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Significant expression of a Chinese scorpion peptide, BmK1, in Escherichia coli through promoter engineering and gene dosage strategy.

Wang J, Xiong Z, Yang Y, Zhao N, Wang Y - Biotechnol. Appl. Biochem. (2013)

Bottom Line: Heterologous expression is an efficient alternative to conventional extraction to produce a specific Buthus martensii Karsch (BmK) peptide.The yield of the purified BmK1 achieved 196.74 mg L(-1) in E. coli BL21(DE3) pJF431, which was improved 2.09-fold compared with the control.This was the highest reported production of scorpion peptides in E. coli.

View Article: PubMed Central - PubMed

Affiliation: Key Laboratory of Synthetic Biology, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, People's Republic of China; State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, People's Republic of China.

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Quantification of soluble BmK1 peptide in culture. (A) SDS-PAGE analysis of the purified BmK1 peptide. (B) The yield of the purified BmK1 peptide.
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fig06: Quantification of soluble BmK1 peptide in culture. (A) SDS-PAGE analysis of the purified BmK1 peptide. (B) The yield of the purified BmK1 peptide.

Mentions: To eventually determine the actual yield of BmK1, the BmK1 peptide for pJF391, pJF393, and pJF431 was purified and quantified by Bradford method 6. The purification result is shown in Fig.6A with little impurities. The maximum yield of BmK1 was 196.74 mg L−1 in E. coli BL21 (DE3) pJF431 (Fig.6B), which was 2.09-fold improved as compared with the control E. coli BL21 (DE3) pJF391 (94.13 mg L−1). This was the highest reported production of scorpion peptides in a microbial cell factory.


Significant expression of a Chinese scorpion peptide, BmK1, in Escherichia coli through promoter engineering and gene dosage strategy.

Wang J, Xiong Z, Yang Y, Zhao N, Wang Y - Biotechnol. Appl. Biochem. (2013)

Quantification of soluble BmK1 peptide in culture. (A) SDS-PAGE analysis of the purified BmK1 peptide. (B) The yield of the purified BmK1 peptide.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4269186&req=5

fig06: Quantification of soluble BmK1 peptide in culture. (A) SDS-PAGE analysis of the purified BmK1 peptide. (B) The yield of the purified BmK1 peptide.
Mentions: To eventually determine the actual yield of BmK1, the BmK1 peptide for pJF391, pJF393, and pJF431 was purified and quantified by Bradford method 6. The purification result is shown in Fig.6A with little impurities. The maximum yield of BmK1 was 196.74 mg L−1 in E. coli BL21 (DE3) pJF431 (Fig.6B), which was 2.09-fold improved as compared with the control E. coli BL21 (DE3) pJF391 (94.13 mg L−1). This was the highest reported production of scorpion peptides in a microbial cell factory.

Bottom Line: Heterologous expression is an efficient alternative to conventional extraction to produce a specific Buthus martensii Karsch (BmK) peptide.The yield of the purified BmK1 achieved 196.74 mg L(-1) in E. coli BL21(DE3) pJF431, which was improved 2.09-fold compared with the control.This was the highest reported production of scorpion peptides in E. coli.

View Article: PubMed Central - PubMed

Affiliation: Key Laboratory of Synthetic Biology, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, People's Republic of China; State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, People's Republic of China.

No MeSH data available.


Related in: MedlinePlus