Affinity-binding immobilization of d-amino acid oxidase on mesoporous silica by a silica-specific peptide
Enzyme immobilization is widely used for large-scale industrial applications. However, the weak absorption through physical methods limits the recovery ability. Here, affinity-binding immobilization of enzymes was explored using a silica-specific affinity peptide (SAP) as a fusion tag to intensify t...
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| Veröffentlicht in: | Journal of industrial microbiology & biotechnology 2019-11, Vol.46 (11), p.1461-1467 |
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| creator | Wang, Miaomiao Qi, Wenjing Xu, Hongping Yu, Huimin Zhang, Shuliang Shen, Zhongyao |
| description | Enzyme immobilization is widely used for large-scale industrial applications. However, the weak absorption through physical methods limits the recovery ability. Here, affinity-binding immobilization of enzymes was explored using a silica-specific affinity peptide (SAP) as a fusion tag to intensify the binding force between the enzyme and mesoporous silica (MPS) carrier.
d-
amino acid oxidase (DAAO) of
Rhodosporidium toruloides
was used as a model enzyme. The optimal screened SAP (LPHWHPHSHLQP) was selected from a M13 phage display peptide library and fused to the C-terminal of DAAO to obtain fused DAAOs with one, two and three SAP tags, respectively. The activity of DAAO–SAP–MPS was superior comparing with DAAO–2SAP–MPS and DAAO–3SAP–MPS; meanwhile DAAO–SAP–MPS shows 36% higher activity than that of DAAO–MPS. Fusion with one SAP improved the thermal stability with a 10% activity increase for immobilized DAAO–SAP–MPS compared to that of DAAO–MPS at 50 °C for 3 h. Moreover, the activity recovery of immobilized DAAO–SAP–MPS was 25% higher in operation stability assessment after six-batch conversions of cephalosporin to glutaryl-7-amino cephalosporanic acid than that of DAAO–MPS. |
| doi_str_mv | 10.1007/s10295-019-02210-5 |
| format | Article |
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d-
amino acid oxidase (DAAO) of
Rhodosporidium toruloides
was used as a model enzyme. The optimal screened SAP (LPHWHPHSHLQP) was selected from a M13 phage display peptide library and fused to the C-terminal of DAAO to obtain fused DAAOs with one, two and three SAP tags, respectively. The activity of DAAO–SAP–MPS was superior comparing with DAAO–2SAP–MPS and DAAO–3SAP–MPS; meanwhile DAAO–SAP–MPS shows 36% higher activity than that of DAAO–MPS. Fusion with one SAP improved the thermal stability with a 10% activity increase for immobilized DAAO–SAP–MPS compared to that of DAAO–MPS at 50 °C for 3 h. Moreover, the activity recovery of immobilized DAAO–SAP–MPS was 25% higher in operation stability assessment after six-batch conversions of cephalosporin to glutaryl-7-amino cephalosporanic acid than that of DAAO–MPS.</description><identifier>ISSN: 1367-5435</identifier><identifier>EISSN: 1476-5535</identifier><identifier>DOI: 10.1007/s10295-019-02210-5</identifier><identifier>PMID: 31289973</identifier><language>eng</language><publisher>Cham: Springer International Publishing</publisher><subject>Affinity ; Amino acid oxidase ; Amino acids ; Amino Acids - metabolism ; Binding ; Biocatalysis - Short Communication ; Biochemistry ; Bioinformatics ; Biomedical and Life Sciences ; Biotechnology ; Cephalosporins ; Cephalosporins - metabolism ; D-Amino-acid oxidase ; D-Amino-Acid Oxidase - genetics ; D-Amino-Acid Oxidase - metabolism ; Enzymes ; Genetic Engineering ; Immobilization ; Industrial applications ; Inorganic Chemistry ; Life Sciences ; Microbiology ; Peptides ; Peptides - metabolism ; Phage display ; Phages ; Recovery ; Rhodosporidium toruloides ; Silica ; Silicon dioxide ; Silicon Dioxide - chemistry ; Stability