Production of biodiesel by Burkholderia cepacia lipase as a function of process parameters.

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Abstrakt

Tytuł:: Production of biodiesel by Burkholderia cepacia lipase as a function of process parameters.
Autorzy:: Ostojčić M; Faculty of Food Technology Osijek, Josip Juraj Strossmayer University of Osijek, Osijek, Croatia.
Budžaki S; Faculty of Food Technology Osijek, Josip Juraj Strossmayer University of Osijek, Osijek, Croatia.
Flanjak I; Faculty of Food Technology Osijek, Josip Juraj Strossmayer University of Osijek, Osijek, Croatia.
Bilić Rajs B; Faculty of Food Technology Osijek, Josip Juraj Strossmayer University of Osijek, Osijek, Croatia.
Barišić I; Faculty of Food Technology Osijek, Josip Juraj Strossmayer University of Osijek, Osijek, Croatia.
Tran NN; School of Chemical Engineering and Advanced Materials, The University of Adelaide, Adelaide, Australia.
Hessel V; School of Chemical Engineering and Advanced Materials, The University of Adelaide, Adelaide, Australia.
Strelec I; Faculty of Food Technology Osijek, Josip Juraj Strossmayer University of Osijek, Osijek, Croatia.
Źródło:: Biotechnology progress [Biotechnol Prog] 2021 Mar; Vol. 37 (2), pp. e3109. Date of Electronic Publication: 2020 Dec 18.
Typ publikacji:: Journal Article
Język:: English
Imprint Name(s):: Publication: <2010-> : Hoboken, NJ : Wiley-Blackwell
Original Publication: [New York, N.Y. : American Institute of Chemical Engineers, c1985-
MeSH Terms:: Biofuels/*analysis
Burkholderia cepacia/*enzymology
Enzymes, Immobilized/*metabolism
Esters/*metabolism
Fatty Acids/*metabolism
Lipase/*metabolism
Esterification ; Hydrogen-Ion Concentration ; Methyltransferases/metabolism ; Temperature
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Contributed Indexing:: Keywords: Burkholderia cepacia lipase; biodiesel; pH optimum; substrate specificity; temperature optimum
Substance Nomenclature:: 0 (Biofuels)
0 (Enzymes, Immobilized)
0 (Esters)
0 (Fatty Acids)
EC 2.1.1.- (Methyltransferases)
EC 2.1.1.15 (fatty acid methyltransferase)
EC 3.1.1.3 (Lipase)
Entry Date(s):: Date Created: 20201214 Date Completed: 20220128 Latest Revision: 20220128
Update Code:: 20240104
DOI:: 10.1002/btpr.3109
PMID:: 33314760
: Czasopismo naukowe

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Despite the already established route of chemically catalyzed transesterification reaction in biodiesel production, due to some of its shortcomings, biocatalysts such as lipases present a vital alternative. Namely, it was noticed that one of the key shortcomings for the optimization of the enzyme catalyzed biodiesel synthesis process is the information on the lipase activity in the reaction mixture. In addition to making optimization difficult, it also makes it impossible to compare the results of the independent research. This article shows how lipase intended for use in biodiesel synthesis can be easily and accurately characterized and what is the enzyme concentration that enables achievement of the desired level of fatty acid methyl esters (FAME) in the final product mixture. Therefore, this study investigated the effect of two different activity loads of Burkholderia cepacia lipase on the biodiesel synthesis varying the pH and temperature optimal for lipase activity. The optimal lipase pH and temperature were determined by two different enzyme assays: spectrophotometric and titrimetric. The B. cepacia lipase pH optimum differentiated between assays, while the lipase optimally hydrolyzed substrates at 50°C. The analysis of FAME during 24 hr of biodiesel synthesis, at two different enzyme concentrations, pH 7, 8, and 10, and using two different buffers, revealed that the transesterification reaction at optimal pH, 1 hr reaction time and lipase activity load of 250 U per gram of reaction mixture was sufficient to produce more than 99% FAME.
(© 2020 American Institute of Chemical Engineers.)

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