ArticleApplied microbiology and biotechnology1996
Expression of the Arxula adeninivorans glucoamylase gene in Kluyveromyces lactis.
Article in Applied microbiology and biotechnology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 38 citations in OpenAlex.
- Article
- Structural Insight into a Yeast Maltase-TheJournal of fungi (Basel, Switzerland) · 2021Article
- Kluyveromyces lactis LAC4 promoter variants that lack function in bacteria but retain full function in K. lactis.Applied and environmental microbiology · 2005Article
- Improved production of heterologous proteins by a glucose repression-defective mutant of Kluyveromyces lactis.Applied and environmental microbiology · 2004Article
- Inducible amplification of gene copy number and heterologous protein production in the yeast Kluyveromyces lactis.Applied and environmental microbiology · 1999Article
- Expression of the Arxula adeninivorans glucoamylase gene in Kluyveromyces lactis.Applied microbiology and biotechnology · 1996Article
- Temperature-dependent dimorphism of the yeast Arxula adeninivorans Ls3.Antonie van Leeuwenhoek · 1995Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The glucoamylase gene of the yeast Arxula adeninivorans was expressed in Kluyveromyces lactis by using the GAP promoter from Saccharomyces cerevisiae and a multicopy plasmid vector. The transformants secreted 90.1% of the synthesized glucoamylase into the culture medium. The secreted glucoamylase activities are about 20 times higher in comparison to those of Saccharomyces cerevisiae transformants using the same promoter. Secreted glucoamylase possesses identical N-terminal amino acid sequences to those secreted by A. adeninivorans showing that cleavage of the N-terminal signal peptide takes place at the same site. Biochemical characteristics of glucoamylase expressed by K. lactis and A. adeninivorans are very similar.
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Registered trials
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