analysis ; Thermal stability</subject><ispartof>Journal of industrial microbiology & biotechnology, 2019-11, Vol.46 (11), p.1461-1467</ispartof><rights>Society for Industrial Microbiology and Biotechnology 2019</rights><rights>Journal of Industrial Microbiology & Biotechnology is a copyright of Springer, (2019). All Rights Reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c456t-180bde8eb7a06d3ef0b4817dcb4d333944a9ab3fb456d13b37a6770a9b61d323</citedby><cites>FETCH-LOGICAL-c456t-180bde8eb7a06d3ef0b4817dcb4d333944a9ab3fb456d13b37a6770a9b61d323</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/s10295-019-02210-5$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10295-019-02210-5$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27923,27924,41487,42556,51318</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31289973$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Miaomiao</creatorcontrib><creatorcontrib>Qi, Wenjing</creatorcontrib><creatorcontrib>Xu, Hongping</creatorcontrib><creatorcontrib>Yu, Huimin</creatorcontrib><creatorcontrib>Zhang, Shuliang</creatorcontrib><creatorcontrib>Shen, Zhongyao</creatorcontrib><title>Affinity-binding immobilization of d-amino acid oxidase on mesoporous silica by a silica-specific peptide</title><title>Journal of industrial microbiology & biotechnology</title><addtitle>J Ind Microbiol Biotechnol</addtitle><addtitle>J Ind Microbiol Biotechnol</addtitle><description>Enzyme immobilization is widely used for large-scale industrial applications. However, the weak absorption through physical methods limits the recovery ability. Here, affinity-binding immobilization of enzymes was explored using a silica-specific affinity peptide (SAP) as a fusion tag to intensify the binding force between the enzyme and mesoporous silica (MPS) carrier.
d-
amino acid oxidase (DAAO) of
Rhodosporidium toruloides
was used as a model enzyme. The optimal screened SAP (LPHWHPHSHLQP) was selected from a M13 phage display peptide library and fused to the C-terminal of DAAO to obtain fused DAAOs with one, two and three SAP tags, respectively. The activity of DAAO–SAP–MPS was superior comparing with DAAO–2SAP–MPS and DAAO–3SAP–MPS; meanwhile DAAO–SAP–MPS shows 36% higher activity than that of DAAO–MPS. Fusion with one SAP improved the thermal stability with a 10% activity increase for immobilized DAAO–SAP–MPS compared to that of DAAO–MPS at 50 °C for 3 h. Moreover, the activity recovery of immobilized DAAO–SAP–MPS was 25% higher in operation stability assessment after six-batch conversions of cephalosporin to glutaryl-7-amino cephalosporanic acid than that of DAAO–MPS.</description><subject>Affinity</subject><subject>Amino acid oxidase</subject><subject>Amino acids</subject><subject>Amino Acids - metabolism</subject><subject>Binding</subject><subject>Biocatalysis - Short Communication</subject><subject>Biochemistry</subject><subject>Bioinformatics</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnology</subject><subject>Cephalosporins</subject><subject>Cephalosporins - metabolism</subject><subject>D-Amino-acid oxidase</subject><subject>D-Amino-Acid Oxidase - genetics</subject><subject>D-Amino-Acid Oxidase - metabolism</subject><subject>Enzymes</subject><subject>Genetic Engineering</subject><subject>Immobilization</subject><subject>Industrial applications</subject><subject>Inorganic Chemistry</subject><subject>Life Sciences</subject><subject>Microbiology</subject><subject>Peptides</subject><subject>Peptides - metabolism</subject><subject>Phage display</subject><subject>Phages</subject><subject>Recovery</subject><subject>Rhodosporidium toruloides</subject><subject>Silica</subject><subject>Silicon dioxide</subject><subject>Silicon Dioxide - chemistry</subject><subject>Stability