ArticleJournal, genetic engineering & biotechnology2023
Cloning and characterization of an acidic lipase from a lipolytic bacterium in tempeh.
Article in Journal, genetic engineering & biotechnology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 6 citations in OpenAlex.
- Activity Enhancement of a Truncated Lipase-Phospholipase from the Marine Thraustochytrid Aurantiochytrium Sp. MG91.Molecular biotechnology · 2026Article
- A Sequence-Based Approach Reveals a Novel Family IV Lipolytic Enzyme in Cereibacter sphaeroides 2.4.1.Molecular biotechnology · 2026Article
- Co-expression, purification, and characterization of an acidophilic and n-hexane-tolerant lipase with its foldase from Burkholderia gladioli Bsp-1.Applied microbiology and biotechnology · 2026Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
backgroundLipases have emerged as essential biocatalysts, having the ability to contribute to a wide range of industrial applications. Microbial lipases have garnered significant industrial attention due to their stability, selectivity, and broad substrate specificity. In the previous study, a unique lipolytic bacterium (Micrococcus luteus EMP48-D) was isolated from tempeh. It turns out the bacteria produce an acidic lipase, which is important in biodiesel production. Our main objectives were to clone the acidic lipase and investigate its potential in biodiesel production.
resultIn this study, the gene encoding a lipase from M. luteus EMP48-D was cloned and expressed heterologously in Escherichia coli. To our knowledge, this is the first attempt at the cloning and expression of the lipase gene from Micrococcus luteus. The amino acid sequence was deduced from the nucleotide sequence (1356 bp) corresponded to a protein of 451 amino acid residues with a molecular weight of about 40 kDa. The presence of a signal peptide suggested that the protein was extracellular. A sequence analysis revealed that the protein had a lipase-specific Gly-X-Ser-X-Gly motif. The enzyme was identified as an acidic lipase with a pH preference of 5.0. Fatty acid preferences for enzyme activities were C8 and C12 (p-nitrophenyl esters), with optimum temperatures at 30-40 °C and still remaining active at 80°C. The enzyme was also shown to convert up to 70% of the substrate into fatty acid methyl ester.
conclusionThe enzyme was a novel acidic lipase that demonstrated both hydrolytic and transesterification reactions. It appeared particularly promising for the synthesis of biodiesel as this enzyme's catalytic reaction was optimum at low temperatures and was still active at high temperatures.
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