib>Sulman, A. M.</creatorcontrib><creatorcontrib>Sidorov, A. I.</creatorcontrib><creatorcontrib>Sulman, M. G.</creatorcontrib><creatorcontrib>Molchanov, V. P.</creatorcontrib><creatorcontrib>Tikhonov, B. B.</creatorcontrib><creatorcontrib>Matveeva, V. G.</creatorcontrib><collection>CrossRef</collection><jtitle>Russian chemical bulletin</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Grebennikova, O. V.</au><au>Sulman, A. M.</au><au>Sidorov, A. I.</au><au>Sulman, M. G.</au><au>Molchanov, V. P.</au><au>Tikhonov, B. B.</au><au>Matveeva, V. G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Magnetically separable biocatalysts based on glucose oxidase for d-glucose oxidation</atitle><jtitle>Russian chemical bulletin</jtitle><stitle>Russ Chem Bull</stitle><date>2022-03-01</date><risdate>2022</risdate><volume>71</volume><issue>3</issue><spage>524</spage><epage>530</epage><pages>524-530</pages><issn>1066-5285</issn><eissn>1573-9171</eissn><abstract>Biocatalytic systems based on glucose oxidase immobilized on the surface of magnetically separable oxides SiO
2
and Al
2
O
3
were studied. Silicon and aluminum oxides acquired magnetic properties due to the introduction of magnetic nanoparticles Fe
3
O
4
into their pores. The support surface was modified with reactive amino groups using (3-aminopropyl)triethoxysilane and was activated using glutaraldehyde to achieve covalent bonding of the enzyme to the magnetically separable supports. Glucose oxidase was immobilized on the modified and activated magnetically separable supports. These biocatalytic systems were studied using low-temperature nitrogen adsorption, transmission electron microscopy, and X-ray photoelectron spectroscopy. All the biocatalytic systems were tested in the reaction of oxidation of
d
-glucose to
d
-gluconic acid. The highest relative activity (95%) was demonstrated by the biocatalyst based on glucose oxidase immobilized on the surface of magnetically separable silica.</abstract><cop>New York</cop><pub>Springer US</pub><doi>10.1007/s11172-022-3443-0</doi><tpages>7</tpages></addata></record> |
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| ispartof | Russian chemical bulletin, 2022-03, Vol.71 (3), p.524-530 |
| issn | 1066-5285 1573-9171 |
| language | eng |
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| source | Springer Nature - Complete Springer Journals |
| subjects | Aluminum oxide Aminopropyltriethoxysilane Chemistry Chemistry and Materials Science Chemistry/Food Science Full Articles Gluconic acid Glucose Glucose oxidase Inorganic Chemistry Iron oxides Low temperature Magnetic properties Nanoparticles Organic Chemistry Oxidation Photoelectrons Silicon dioxide |
| title | Magnetically separable biocatalysts based on glucose oxidase for d-glucose oxidation |
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