analysis</subject><subject>Thermal stability</subject><issn>1367-5435</issn><issn>1476-5535</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp9kctKBDEQRYMovn_AhQTcuInm2eksRXyB4Gb2Iemkh5LpTtvpAcevN-OMCi5cVUGde6uoi9AZo1eMUn2dGeVGEcoMoZwzStQOOmRSV0QpoXZLLypNlBTqAB3l_EopVVrzfXQgGK-N0eIQwU3bQg_TinjoA_RzDF2XPCzgw02QepxaHIjroE_YNRBweofgcsRl1MWchjSmZca5CBqH_Qq7bU_yEBtoocFDHCYI8QTttW6R4-m2HqPZ_d3s9pE8vzw83d48k0aqaiKspj7EOnrtaBVEbKmXNdOh8TIIIYyUzjgvWl_owIQX2lVaU2d8xYLg4hhdbmyHMb0tY55sB7mJi4XrY7nUcq6UrKSp1-jFH_Q1Lce-HLemJDO0EqpQfEM1Y8p5jK0dRujcuLKM2nUOdpODLTnYrxzsWnS-tV76LoYfyffjCyA2QC6jfh7H393_2H4CpX2TlA</recordid><startdate>20191101</startdate><enddate>20191101</enddate><creator>Wang, Miaomiao</creator><creator>Qi, Wenjing</creator><creator>Xu, Hongping</creator><creator>Yu, Huimin</creator><creator>Zhang, Shuliang</creator><creator>Shen, Zhongyao</creator><general>Springer International Publishing</general><general>Oxford University Press</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>3V.</scope><scope>7QL</scope><scope>7QR</scope><scope>7T7</scope><scope>7WY</scope><scope>7WZ</scope><scope>7X7</scope><scope>7XB</scope><scope>87Z</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8FL</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BEZIV</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FRNLG</scope><scope>FYUFA</scope><scope>F~G</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>HCIFZ</scope><scope>K60</scope><scope>K6~</scope><scope>K9.</scope><scope>L.-</scope><scope>LK8</scope><scope>M0C</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQBIZ</scope><scope>PQBZA</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>20191101</creationdate><title>Affinity-binding immobilization of d-amino acid oxidase on mesoporous silica by a silica-specific peptide</title><author>Wang, Miaomiao ; Qi, Wenjing ; Xu, Hongping ; Yu, Huimin ; Zhang, Shuliang ; Shen, Zhongyao</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c456t-180bde8eb7a06d3ef0b4817dcb4d333944a9ab3fb456d13b37a6770a9b61d323</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Affinity</topic><topic>Amino acid oxidase</topic><topic>Amino acids</topic><topic>Amino Acids - metabolism</topic><topic>Binding</topic><topic>Biocatalysis - Short Communication</topic><topic>Biochemistry</topic><topic>Bioinformatics</topic><topic>Biomedical and Life Sciences</topic><topic>Biotechnology</topic><topic>Cephalosporins</topic><topic>Cephalosporins - metabolism</topic><topic>D-Amino-acid oxidase</topic><topic>D-Amino-Acid Oxidase - genetics</topic><topic>D-Amino-Acid Oxidase - metabolism</topic><topic>Enzymes</topic><topic>Genetic Engineering</topic><topic>Immobilization</topic><topic>Industrial applications</topic><topic>Inorganic Chemistry</topic><topic>Life Sciences</topic><topic>Microbiology</topic><topic>Peptides</topic><topic>Peptides - metabolism</topic><topic>Phage display</topic><topic>Phages</topic><topic>Recovery</topic><topic>Rhodosporidium toruloides</topic><topic>Silica</topic><topic>Silicon dioxide</topic><topic>Silicon Dioxide - chemistry</topic><topic>Stability analysis</topic><topic>Thermal stability</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, Miaomiao</creatorcontrib><creatorcontrib>Qi, Wenjing</creatorcontrib><creatorcontrib>Xu, Hongping</creatorcontrib><creatorcontrib>Yu, Huimin</creatorcontrib><creatorcontrib>Zhang, Shuliang</creatorcontrib><creatorcontrib>Shen, Zhongyao</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Chemoreception Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>ABI/INFORM Collection</collection><collection>ABI/INFORM Global (PDF only)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>ABI/INFORM Global (Alumni Edition)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ABI/INFORM Collection (Alumni