Bioprocess Scale-up for Acetohydroxamic Acid Production by Hyperactive Acyltransferase of Immobilized Rhodococcus Pyridinivorans
In this study, Rhodococcus pyridinivorans cells containing hyperactive acyltransferase was immobilized on various macromolecules based-polymeric matrices and used to improve acetohydroxamic acid production. The calcium-alginate-based matrix retained the maximum residual activity up to 97.8% as compa...
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| Veröffentlicht in: | Catalysis letters 2022-04, Vol.152 (4), p.944-953 |
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| creator | Devi, Neena Patel, Sanjay K. S. Kumar, Pradeep Singh, Archana Thakur, Nandita Lata, Jeevan Pandey, Deepak Thakur, Vikram Chand, Duni |
| description | In this study,
Rhodococcus pyridinivorans
cells containing hyperactive acyltransferase was immobilized on various macromolecules based-polymeric matrices and used to improve acetohydroxamic acid production. The calcium-alginate-based matrix retained the maximum residual activity up to 97.8% as compared to free cells (576 U/mg of dry cell weight). After immobilization, cells exhibited a significant improvement in their tolerance towards pH, temperature, and metal ions as potent enzyme inhibitors. Immobilized cells showed 25.5-fold higher thermal stability at 60 °C to control (free cells). Compared to free cells, immobilized cells exhibited a high bioconversion of acetamide and hydroxylamine-HCl to acetohydroxamic acid up to 96% molar conversion. Repeated bench-scale production at 3-L culture, immobilized cells showed 9.5-fold higher residual conversion as compared to control (100%), after five cycles of reuses. The product characterization achieved high purity (97%) of acetohydroxamic acid. This finding showed high feasibility to achieve efficient conversion that can be scaled up to the industrial level for biotechnological application.
Graphical Abstract |
| doi_str_mv | 10.1007/s10562-021-03696-4 |
| format | Article |
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Rhodococcus pyridinivorans
cells containing hyperactive acyltransferase was immobilized on various macromolecules based-polymeric matrices and used to improve acetohydroxamic acid production. The calcium-alginate-based matrix retained the maximum residual activity up to 97.8% as compared to free cells (576 U/mg of dry cell weight). After immobilization, cells exhibited a significant improvement in their tolerance towards pH, temperature, and metal ions as potent enzyme inhibitors. Immobilized cells showed 25.5-fold higher thermal stability at 60 °C to control (free cells). Compared to free cells, immobilized cells exhibited a high bioconversion of acetamide and hydroxylamine-HCl to acetohydroxamic acid up to 96% molar conversion. Repeated bench-scale production at 3-L culture, immobilized cells showed 9.5-fold higher residual conversion as compared to control (100%), after five cycles of reuses. The product characterization achieved high purity (97%) of acetohydroxamic acid. This finding showed high feasibility to achieve efficient conversion that can be scaled up to the industrial level for biotechnological application.
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Rhodococcus pyridinivorans
cells containing hyperactive acyltransferase was immobilized on various macromolecules based-polymeric matrices and used to improve acetohydroxamic acid production. The calcium-alginate-based matrix retained the maximum residual activity up to 97.8% as compared to free cells (576 U/mg of dry cell weight). After immobilization, cells exhibited a significant improvement in their tolerance towards pH, temperature, and metal ions as potent enzyme inhibitors. Immobilized cells showed 25.5-fold higher thermal stability at 60 °C to control (free cells). Compared to free cells, immobilized cells exhibited a high bioconversion of acetamide and hydroxylamine-HCl to acetohydroxamic acid up to 96% molar conversion. Repeated bench-scale production at 3-L culture, immobilized cells showed 9.5-fold higher residual conversion as compared to control (100%), after five cycles of reuses. The product characterization achieved high purity (97%) of acetohydroxamic acid. This finding showed high feasibility to achieve efficient conversion that can be scaled up to the industrial level for biotechnological application.
