Expression and characterization of a novel trehalase from Microvirga sp. strain MC18

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Updated: Nov 17, 2025

Rapid One-step Enzymatic Synthesis and All-aqueous Purification of Trehalose Analogues
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Rapid One-step Enzymatic Synthesis and All-aqueous Purification of Trehalose Analogues

Published on: February 17, 2017

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Chaonan Dong1, Qiwen Fan1, Xu Li1

  • 1Key Laboratory of Agricultural Environmental Microbiology, Ministry of Agriculture, College of Life Science, Nanjing Agricultural University, Nanjing, 210095, PR China.

Protein Expression and Purification
|February 16, 2021
PubMed

Insights

Researchers identified and characterized a bacterial trehalase from Microvirga sp. strain MC18. This glycoside hydrolase family 15 enzyme efficiently converts trehalose to glucose under optimized conditions.

Area of Science:

  • Enzymology
  • Microbiology
  • Biochemistry

Background:

  • Trehalase is crucial for trehalose hydrolysis, yielding glucose.
  • This enzyme exists in various forms across different tissues.
  • Understanding microbial trehalases offers insights into carbohydrate metabolism.

Purpose of the Study:

  • To identify and characterize a bacterial trehalase from Microvirga sp. strain MC18.
  • To investigate the enzymatic properties of the recombinant trehalase (MtreH).
  • To determine optimal conditions for trehalose bioconversion.

Main Methods:

  • Identification of a putative trehalase gene (GH15) in Microvirga sp. strain MC18.
  • Heterologous expression of the gene in E. coli.
  • Purification and biochemical characterization of the recombinant enzyme (rMtreH).

Main Results:

  • The purified recombinant trehalase MtreH showed a specific activity of 24 U/mg.
  • Optimal activity was observed at 40°C and pH 7.0, with Ca2+ enhancing stability and activity.
  • Optimized bioconversion conditions were 40°C, pH 7.0, 10 hours, and 1% trehalose.

Conclusions:

  • The characterized bacterial trehalase (rMtreH) is a functional GH15 enzyme.
  • This study enhances understanding of trehalose metabolism in prokaryotes.
  • The enzyme shows potential for biotechnological applications in trehalose bioconversion.
Keywords:
Enzymological characterizationHeterologous expressionMicrovirga sp. strain MC18Trehalase

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