Edition)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Business Premium Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Business Premium Collection (Alumni)</collection><collection>Health Research Premium Collection</collection><collection>ABI/INFORM Global (Corporate)</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Business Collection (Alumni Edition)</collection><collection>ProQuest Business Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ABI/INFORM Professional Advanced</collection><collection>ProQuest Biological Science Collection</collection><collection>ABI/INFORM Global</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Business</collection><collection>ProQuest One Business (Alumni)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of industrial microbiology & biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, Miaomiao</au><au>Qi, Wenjing</au><au>Xu, Hongping</au><au>Yu, Huimin</au><au>Zhang, Shuliang</au><au>Shen, Zhongyao</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Affinity-binding immobilization of d-amino acid oxidase on mesoporous silica by a silica-specific peptide</atitle><jtitle>Journal of industrial microbiology & biotechnology</jtitle><stitle>J Ind Microbiol Biotechnol</stitle><addtitle>J Ind Microbiol Biotechnol</addtitle><date>2019-11-01</date><risdate>2019</risdate><volume>46</volume><issue>11</issue><spage>1461</spage><epage>1467</epage><pages>1461-1467</pages><issn>1367-5435</issn><eissn>1476-5535</eissn><abstract>Enzyme immobilization is widely used for large-scale industrial applications. However, the weak absorption through physical methods limits the recovery ability. Here, affinity-binding immobilization of enzymes was explored using a silica-specific affinity peptide (SAP) as a fusion tag to intensify the binding force between the enzyme and mesoporous silica (MPS) carrier.
d-
amino acid oxidase (DAAO) of
Rhodosporidium toruloides
was used as a model enzyme. The optimal screened SAP (LPHWHPHSHLQP) was selected from a M13 phage display peptide library and fused to the C-terminal of DAAO to obtain fused DAAOs with one, two and three SAP tags, respectively. The activity of DAAO–SAP–MPS was superior comparing with DAAO–2SAP–MPS and DAAO–3SAP–MPS; meanwhile DAAO–SAP–MPS shows 36% higher activity than that of DAAO–MPS. Fusion with one SAP improved the thermal stability with a 10% activity increase for immobilized DAAO–SAP–MPS compared to that of DAAO–MPS at 50 °C for 3 h. Moreover, the activity recovery of immobilized DAAO–SAP–MPS was 25% higher in operation stability assessment after six-batch conversions of cephalosporin to glutaryl-7-amino cephalosporanic acid than that of DAAO–MPS.</abstract><cop>Cham</cop><pub>Springer International Publishing</pub><pmid>31289973</pmid><doi>10.1007/s10295-019-02210-5</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Journal of industrial microbiology & biotechnology, 2019-11, Vol.46 (11), p.1461-1467 |
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| subjects | Affinity Amino acid oxidase Amino acids Amino Acids - metabolism Binding Biocatalysis - Short Communication Biochemistry Bioinformatics Biomedical and Life Sciences Biotechnology Cephalosporins Cephalosporins - metabolism D-Amino-acid oxidase D-Amino-Acid Oxidase - genetics D-Amino-Acid Oxidase - metabolism Enzymes Genetic Engineering Immobilization Industrial applications Inorganic Chemistry Life Sciences Microbiology Peptides Peptides - metabolism Phage display Phages Recovery Rhodosporidium toruloides Silica Silicon dioxide Silicon Dioxide - chemistry Stability analysis Thermal stability |
| title | Affinity-binding immobilization of d-amino acid oxidase on mesoporous silica by a silica-specific peptide |
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