The patent badge is an abbreviated version of the USPTO patent document. The patent badge does contain a link to the full patent document.

The patent badge is an abbreviated version of the USPTO patent document. The patent badge covers the following: Patent number, Date patent was issued, Date patent was filed, Title of the patent, Applicant, Inventor, Assignee, Attorney firm, Primary examiner, Assistant examiner, CPCs, and Abstract. The patent badge does contain a link to the full patent document (in Adobe Acrobat format, aka pdf). To download or print any patent click here.

Date of Patent:
Apr. 30, 2019

Filed:

Jul. 24, 2017
Applicant:

Jiangnan University, Wuxi, CN;

Inventors:

Song Liu, Wuxi, CN;

Weixin Zhao, Wuxi, CN;

Jian Chen, Wuxi, CN;

Guocheng Du, Wuxi, CN;

Assignee:
Attorneys:
Primary Examiner:
Int. Cl.
CPC ...
C12N 9/00 (2006.01); C12N 5/00 (2006.01); C07K 19/00 (2006.01); C07K 1/04 (2006.01); C07K 7/08 (2006.01); C12N 9/88 (2006.01); C12N 9/02 (2006.01); C07K 14/00 (2006.01);
U.S. Cl.
CPC ...
C07K 7/08 (2013.01); C07K 14/00 (2013.01); C12N 9/0069 (2013.01); C12N 9/88 (2013.01); C12Y 113/11012 (2013.01); C12Y 402/02002 (2013.01); C07K 2319/40 (2013.01); C07K 2319/60 (2013.01);
Abstract

The present invention relates to a multi-functional peptide benefiting expression, purification, stabilization and catalytic efficiency of recombinant proteins, which relates to the field of enzyme engineering and protein purification. The present invention provides a self-assembling amphipathic peptide, which fused with proteins including alkaline polygalacturonate lyase (PGL), lipoxygenase (LOX) and green fluorescent protein (GFP), which leads to successful purification by the nickel affinity chromatography with recovery rates were 47.01%, 39.01% and 56.1%, respectively. Furthermore, the expression quantity and thermostability of the three proteins were enhanced in different degree. Of which the half-life of the PGL-S1v1 and LOX-S1v1 were 2.3 and 3.8-fold as compared with the corresponding wild-type and the specific activity were 1.1 and 1.9-fold increase, respectively. The crude enzyme activity of PGL-S1v1 was 9-fold increase than the PGL.


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