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High-level expression of soluble human β-defensin-2 in Escherichia coli

Paper ID Volume ID Publish Year Pages File Format Full-Text
36761 45146 2004 7 PDF Available
Title
High-level expression of soluble human β-defensin-2 in Escherichia coli
Abstract

Human β-defensin-2 (hBD2) is a short cationic peptide with a broad antimicrobial spectrum. The coding sequence of hBD2 was cloned into pET-32a (+) to construct a fusion expression plasmid, pET32–hBD2, which was transformed into E. coli BL21 (DE3) for expression. The cultivation parameters of the expression vector harboring strain were optimized to produce the fusion protein in soluble form efficiently and to avoid the formation of insoluble inclusion bodies. The optimal conditions were determined as following: cultivation at 28 °C in MBL medium, induction at middle stage of exponential growth with 0.8 mM IPTG, and post-induction expression for 8 h. Under the above conditions, a high percentage of the target fusion protein (≥92.3%) was expressed in soluble form and the volumetric productivity of soluble fusion protein reached 1.3 g/l. The culture process was successfully scaled up in a 10 l bench-top fermentor.

Keywords
Antimicrobial peptide; Human β-defensin-2; Soluble protein; Optimization
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High-level expression of soluble human β-defensin-2 in Escherichia coli
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 39, Issue 12, 29 October 2004, Pages 2199–2205
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
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Full-text PDF Download
Online Support
Any Questions? feel free to contact us