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001 on1231501438;

003 OCoLC;

005 20210831091551.0;

006 m o d ;

007 cr unu||||||||;

008 210114s2020 ncua obm 000 0 eng d;

035 a| (Sirsi) o1231501438;

035 a| (OCoLC)1231501438;

049 a| EREE;

090 a| TP248.E5;

100 1 a| Patel, Mitul P.,e| author.?| UNAUTHORIZED;

245 10 a| Screening and characterization of biocatalysts for synthesis of Wieland Miescher Ketone :b| a versatile synthetic intermediate /c| by Mitul P. Patel.;

264 1 a| [Greenville, N.C.] :b| [East Carolina University],c| 2020.;

300 a| 64 pages :b| illustrations;

336 a| textb| txt2| rdacontent;

337 a| computerb| c2| rdamedia;

338 a| online resourceb| cr2| rdacarrier;

347 a| text fileb| PDFc| 1.591 MB2| rda;

538 a| System requirements: Adobe Reader.;

538 a| Mode of access: World Wide Web.;

502 b| M.S.c| East Carolina Universityd| 2020.;

500 a| Presented to the faculty of the Department of Chemistry;

500 a| Advisor: Robert Hughes;

500 a| Title from PDF t.p. (viewed August 30, 2021).;

520 3 a| Biocatalysts derived from biological molecules such as proteins, RNA, and DNA have long been exploited for applications in synthetic chemistry. Lipases, a versatile class of biocatalysts, are known to exhibit significant promiscuity for non-native substrates in non-aqueous and mixed organic/aqueous solvents. While lipases are known to possess catalytic activity for a wide range of organic transformations, predicting which lipases will catalyze specific carbon-carbon bond forming reactions remains a significant challenge. In this study, the catalytic potential of a library of commercially available lipases was investigated by screening them for catalysis of the Robinson Annulation, a synthetically important carbon-carbon bond forming reaction. Specifically, the lipase library was screened for synthesis of the Wieland-Miescher Ketone, an important intermediate in the synthesis of biologically active compounds such as steroids and terpenoids, from methyl vinyl ketone and 2-methyl-1,3-cyclohexanedione. An optimized procedure is presented for Wieland-Miescher Ketone synthesis using a crude preparation of porcine pancreatic lipase (PPL), reporting on both yield and enantiomeric excess. Finally, commercially available lipases are often sold as crude preparations, containing many different proteins, and are often used by many researchers without further purification, potentially obscuring the identity of the catalytic species. Therefore, a methodology to isolate and characterize the active component(s) of these lipase formulations is described in this study.;

504 a| Includes bibliographical references.;

650 0 a| Enzymesx| Synthesis.=| ^A2443;

650 0 a| Biosynthesis.=| ^A56702;

653 a| Lipases;

653 a| Wieland Miescher Ketone;

700 1 a| Hughes, Robert,e| degree supervisor.=| ^A61249;

710 2 a| East Carolina University.b| Department of Chemistry.?| UNAUTHORIZED;

856 40 z| Access via ScholarShipu| http://hdl.handle.net/10342/8809;

949 o| wjh;

994 a| C0b| ERE;

596 a| 1 4;

998 a| 5547890;

999 a| CLICK ON WEB ADDRESSw| ASISc| 1i| 5547890-1001l| JNETm| JOYNERr| Ys| Yt| JNE3ETDu| 1/14/2021x| ETDz| JERESOURCE;

999 a| CLICK ON WEB ADDRESSw| ASISc| 1i| 5547890-2001l| HSLELECm| HSLr| Ys| Yt| HEETDu| 1/14/2021x| ETDz| HERESOURCE;

Screening and characterization of biocatalysts for synthesis of Wieland Miescher Ketone : a versatile synthetic intermediate / by Mitul P. Patel.

Author/creator	Patel, Mitul P. author.
Other author	Hughes, Robert, degree supervisor.
Other author	East Carolina University. Department of Chemistry.
Format	Theses and dissertations
Publication	[Greenville, N.C.] : [East Carolina University], 2020.
Description	64 pages : illustrations
Supplemental Content	Access via ScholarShip
Subjects	Enzymes--Synthesis. Biosynthesis.

Summary	Biocatalysts derived from biological molecules such as proteins, RNA, and DNA have long been exploited for applications in synthetic chemistry. Lipases, a versatile class of biocatalysts, are known to exhibit significant promiscuity for non-native substrates in non-aqueous and mixed organic/aqueous solvents. While lipases are known to possess catalytic activity for a wide range of organic transformations, predicting which lipases will catalyze specific carbon-carbon bond forming reactions remains a significant challenge. In this study, the catalytic potential of a library of commercially available lipases was investigated by screening them for catalysis of the Robinson Annulation, a synthetically important carbon-carbon bond forming reaction. Specifically, the lipase library was screened for synthesis of the Wieland-Miescher Ketone, an important intermediate in the synthesis of biologically active compounds such as steroids and terpenoids, from methyl vinyl ketone and 2-methyl-1,3-cyclohexanedione. An optimized procedure is presented for Wieland-Miescher Ketone synthesis using a crude preparation of porcine pancreatic lipase (PPL), reporting on both yield and enantiomeric excess. Finally, commercially available lipases are often sold as crude preparations, containing many different proteins, and are often used by many researchers without further purification, potentially obscuring the identity of the catalytic species. Therefore, a methodology to isolate and characterize the active component(s) of these lipase formulations is described in this study.
General note	Presented to the faculty of the Department of Chemistry
General note	Advisor: Robert Hughes
General note	Title from PDF t.p. (viewed August 30, 2021).
Dissertation note	M.S. East Carolina University 2020.
Bibliography note	Includes bibliographical references.
Technical details	System requirements: Adobe Reader.
Technical details	Mode of access: World Wide Web.

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Screening and characterization of biocatalysts for synthesis of Wieland Miescher Ketone : a versatile synthetic intermediate / by Mitul P. Patel.

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