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Enzyme‐catalyzed transesterification of lipids in methyl acetate using a methanol tolerant lipase from Proteus mirabilis (583.5)
Author(s) -
Carey Demetrius,
Witherow D. Scott
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.583.5
Subject(s) - transesterification , lipase , proteus mirabilis , chemistry , methanol , enzyme , catalysis , biodiesel production , organic chemistry , recombinant dna , escherichia coli , biochemistry , biodiesel , gene
Recombinant lipase catalyzed biodiesel production has the potential to be more economically efficient than traditional acid and/or base catalyzed methods. Enzyme catalysis may require smaller loads, lower temperatures, less time and can be repeated if immobilized enzymes are utilized. However, many lipases expressed in E.coli are found in inclusion bodies, making recombinant production difficult. Further, often they are denatured in the methanol, the most common acyl acceptor. Lipase from Proteus mirabilis is naturally soluble in E.coli and has previously been mutated for methanol tolerance. These “dieselzymes” have not been previously characterized or optimized in reactions using alternate acyl acceptors. Mutated “dieselzymes” have been expressed in E.coli using the pET28 bacterial expression vector, purified using immobilized metal affinity chromatography and characterized for transesterification activity in reactions using methyl acetate, p‐nitrophenyl palmitate, and synthetic triacylglycerides at varying pHs and temperatures