ArticleIndian journal of microbiology2015
Heterologous Expression and Efficient Secretion of Chitosanase from Microbacterium sp. in Escherichia coli.
Article in Indian journal of microbiology, 2015. 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, 26 citations in OpenAlex.
- Article
- Genome-wide identification of the crustacyanin gene family in Neocaridina denticulata sinensis based on comparative genomics and localization analysis.BMC genomics · 2025Article
- Molecular characterization and functional analysis of peroxiredoxin 3 (NdPrx3) fromFish and shellfish immunology reports · 2023Article
- Gene cloning and molecular characterization of a thermostable chitosanase from Bacillus cereus TY24.BMC biotechnology · 2022Article
- Genomics and transcriptomics reveal new molecular mechanism of vibriosis resistance in fish.Frontiers in immunology · 2022Article
- A temperature-induced chitosanase bacterial cell-surface display system for the efficient production of chitooligosaccharides.Biotechnology letters · 2021Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
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Abstract
A recombinant expression vector, pCT7-CHISP6H, was constructed for the secretory expression of mature peptide of chitosanase (mMschito) from Microbacterium sp. OU01. The vector contains several elements, including T7 promoter, signal peptide sequence of mschito, 6 × His-tag sequence and PmaCI restriction enzyme cloning site. In pCT7-CHISP6H, mMschito was fused into signal peptide sequence of mschito gene to construct recombinant plasmid pCT7-CHISP6H-mMschito. The recombinant plasmid was transformed into Escherichia coli BL21(DE3) and then expressed. The recombinant protein was secreted into the Luria-Bertani broth and the chitosanase activity in supernatant of the culture could reach up to 67.56 U/mL. The rmMschito in the broth supernatant was purified using HisTrap™ FF Crude column and the purified rmMschito was shown to be apparent homogeneity by 12 % SDS-PAGE analysis. Detected by 4700 MALDI-TOF-TOF-MS, the molecular weight of the purified rmMschito was 26,758.1875 and it was consistent with the predicted molecular weight. Chitosan (degree of deacetylation of 99 %) was mostly hydrolyzed into chitopentaose, chitotriose, and chitobiose by the purified rmMschito.
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