ArticlePloS one2023
Expression and secretion of glycosylated barley oxalate oxidase in Pichia pastoris.
Article in PloS one, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed, 9 citations in OpenAlex.
- Efficient refolding, purification, and characterization of barley oxalate oxidase in Escherichia coli.Microbial cell factories · 2025Article
- Glycosylated Foot-And-Mouth Disease Virus-Like Particles Produced in Pichia Pastoris Enhance Stability and Immunogenicity.Microbial biotechnology · 2025Article
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Authors and funding
7 authors at 1 institution in 1 country.
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Abstract
Oxalate oxidase is an enzyme that degrades oxalate and is used in commercial urinary assays to measure oxalate levels. The objective of this study was to establish an enhanced expression system for secretion and purification of oxalate oxidase using Pichia pastoris. A codon optimized synthetic oxalate oxidase gene derived from Hordeum vulgare (barley) was generated and cloned into the pPICZα expression vector downstream of the N-terminal alpha factor secretion signal peptide sequence and used for expression in P. pastoris X-33 strain. A novel chimeric signal peptide consisting of the pre-OST1 sequence fused to pro-αpp8 containing several amino acid substitutions was also generated to enhance secretion. Active enzyme was purified to greater than 90% purity using Q-Sepharose anion exchange chromatography. The purified oxalate oxidase enzyme had an estimated Km value of 256μM, and activity was determined to be 10U/mg. We have developed an enhanced oxalate oxidase expression system and method for purification.
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