The influence of elastin-like polypeptides length on the enzymatic properties of insoluble active ELPs-xylanase aggregates*

The length of elastin-like polypeptides (ELPs) is an important factor affecting the properties of the insoluble active ELPs-xylanase aggregates (IAEXA), but such effect lacks systematic research. In this study we constructed the cloning and expression vector of the fusion gene with xylanase and different length of ELPs, obtained the IAEXA with different length of ELPs by expression and purification, and investigated the enzymatic properties in detail. It showed that the optimum temperature of all the IAEXA was 70 °C, which was 20 °C higher than that of the free xylanase; the optimal pH of IAEXA was 7.0, which was 1 pH unit higher than that of the free one but still kept more than 80% of the activity at pH 8-9, with the alkali-resistant ability greatly improved. The thermal stability of IAEXA was the best with 40 repeat ELPs, the pH stability and reusability the best with 80 repeat ELPs, and the substrate affinity the best with 60 repeats of ELPs. The IAEXAs formed with the longer ELPs were better both in catalytic activity and reusability and might have more potential in biocatalysis.

• Publication year

  2016

• Venue

  Chinese Journal of Applied and Environmental Biology

• Publication date

  2016-10-01

• Fields of study

  Not labeled

• Identifiers
  DOI 10.3724/sp.j.1145.2015.12018
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar

• No claims are published for this paper.

• No concepts are published for this paper.

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