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The fusions of elastin-like polypeptides and xylanase self-assembled into insoluble active xylanase particles

Paper ID Volume ID Publish Year Pages File Format Full-Text
23228 43421 2014 7 PDF Available
Title
The fusions of elastin-like polypeptides and xylanase self-assembled into insoluble active xylanase particles
Abstract

•We first found the active xylanase particles on ELPs with considerable higher activity and stability.•We evaluated the characterizations of the insoluble active xylanase particles in detail and the results were encouraging.•The active xylanase particles on ELPs can be regard as “site-specific immobilized” on the ELPs.

We fused the genes of elastin-like polypeptides (ELPs) and xylanase and then expressed them in Escherichia coli. Unexpectedly, the fusion proteins self-assembled into insoluble active particles as the ELPs underwent a hardly reversible phase transition. The specific activity of the particles was 92% of the native counterparts, which means it can act as a pull-down handler for converting soluble proteins into active aggregates. We evaluated the characterizations of the insoluble active xylanase particles in detail and the results were encouraging. The pH optimum (6.0) of the particles was the same as the free one, but the optimum pH range was 5–7, while the free xylanase was 6–7. The free xylanase had an optimum temperature of 50 °C, whereas the insoluble active xylanase particles shifted to 70 °C. The pH stability, thermostability and storage stability of the xylanase particles increased significantly when compared with the free xylanase. We also observed an increase of the Km values of the free xylanase from 0.374 g L−1 to 0.980 g L−1 at the insoluble state. The considerable higher activity and stability of the xylanase particles were much like immobilized xylanases and could be valuable for its industrial application.

Keywords
Elastin-like polypeptide; Xylanase; Active protein aggregates; Stability; Immobilization
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The fusions of elastin-like polypeptides and xylanase self-assembled into insoluble active xylanase particles
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 177, 10 May 2014, Pages 60–66
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
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us