Literature DB >> 28651873

Improving trehalose synthase activity by adding the C-terminal domain of trehalose synthase from Thermus thermophilus.

Yan Li1, Ziwei Wang1, Yue Feng1, Qipeng Yuan2.   

Abstract

The aim of this work was to study the activities of four other TreS enzymes from different sources linked with or without TtTreS-C. The results showed that a flexible linker peptide between TreS enzymes and TtTreS-C is essential for their activity enhancement. Moreover, the specific activities of the four enzymes were also improved by linking to the TtTreS-C fragment. Together, our study provides novel insights into the functions of the C-terminal domain of TtTreS, and would facilitate its future application in enzyme engineering.
Copyright © 2017 Elsevier Ltd. All rights reserved.

Entities:  

Keywords:  C-terminal domain; Expression; Specific activity; Trehalose; Trehalose synthase

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Year:  2017        PMID: 28651873     DOI: 10.1016/j.biortech.2017.05.189

Source DB:  PubMed          Journal:  Bioresour Technol        ISSN: 0960-8524            Impact factor:   9.642


  1 in total

1.  Improvement of Trehalose Production by Immobilized Trehalose Synthase from Thermus thermophilus HB27.

Authors:  Jing Sun; Shizeng Wang; Wenna Li; Ruimin Li; Sheng Chen; Hyon Il Ri; Tae Mun Kim; Myong Su Kang; Lu Sun; Xinxiao Sun; Qipeng Yuan
Journal:  Molecules       Date:  2018-05-04       Impact factor: 4.411

  1 in total

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