A novel thermotolerant L-rhamnose isomerase variant for biocatalytic conversion of D-allulose to D-allose.

ABSTRACT: A novel L-rhamnose isomerase was identified and cloned from an extreme-temperature aquatic habitat metagenome. The deduced amino acid sequence homology suggested the possible source of this metagenomic sequence to be Chloroflexus islandicus. The gene expression was performed in a heterologous host, Escherichia coli, and the recombinant protein L-rhamnose isomerase (L-RI_M) was extracted and purified. The catalytic function of L-RI_M was characterized for D-allulose to D-allose bioconversion. D-Allose is a sweet, rare sugar molecule with anti-tumour, anti-hypertensive, cryoprotective, and antioxidative properties. The characterization experiments showed L-RI_M to be a Co⁺⁺- or Mn⁺⁺-dependent metalloenzyme. L-RI_M was remarkably a

SUBMITTER: Sharma S 

PROVIDER: S-EPMC10987364 | biostudies-literature | 2024 Apr

REPOSITORIES: biostudies-literature