ArticleJournal of industrial microbiology & biotechnology2010
Production and single-step purification of Brugia malayi abundant larval transcript (ALT-2) using hydrophobic interaction chromatography.
Article in Journal of industrial microbiology & biotechnology, 2010. 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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Who cites it
7 citing papers in PubMed, 17 citations in OpenAlex.
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- Dissolved-oxygen feedback control fermentation for enhancing β-carotene in engineered Yarrowia lipolytica.Scientific reports · 2020Article
- Development of nsP2 protease based cell free high throughput screening assay for evaluation of inhibitors against emerging Chikungunya virus.Scientific reports · 2018Article
- Sophisticated Cloning, Fermentation, and Purification Technologies for an Enhanced Therapeutic Protein Production: A Review.Frontiers in pharmacology · 2017Review
- Immunogenicity of Brugia malayi Abundant Larval Transcript-2, a potential filarial vaccine candidate expressed in tobacco.Plant cell reports · 2014Article
- Production of recombinant nonstructural 1 protein in Escherichia coli for early detection of Japanese encephalitis virus infection.Microbial biotechnology · 2012Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Abundant larval transcript (ALT), a novel filarial protein, has been shown to have great potential as a vaccine in the prevention of human lymphatic filariasis. In this study, we report a method for the production of recombinant ALT-2 protein, expressed in the cytoplasm of bacterium Escherichia coli in soluble form and purification in a single step using hydrophobic interaction chromatography (HIC). Fermentation was done by continuous fed-batch methodology with dissolved oxygen (DO)-controlled feed addition. The culture was induced with 1 mM isopropyl-β-D: -thiogalactopyranoside (IPTG). Up to 9 g/l dry cell weight (DCW) of biomass was obtained from 1.6 l of Luria-Bertani (LB) broth in a bench-scale reactor. Around 200 mg/l of purified ALT-2 with a yield of about 60% was obtained. This is almost a 2.5-fold increase in final protein yield compared to purification using immobilized metal affinity chromatography (IMAC).
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