Expression of Recombinant Galactose Oxidase by Pichia pastoris
Protein Expression and Purification, ISSN: 1046-5928, Vol: 20, Issue: 1, Page: 105-111
2000
- 65Citations
- 55Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations65
- Citation Indexes65
- 65
- CrossRef48
- Captures55
- Readers55
- 55
Article Description
Galactose oxidase catalyzes the oxidation of a variety of primary alcohols, producing hydrogen peroxide as a product. Among hexose sugars, the enzyme exhibits a high degree of specificity for the C6-hydroxyl of galactose and its derivatives, underlying a number of important bioanalytical applications. Galactose oxidase cDNA has been cloned for expression in Pichia pastoris both as the full-length native sequence and as a fusion with the glucoamylase signal peptide. Expression of the full-length native sequence results in a mixture of partly processed and mature galactose oxidase. In contrast, the fusion construct directs efficient secretion of correctly processed galactose oxidase in high-density, methanol-induced fermentation. Culture conditions (including induction temperature and pH) have been optimized to improve the quality and yield (500 mg/L) of recombinant enzyme. Lowering the temperature from 30 to 25°C during the methanol induction phase results in a fourfold increase in yield. A simple two-step purification and one-step activation produce highly active galactose oxidase suitable for a wide range of biomedical and bioanalytical applications.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S1046592800912877; http://dx.doi.org/10.1006/prep.2000.1287; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0033809942&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/11035958; https://linkinghub.elsevier.com/retrieve/pii/S1046592800912877
Elsevier BV
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