ArticleJournal of industrial microbiology & biotechnology2014
Soluble expression of pullulanase from Bacillus acidopullulyticus in Escherichia coli by tightly controlling basal expression.
Article in Journal of industrial microbiology & biotechnology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers, 1 of them a synthesis that pooled it.
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Who cites it
8 citing papers in PubMed, 1 synthesis or guideline pooled it, 28 citations in OpenAlex.
- Recombinant expression of insoluble enzymes in Escherichia coli: a systematic review of experimental design and its manufacturing implications.Microbial cell factories · 2021Pooled it
- Pediococcus acidilactici WSP-AZM23: Genomic Insights, In Vitro Probiotic Potential, and Computational Analysis for Biotherapeutic Applications.Biochemical genetics · 2026Article
- Characterization of a unique phosphopantetheinyl transferase (PPTase) in the fish pathogen Pseudomonas plecoglossicida.PloS one · 2026Article
- Characterization of different isogenic mutants derived from improved strains ofBiochemistry and biophysics reports · 2025Article
- Efficient production of extracellular pullulanase in Bacillus subtilis ATCC6051 using the host strain construction and promoter optimization expression system.Microbial cell factories · 2018Article
- Efficient extracellular expression of Bacillus deramificans pullulanase in Brevibacillus choshinensis.Journal of industrial microbiology & biotechnology · 2016Article
- Downsizing a pullulanase to a small molecule with improved soluble expression and secretion efficiency in Escherichia coli.Microbial cell factories · 2016Article
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Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacillus acidopullulyticus pullulanase (BaPul13A) is a widely used debranching enzyme in the starch industry. A few details have been reported on the heterologous expression of BaPul13A in Escherichia coli (E. coli). This study compares different E. coli expression systems to improve the soluble expression level of BaPul13A. When pET22b(+)/pET28a(+) was used as the expression vector, the soluble expression of BaPul13A can be achieved by tightly controlling basal expression, whereas pET-20b(+)/pGEX4T2 leads to insoluble inclusion bodies. An efficient process control strategy aimed at minimizing the formation of inclusion bodies and enhancing the production of pullulanase was developed by a step decrease of the temperature in a 5-L fermentor. The highest total enzyme activity of BaPul13A reached 1,156.32 U/mL. This work reveals that the T7 promoter with lac operator and lacI gene collectively contribute to the soluble expression of BaPul13A, whereas either a T7 promoter alone or combined with the lac operator and lacI gene results in poor solubility. Basal expression in the initial growth phase of the host significantly affects the solubility of BaPul13A in E. coli.
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