ArticleBiotechnology for biofuels2019
N-terminal domain replacement changes an archaeal monoacylglycerol lipase into a triacylglycerol lipase.
Article in Biotechnology for biofuels, 2019. 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, 20 citations in OpenAlex.
- Enhancing the characteristics of phenolic acid decarboxylase via N-terminal substitution and investigating its immobilization.BMC biotechnology · 2025Article
- Enzyme engineering for functional lipids synthesis: recent advance and perspective.Bioresources and bioprocessing · 2024Review
- N-terminal lid swapping contributes to the substrate specificity and activity of thermophilic lipase TrLipE.Frontiers in microbiology · 2023Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
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Abstract
backgroundLipolytic enzymes of hyperthermophilic archaea generally prefer small carbon chain fatty acid esters (C
resultsTON-LPL and rc-TGL were cloned and overexpressed in
conclusionsHere, we have confirmed the predicted esterase activity of TON-LPL and also performed the lid engineering on TON-LPL which effectively expanded its substrate specificity from monoglycerides to triglycerides. This approach provides a way to engineer other hyperthermophilic esterases into industrially suitable lipases by employing N-terminal domain replacement. The immobilized preparation of rc-TGL has shown significant activity with castor oil and has a potential application in castor oil biorefinery to obtain value-added chemicals.
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