Expanding the Thermomyces lanuginosus lipase repertoire: genome-guided discovery and characterisation of three thermostable lipolytic enzymes
- 1Department of Biotechnology and Food Technology, Durban University of Technology, Durban, KZN South Africa
- 2National Research Foundation, Meiring Naude Road, Brummeria, Pretoria, South Africa
- 3College of Agriculture, Engineering and Science School of Life Science, University of KwaZulu-Natal, Westville, Durban, South Africa
Abstract
Thermomyces lanuginosus produces one of the most widely used commercial thermostable lipases, including its genetically modified variants. Although these lipases have been used for decades, no other new lipases have been reported from T. lanuginosus. Genome sequencing of this fungus resulted in the identification of additional putative lipases. A comparative sequence analysis revealed distinct differences among these additional lipolytic enzymes, exhibiting minimal sequence identity and similarity to known lipases. Their recombinant expression in Escherichia. coli yielded LipA (176.2 U/mL), LipB (184.1 U/mL), and LipC (181 U/mL). Optimal activity was observed at 60˚C and pH 8. All three enzymes preferred long chain substrates, LipA and LipB favoured p-nitrophenyl palmitate (C16) while LipC preferred p-nitrophenyl stearate (C18). The thermodynamic analysis of these lipases at 60, 70 and 80˚C showed varying deactivation energies (Ed), entropies (ΔS), and enthalpies (ΔH). LipC exhibited the lowest Kd values (0.078 to 0.193 h− 1), and the highest Ed (44.57 kJ mol− 1) and t1/2 (3.59 to 8.91) values. The elevated Ed of LipC is therefore consistent with its lower Kd values and extended half‑life, supporting its classification as the most thermostable variant in this study. These results were consistent with the in-silico prediction and analysis.
Supplementary Information: The online version contains supplementary material available at https://doi.org/10.1186/s12866-026-05220-3.
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BibTeX
@article{mbamali2026expanding,
title = {{Expanding the Thermomyces lanuginosus lipase repertoire: genome-guided discovery and characterisation of three thermostable lipolytic enzymes}},
author = {Siphiwengesihle Kuhle Silindile Mbamali and Nokuthula Peace Mchunu and Sandile Ngubane and Kugen Permaul},
journal = {BMC Microbiology},
year = {2026},
month = jul,
doi = {10.1186/s12866-026-05220-3},
url = {https://doi.org/10.1186/s12866-026-05220-3},
note = {CC BY-NC-ND 4.0},
}
RIS
TY - JOUR
TI - Expanding the Thermomyces lanuginosus lipase repertoire: genome-guided discovery and characterisation of three thermostable lipolytic enzymes
AU - Siphiwengesihle Kuhle Silindile Mbamali
AU - Nokuthula Peace Mchunu
AU - Sandile Ngubane
AU - Kugen Permaul
PY - 2026
DA - 2026/07/30
JO - BMC Microbiology
DO - 10.1186/s12866-026-05220-3
UR - https://doi.org/10.1186/s12866-026-05220-3
AB - Thermomyces lanuginosus produces one of the most widely used commercial thermostable lipases, including its genetically modified variants. Although these lipases have been used for decades, no other new lipases have been reported from T. lanuginosus. Genome sequencing of this fungus resulted in the identification of additional putative lipases. A comparative sequence analysis revealed distinct differences among these additional lipolytic enzymes, exhibiting minimal sequence identity and similarity to known lipases. Their recombinant expression in Escherichia. coli yielded LipA (176.2 U/mL), LipB (184.1 U/mL), and LipC (181 U/mL). Optimal activity was observed at 60˚C and pH 8. All three enzymes preferred long chain substrates, LipA and LipB favoured p-nitrophenyl palmitate (C16) while LipC preferred p-nitrophenyl stearate (C18). The thermodynamic analysis of these lipases at 60, 70 and 80˚C showed varying deactivation energies (Ed), entropies (ΔS), and enthalpies (ΔH). LipC exhibited the lowest Kd values (0.078 to 0.193 h− 1), and the highest Ed (44.57 kJ mol− 1) and t1/2 (3.59 to 8.91) values. The elevated Ed of LipC is therefore consistent with its lower Kd values and extended half‑life, supporting its classification as the most thermostable variant in this study. These results were consistent with the in-silico prediction and analysis. Supplementary Information: The online version contains supplementary material available at https://doi.org/10.1186/s12866-026-05220-3.
SN - 1471-2180
ER -