Graphical Abstract</description><subject>Acids</subject><subject>Alginates</subject><subject>Amides</subject><subject>Bioconversion</subject><subject>Catalysis</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Comparative analysis</subject><subject>Control stability</subject><subject>Dry cells</subject><subject>Enzyme inhibitors</subject><subject>Enzymes</subject><subject>Hydroxides</subject><subject>Industrial Chemistry/Chemical Engineering</subject><subject>Macromolecules</subject><subject>Organic acids</subject><subject>Organometallic Chemistry</subject><subject>Physical Chemistry</subject><subject>Rhodococcus</subject><subject>Thermal stability</subject><issn>1011-372X</issn><issn>1572-879X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>AFKRA</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><recordid>eNp9kcFrFDEUxgdRsFb_AU8BTx5SX5KZyeS4FrULBUur0FvIJC_blJ3JmsyUjif_dLOuUBZEckjey-9L-N5XVW8ZnDEA-SEzaFpOgTMKolUtrZ9VJ6yRnHZS3T4vZ2CMCslvX1avcr4HACWZOql-fQxxl6LFnMmNNVuk8474mMjK4hTvFpfioxmCLXVw5CpFN9spxJH0C7lYdphMKR-wXC_bKZkx-9LKSKIn62GIfdiGn-jI9V100UZr50yulhRcGMND3POvqxfebDO--bufVt8_f_p2fkEvv35Zn68uqa05TLTv-s5L15keTNPwXvXKKeSGeek9mLa30CmBtpaq5QrBOiGkZag8qzthhDit3h3eLW5_zJgnfR_nNJYvNW-FYrxpBDxRmzIKHUYfiyk7hGz1qoxVcSZUXaizf1BlOSyjiiP6UPpHgvdHgsJM-DhtzJyzXt9cH7P8wNoUc07o9S6FwaRFM9D7sPUhbF3C1n_C1nuROIhygccNpid3_1H9BtazrdM</recordid><startdate>20220401</startdate><enddate>20220401</enddate><creator>Devi, Neena</creator><creator>Patel, Sanjay K. 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S.</creatorcontrib><creatorcontrib>Kumar, Pradeep</creatorcontrib><creatorcontrib>Singh, Archana</creatorcontrib><creatorcontrib>Thakur, Nandita</creatorcontrib><creatorcontrib>Lata, Jeevan</creatorcontrib><creatorcontrib>Pandey, Deepak</creatorcontrib><creatorcontrib>Thakur, Vikram</creatorcontrib><creatorcontrib>Chand, Duni</creatorcontrib><collection>CrossRef</collection><collection>Gale In Context: Science</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>SciTech Premium Collection</collection><collection>Materials Science Database</collection><collection>Materials Science Collection</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 China</collection><jtitle>Catalysis letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Devi, Neena</au><au>Patel, Sanjay K. S.</au><au>Kumar, Pradeep</au><au>Singh, Archana</au><au>Thakur, Nandita</au><au>Lata, Jeevan</au><au>Pandey, Deepak</au><au>Thakur, Vikram</au><au>Chand, Duni</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Bioprocess Scale-up for Acetohydroxamic Acid Production by Hyperactive Acyltransferase of Immobilized Rhodococcus Pyridinivorans</atitle><jtitle>Catalysis letters</jtitle><stitle>Catal Lett</stitle><date>2022-04-01</date><risdate>2022</risdate><volume>152</volume><issue>4</issue><spage>944</spage><epage>953</epage><pages>944-953</pages><issn>1011-372X</issn><eissn>1572-879X</eissn><abstract>In this study,
Rhodococcus pyridinivorans
cells containing hyperactive acyltransferase was immobilized on various macromolecules based-polymeric matrices and used to improve acetohydroxamic acid production. The calcium-alginate-based matrix retained the maximum residual activity up to 97.8% as compared to free cells (576 U/mg of dry cell weight). After immobilization, cells exhibited a significant improvement in their tolerance towards pH, temperature, and metal ions as potent enzyme inhibitors. Immobilized cells showed 25.5-fold higher thermal stability at 60 °C to control (free cells). Compared to free cells, immobilized cells exhibited a high bioconversion of acetamide and hydroxylamine-HCl to acetohydroxamic acid up to 96% molar conversion. Repeated bench-scale production at 3-L culture, immobilized cells showed 9.5-fold higher residual conversion as compared to control (100%), after five cycles of reuses. The product characterization achieved high purity (97%) of acetohydroxamic acid. This finding showed high feasibility to achieve efficient conversion that can be scaled up to the industrial level for biotechnological application.
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| ispartof | Catalysis letters, 2022-04, Vol.152 (4), p.944-953 |
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| source | Springer Nature - Complete Springer Journals |
| subjects | Acids Alginates Amides Bioconversion Catalysis Chemistry Chemistry and Materials Science Comparative analysis Control stability Dry cells Enzyme inhibitors Enzymes Hydroxides Industrial Chemistry/Chemical Engineering Macromolecules Organic acids Organometallic Chemistry Physical Chemistry Rhodococcus Thermal stability |
| title | Bioprocess Scale-up for Acetohydroxamic Acid Production by Hyperactive Acyltransferase of Immobilized Rhodococcus Pyridinivorans |
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