Heterologous expression and interfacial activity evaluation of Pleurotus ostreatus hydrophobin Vmh2 mutants in Tremella fuciformis.

Yuxin Gou, Aimin Ma

Abstract read

In one paragraph

Article in World journal of microbiology & biotechnology, 2026. 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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1citing papers in PubMed

–field-weighted citation impact

1 · What the graph read from it

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3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

Production of Recombinant Hemoglobin inFoods (Basel, Switzerland) · 2026
Article

4 · The record

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5 · Who and what money

Authors and funding

2 authors.

Yuxin GouCollege of Food Science and Technology, Huazhong Agricultural University, Wuhan, 430000, China.

Aimin MaCollege of Food Science and Technology, Huazhong Agricultural University, Wuhan, 430000, China. aiminma@mail.hzau.edu.cn.

Funding

National Natural Science Foundation of China 31572182

6 · The paper itself

Abstract

Hydrophobins are exceptional amphiphilic proteins, yet their industrial adoption is hindered by a dual "production-performance" bottleneck: low natural yields and fixed interfacial properties. Vmh2 from Pleurotus ostreatus is particularly noteworthy for its unique self-assembly into long-range helical fibers, offering distinct advantages over traditional rodlet-forming hydrophobins. In this study, we implemented a synergistic optimization strategy to simultaneously overcome yield limitations and enhance interfacial functionality. By introducing site-directed mutations (N76V and S62I) into the critical Cys3-Cys4 and Cys7-Cys8 loops-which dictate surface polarity-and integrating a high-efficiency endogenous Ygyp promoter, a robust heterologous expression platform was established in Tremella fuciformis yeast-like cells. Our results demonstrate that this coordinated approach significantly elevated transcriptional levels to 11.72-fold higher than the wild type, achieving an average hydrophobin output of 20.60 mg/g DW, representing a substantial increase in hydrophobin yields. Biophysical characterization revealed that strengthening hydrophobic patches precisely modulated surface polarity, with the surface hydrophobicity index (S

Indexed as

BasidiomycotaFungal ProteinsPleurotusHydrophobic and Hydrophilic InteractionsMutagenesis, Site-DirectedMutationPromoter Regions, GeneticRecombinant ProteinsFungal ProteinsRecombinant ProteinsHeterologous expressionInterfacial activitySite-directed mutagenesisTremella fuciformisVmh2

Identifiers

PMID42201502

DOI10.1007/s11274-026-05050-5

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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.