Heterologous expression of Thermomyces lanuginosus lipase in Aspergillus niger: stress resistance, optimization of fermentation conditions, and transcriptomic analysis.

Xiaoyan Shang, Rong Tang, Nanyu Han, Zunxi Huang, Le Yang

Abstract read

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Article in AMB Express, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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5 · Who and what money

Authors and funding

5 authors.

Xiaoyan Shang *Engineering Research Center for Valorization of Unique Bio-Resources in Yunnan, Ministry of Education, School of Life Sciences, Yunnan Normal University, Kunming, 650500, People's Republic of China.

Rong Tang *Engineering Research Center for Valorization of Unique Bio-Resources in Yunnan, Ministry of Education, School of Life Sciences, Yunnan Normal University, Kunming, 650500, People's Republic of China.

Nanyu HanEngineering Research Center for Valorization of Unique Bio-Resources in Yunnan, Ministry of Education, School of Life Sciences, Yunnan Normal University, Kunming, 650500, People's Republic of China.

Zunxi HuangEngineering Research Center for Valorization of Unique Bio-Resources in Yunnan, Ministry of Education, School of Life Sciences, Yunnan Normal University, Kunming, 650500, People's Republic of China.

Le YangEngineering Research Center for Valorization of Unique Bio-Resources in Yunnan, Ministry of Education, School of Life Sciences, Yunnan Normal University, Kunming, 650500, People's Republic of China. yangle@ynnu.edu.cn.

Funding

Fundamental Research Funding of Yunnan Province 202401AU070050

6 · The paper itself

Abstract

Aspergillus niger serves as a cell factory for efficient enzyme production. The lipase derived from Thermomyces lanuginosus (TLL) is known for its remarkable thermal stability and is extensively utilized in various industrial fields. In this study, a heterologous expression strain, ΔAnTll-11, of TLL was successfully constructed in A. niger. Through fermentation optimization, the lipase activity was enhanced 8.7-fold to 4547.95 U/mL, compared with the initial value of 520 U/mL. Enzymatic characterization indicated that the recombinant lipase exhibited optimum activity at pH 9.5 and 45 °C, and its activity was positively influenced by Ca

Indexed as

Aspergillus nigerFermentation condition optimizationHeterologous expressionThermomyces lanuginosus lipaseTranscriptomic

Identifiers

PMID41507679

DOI10.1186/s13568-025-02007-z

PMCPMC12873016

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LicenceCC BY-NC-ND

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.