Halomonas elongata: a microbial source of highly stable enzymes for applied biotechnology

Abstract

Extremophilic microorganisms, which are resistant to extreme levels of temperature, salinity, pH, etc., have become popular tools for biotechnological applications. Due to their availability and cost-efficacy, enzymes from extremophiles are getting the attention of researchers and industries in the field of biocatalysis to catalyze diverse chemical reactions in a selective and sustainable manner. In this mini-review, we discuss the advantages of Halomonas elongata as moderate halophilic bacteria to provide suitable enzymes for biotechnology. While enzymes from H. elongata are more resistant to the presence of salt compared to their mesophilic counterparts, they are also easier to produce in heterologous hosts compared with more extremophilic microorganisms. Herein, a set of different enzymes (hydrolases, transferases, and oxidoreductases) from H. elongata are showcased, highlighting their interesting properties as more efficient and sustainable biocatalysts. With this, we aim to improve the visibility of halotolerant enzymes and their uncommon properties to integrate biocatalysis in industrial set-ups. KEYPOINTS: • Production and use of halotolerant enzymes can be easier than strong halophilic ones. • Enzymes from halotolerant organisms are robust catalysts under harsh conditions. • Halomonas elongata has shown a broad enzyme toolbox with biotechnology applications.

Keywords: Biocatalysis; Biotechnology; Co-solvent stability; Enzyme; Halomonas; Halotolerant.

Fig. 1

Overview of the application of enzymes from H. elongata. Reaction schemes represent the main types of enzymatic reactions described by using enzymes from H. elongata

Fig. 2

Comparison of the residue composition of a halotolerant aminotransferase enzyme (Uniprot: E1V913) and its homolgous from E. coli (Uniprot: P42588). Asp and Glu residues are highlighted in red, while Phe, Leu, and Ile are depicted in white