prikaz prve stranice dokumenta Employment of alkane 1-monooxygenase in efficient whole-cell production of tulipalin A
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master's thesis
Employment of alkane 1-monooxygenase in efficient whole-cell production of tulipalin A
Zagreb: University of Zagreb, Faculty of Food Technology and Biotechnology, 2023. urn:nbn:hr:159:471414
Grgić, Marina
University of Zagreb
Faculty of Food Technology and Biotechnology
Department of Biochemical Engineering
Laboratory for Biochemical Engineering, Industrial Microbiology and Malting and Brewing Technology

Institutional repository: Repository of the Faculty of Food Technology and Biotechnology

Cite this document

Grgić, M. (2023). Employment of alkane 1-monooxygenase in efficient whole-cell production of tulipalin A (Master's thesis). Zagreb: University of Zagreb, Faculty of Food Technology and Biotechnology. Retrieved from https://urn.nsk.hr/urn:nbn:hr:159:471414

Grgić, Marina. "Employment of alkane 1-monooxygenase in efficient whole-cell production of tulipalin A." Master's thesis, University of Zagreb, Faculty of Food Technology and Biotechnology, 2023. https://urn.nsk.hr/urn:nbn:hr:159:471414

Grgić, Marina. "Employment of alkane 1-monooxygenase in efficient whole-cell production of tulipalin A." Master's thesis, University of Zagreb, Faculty of Food Technology and Biotechnology, 2023. https://urn.nsk.hr/urn:nbn:hr:159:471414

Grgić, M. (2023). 'Employment of alkane 1-monooxygenase in efficient whole-cell production of tulipalin A', Master's thesis, University of Zagreb, Faculty of Food Technology and Biotechnology, accessed 25 July 2024, https://urn.nsk.hr/urn:nbn:hr:159:471414

Grgić M. Employment of alkane 1-monooxygenase in efficient whole-cell production of tulipalin A [Master's thesis]. Zagreb: University of Zagreb, Faculty of Food Technology and Biotechnology; 2023 [cited 2024 July 25] Available at: https://urn.nsk.hr/urn:nbn:hr:159:471414

M. Grgić, "Employment of alkane 1-monooxygenase in efficient whole-cell production of tulipalin A", Master's thesis, University of Zagreb, Faculty of Food Technology and Biotechnology, Zagreb, 2023. Available at: https://urn.nsk.hr/urn:nbn:hr:159:471414

Metadata
TitleEmployment of alkane 1-monooxygenase in efficient whole-cell production of tulipalin A
Title (croatian)Primjena alkan-1-monooksigenaze u učinkovitoj cjelostaničnoj proizvodnji tulipalina A
AuthorMarina Grgić
MentorAnita Slavica (mentor)
Committee memberRenata Teparic (predsjednik povjerenstva)
Committee memberBlaženka Kos (član povjerenstva)
GranterUniversity of Zagreb
Faculty of Food Technology and Biotechnology
(Department of Biochemical Engineering)
(Laboratory for Biochemical Engineering, Industrial Microbiology and Malting and Brewing Technology)
Zagreb
Defense date and country2023-07-18, Croatia
Scientific / art field,
discipline and subdiscipline		BIOTECHNICAL SCIENCES
Biotechnology
Abstract
Alkane 1-monooxygenases (Alk) were investigated in order to optimize the conversion of isoprenyl acetate (MBAc) to 3-(hydroxymethyl)but-3-en-1-yl acetate (HMBAc), as a part of the artificial synthetic pathway towards tulipalin A. Hydroxylation of MBAc to HMBAc and n-octane to 1-octanol and 1-octanoic acid, by employed Alk enzymes expressed in E. coli BL21(DE3) cells was more efficient at 25 °C than at 30 or 20 °C. Co-expression of a transporter of the hydrophobic substrate MBAc - AlkL with Alk from Marinobacter hydrocarbonoclasticus SP17 (MhAlkMO) has improved the uptake and conversion of MBAc by 1.4-fold. The highest specific activity toward the substrate was estimated for the mutant MhAlkMO-I238V (3.61 U gcdw⁻¹ ), which is a 2.8-fold improvement in comparison to the originally tested Alk from Pseudomonas putida GPo1 (AlkB).
Abstract (croatian)
Istražena je primjena alkan 1-monooksigenaza (Alk) u cilju optimizacije konverzije izoprenil acetata (MBAc) do 3-(hidroksimetil)but-3-en-1-il acetata (HMBAc), koja je dio kreiranog puta sinteze tulipalina A. Hidroksilacija MBAc do HMBAc kao i n-oktana do 1-oktanola i 1-oktanske kiseline odabranim Alk enzimima, koji su eksprimirani u stanicama E. coli BL21(DE3), bila je učinkovitija pri 25 °C nego pri 30 ili 20 °C. Ko-ekspresija transportera hidrofobnog susptrata MBAc - AlkL sa Alk iz Marinobacter hydrocarbonoclasticus SP17 (MhAlkMO) poboljšala je transport i konverziju ovoga supstrata za 1.4 puta. Najveća specifična aktivnost prema MBAc procijenjena je za mutant MhAlkMO-I238V (3.61 U gcdw⁻¹), što je poboljšanje specifične aktivnosti od 2.8-puta u usporedbi s prvobitno testiranom Alk iz Pseudomonas putida GPo1 (AlkB).
Keywords
Keywords (croatian)
Languageenglish
URN:NBNurn:nbn:hr:159:471414
Study programmeTitle: Molecular Biotechnology
Study programme type: university
Study level: graduate
Academic / professional title: magistar/magistra inženjer/inženjerka molekularne biotehnologije (magistar/magistra inženjer/inženjerka molekularne biotehnologije)
Type of resourceText
File originBorn digital
Access conditionsOpen access
Terms of useLicence Attribution-NoDerivatives 4.0 International (CC BY-ND 4.0) icon
Created on2024-06-13 08:28:21