ArticleScientific reports2016
Improved Production of Active Streptomyces griseus Trypsin with a Novel Auto-Catalyzed Strategy.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 17 citations in OpenAlex.
- Molecular basis of trypsin's autolysis resistance acetylation for sustained enzymatic activity.Food chemistry: X · 2026Article
- Degradation of NaturalMarine drugs · 2024Article
- A novel method for silkworm cocoons self-degumming and its effect on silk fibers.Journal of advanced research · 2023Article
- Improving production of Streptomyces griseus trypsin for enzymatic processing of insulin precursor.Microbial cell factories · 2020Article
- Insight to Improve α-L-Arabinofuranosidase Productivity inFrontiers in microbiology · 2018Article
- Recent advances of molecular toolbox construction expand Pichia pastoris in synthetic biology applications.World journal of microbiology & biotechnology · 2017Review
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
N-terminal sequences play crucial roles in regulating expression, translation, activation and enzymatic properties of proteins. To reduce cell toxicity of intracellular trypsin and increase secretory expression, we developed a novel auto-catalyzed strategy to produce recombinant trypsin by engineering the N-terminus of mature Streptomyces griseus trypsin (SGT). The engineered N-terminal peptide of SGT was composed of the thioredoxin, glycine-serine linker, His6-tag and the partial bovine trypsinogen pro-peptide (DDDDK). Furthermore, we constructed a variant TLEI with insertion of the artificial peptide at N-terminus and site-directed mutagenesis of the autolysis residue R145. In fed-batch fermentation, the production of extracellular trypsin activity was significantly improved to 47.4 ± 1.2 U·ml(-1) (amidase activity, 8532 ± 142.2 U·ml(-1) BAEE activity) with a productivity of 0.49 U·ml(-1)·h(-1), which was 329% greater than that of parent strain Pichia pastoris GS115-SGT. This work has significant potential to be scaled-up for microbial production of SGT. In addition, the N-terminal peptide engineering strategy can be extended to improve heterologous expression of other toxic enzymes.
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