ArticleFEMS yeast research2011
A set of aspartyl protease-deficient strains for improved expression of heterologous proteins in Kluyveromyces lactis.
Article in FEMS yeast research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 17 citations in OpenAlex.
- Proteolytic stabilization of a spider venom peptide results in an orally active bioinsecticide.Pest management science · 2025Article
- A convenient broad-host counterselectable system endowing rapid genetic manipulations of Kluyveromyces lactis and other yeast species.Microbial cell factories · 2024Article
- Identification of a Yarrowia lipolytica acetamidase and its use as a yeast genetic marker.Microbial cell factories · 2020Article
- Constructing a human complex type N-linked glycosylation pathway in Kluyveromyces marxianus.PloS one · 2020Article
- A Novel Regulated Hybrid Promoter That Permits Autoinduction of Heterologous Protein Expression in Kluyveromyces lactis.Applied and environmental microbiology · 2019Article
- Heterologous expression of an α-amylase inhibitor from common bean (Phaseolus vulgaris) in Kluyveromyces lactis and Saccharomyces cerevisiae.Microbial cell factories · 2017Article
- Development of a Candida glabrata dominant nutritional transformation marker utilizing the Aspergillus nidulans acetamidase gene (amdS).FEMS yeast research · 2016Article
- amdSYM, a new dominant recyclable marker cassette for Saccharomyces cerevisiae.FEMS yeast research · 2013Article
- Genome-wide metabolic (re-) annotation of Kluyveromyces lactis.BMC genomics · 2012Article
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Authors and funding
11 authors at 4 institutions in 1 country.
Funding
Abstract
Secretion of recombinant proteins is a common strategy for heterologous protein expression using the yeast Kluyveromyces lactis. However, a common problem is degradation of a target recombinant protein by secretory pathway aspartyl proteases. In this study, we identified five putative pfam00026 aspartyl proteases encoded by the K. lactis genome. A set of selectable marker-free protease deletion mutants was constructed in the prototrophic K. lactis GG799 industrial expression strain background using a PCR-based dominant marker recycling method based on the Aspergillus nidulans acetamidase gene (amdS). Each mutant was assessed for its secretion of protease activity, its health and growth characteristics, and its ability to efficiently produce heterologous proteins. In particular, despite having a longer lag phase and slower growth compared with the other mutants, a Δyps1 mutant demonstrated marked improvement in both the yield and the quality of Gaussia princeps luciferase and the human chimeric interferon Hy3, two proteins that experienced significant proteolysis when secreted from the wild-type parent strain.
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