Recombinant expression, refolding, purification and characterization of Pseudomonas aeruginosa protease IV in Escherichia coli
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- 作者：Mingzhi Zhaoa ; Man Caif ; Feilin Wua ; b ; Yao Zhanga ; d ; Zhi Xiongb ; Ping Xua ; c ; e ; xuping_bprc@126.com" class="auth_mail" title="E-mail the corresponding author
- 关键词：Pseudomonas aeruginosa ; Protease IV ; Recombinant expression ; Refolding ; Purification ; Activity
- 刊名：Protein Expression and Purification
- 出版年：2016
- 出版时间：October 2016
- 年：2016
- 卷：126
- 期：Complete
- 页码：69-76
- 全文大小：1654 K
文摘
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A pET-32a-TRX-pro-protease IV vector was constructed after codon optimization.
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The protease IV was expressed in inclusion bodies in Escherichia coli BL21(DE3) strain.
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A regeneration strategy composed of refolding and activation was developed.
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The auto-degradation property was efficiently inhibited during purification.
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The recombinant protease IV showed high activity and lysine digestion specificity.