Construction of an Aspergillus oryzae △nptB△pyrG Host for Homologous Expression of Lipase and Catalytic Property Characterization of Recombinant Lipase.

Yueting Zhang, Hongmei Nie, Fei Zhang, Mengmeng Jin, Zhao Wang, Jianyong Zheng

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Article in Applied biochemistry and biotechnology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

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Development ofJournal of fungi (Basel, Switzerland) · 2024
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6 authors.

Yueting ZhangKey Laboratory of Bioorganic Synthesis of Zhejiang Province, College of Biotechnology and Bioengineering, Zhejiang University of Technology, Hangzhou, 310014, China.

Hongmei NieKey Laboratory of Bioorganic Synthesis of Zhejiang Province, College of Biotechnology and Bioengineering, Zhejiang University of Technology, Hangzhou, 310014, China.

Fei ZhangKey Laboratory of Bioorganic Synthesis of Zhejiang Province, College of Biotechnology and Bioengineering, Zhejiang University of Technology, Hangzhou, 310014, China.

Mengmeng JinKey Laboratory of Bioorganic Synthesis of Zhejiang Province, College of Biotechnology and Bioengineering, Zhejiang University of Technology, Hangzhou, 310014, China.

Zhao WangKey Laboratory of Bioorganic Synthesis of Zhejiang Province, College of Biotechnology and Bioengineering, Zhejiang University of Technology, Hangzhou, 310014, China.

Jianyong ZhengKey Laboratory of Bioorganic Synthesis of Zhejiang Province, College of Biotechnology and Bioengineering, Zhejiang University of Technology, Hangzhou, 310014, China. zjy821212@zjut.edu.cn.ORCID http://orcid.org/0000-0002-9821-1062

Funding

National Defense Science and Technology Innovation Fund of the Chinese Academy of Sciences cstc2021jscx-jbgsX0002National Natural Science Foundation of China no. 31600639

6 · The paper itself

Abstract

Aspergillus oryzae is an ideal cell factory for protein expression with powerful protein processing and secretion capabilities. The current study aimed to explore the homologous expression of A. oryzae lipase AOL (GenBank: KP975533) by constructing an auxotrophic A. oryzae △pyrG△nptB and subsequently characterizing the immobilization and catalytic properties of recombinant lipase. Initially, the pyrG gene knocked out in wild-type A. oryzae by homologous recombination, followed by the creation of a uridine/uracil auxotroph transformation. Through this system, the protease gene nptB was precisely knocked out, leading to a substantial decrease in extracellular (39.04%) and intracellular (90.07%) protease activity. The A. oryzae △nptB△pyrG strain was used as host for homologous expression of lipase AOL. After transformation of linearized lipase-expression cassette, the engineered A. oryzae AOL-8 was screened out with the lipase gene copy number of 14, exhibiting extracellular and intracellular lipase activities of 1.75 U/mL and 46.4 U/g, respectively. Subsequently, the production and immobilization of the recombinant lipase, via physical adsorption on macroporous resin XRZ04B, were achieved through submerged fermentation of the AOL-8 strain. The results of esterification catalytic properties of immobilized recombinant lipase indicated that the lipase exhibited optimal catalytic activity with lauric acid and methanol as substrates, a reaction temperature of 35 °C, and n-hexane as the preferred solvent medium; its highest conversion rate can reach at 72.3%.

Indexed as

Aspergillus oryzaeFungal ProteinsLipaseBiocatalysisCatalysisEnzymes, ImmobilizedRecombinant ProteinsEnzymes, ImmobilizedFungal ProteinsLipaseRecombinant ProteinsAspergillus oryzaeAuxotrophicEsterification catalytic propertiesHomologous expressionLipase

Identifiers

PMID39325292

DOI10.1111/j.1432-1033.2004.04163.x

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