An enzyme immobilized microreactor for continuous-flow biocatalysis of ginsenoside Rb1

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dc.authoridKazan, Aslihan/0000-0002-8947-8494
dc.authorscopusid56196033300
dc.authorscopusid57190660119
dc.authorscopusid57212005164
dc.authorscopusid57212001154
dc.authorscopusid24069513800
dc.authorscopusid22837401200
dc.authorwosidYesil-Celiktas, Ozlem/AAI-5713-2020
dc.authorwosidKazan, Aslihan/GRS-2694-2022
dc.contributor.authorKazan, Aslihan
dc.contributor.authorHu, Xihua
dc.contributor.authorStahl, Alina
dc.contributor.authorFrerichs, Heike
dc.contributor.authorSmirnova, Irina
dc.contributor.authorYesil-Celiktas, Ozlem
dc.date.accessioned2023-01-12T19:49:50Z
dc.date.available2023-01-12T19:49:50Z
dc.date.issued2021
dc.departmentN/A/Departmenten_US
dc.description.abstractBACKGROUND Ginsenoside Rb1 is one of the major bioactive components of Panax ginseng C.A. Meyer (Araliaceae), a medicinal plant that has been used for therapeutic purposes for thousands of years in Asian countries. The pharmaceutical activity of ginsenoside Rb1 highly depends on molecular structure and its deglycosylated metabolites are known to be more potent bioactive compounds. However, these deglycosylated ginsenosides do not exist naturally so they are usually obtained by poorly selective methods, like chemical hydrolysis. RESULTS In this study, the development and characterization of an alginate-based immobilized enzyme microreactor for the catalytic conversion of ginsenoside Rb1 to more bioactive metabolites have been reported. Enzyme kinetic parameters were calculated and characterization tests (such as determination of surface area of alginate matrix, long-term use, and effect of residence time on conversion yield) were conducted. The system was operated under continuous-flow conditions and compared with acidic and batch enzymatic hydrolysis experiments, as conventional approaches. The enzymatic microreactor showed an enhanced activity by producing 13-fold higher amount of ginsenoside F2 than batch enzymatic hydrolysis. CONCLUSION Obtained results indicated that the newly developed enzymatic microreactor could successfully convert ginsenoside Rb1 to more active metabolites and have a potential for the biocatalysis of multiple ginsenosides, as well as pharmaceutically active compounds. (c) 2021 Society of Chemical Industry (SCI).en_US
dc.description.sponsorshipScientific and Technological Research Council of Turkey (TUBITAK) [:113M050, 2211-C]; Federal Ministry of Education and Research (BMBF) [01DL14002]en_US
dc.description.sponsorshipThis work was supported by the Scientific and Technological Research Council of Turkey (TUBITAK, grant numbers:113M050 and 2211-C) and the Federal Ministry of Education and Research (BMBF, grant number 01DL14002).en_US
dc.identifier.doi10.1002/jctb.6887
dc.identifier.endpage3357en_US
dc.identifier.issn0268-2575
dc.identifier.issn1097-4660
dc.identifier.issn0268-2575en_US
dc.identifier.issn1097-4660en_US
dc.identifier.issue12en_US
dc.identifier.scopus2-s2.0-85113908808en_US
dc.identifier.scopusqualityQ1en_US
dc.identifier.startpage3349en_US
dc.identifier.urihttps://doi.org/10.1002/jctb.6887
dc.identifier.urihttps://hdl.handle.net/11454/75926
dc.identifier.volume96en_US
dc.identifier.wosWOS:000691380900001en_US
dc.identifier.wosqualityQ2en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherWileyen_US
dc.relation.ispartofJournal Of Chemical Technology And Biotechnologyen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectbeta-glucosidaseen_US
dc.subjectalginate hydrogelen_US
dc.subjectginsenosideen_US
dc.subjectimmobilizationen_US
dc.subjectmicroreactoren_US
dc.subjectBeta-Glucosidaseen_US
dc.subjectPanax-Ginsengen_US
dc.subjectSaponinsen_US
dc.subjectHydrolysisen_US
dc.subjectBiotransformationen_US
dc.subjectOptimizationen_US
dc.subjectPerformanceen_US
dc.subjectExtractionen_US
dc.subjectProductsen_US
dc.subjectHydrogelen_US
dc.titleAn enzyme immobilized microreactor for continuous-flow biocatalysis of ginsenoside Rb1en_US
dc.typeArticleen_US

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