Microbial Deglycosylation of Plant Metabolites: A Case Study with Actinoplanes missouriensis 431T

BAGLIONI, MICAELA; FRIES, ALEXANDER; MÜLLER, MICHAEL; BRECCIA, JAVIER D.; MAZZAFERRO, LAURA S.

ACS Food Science and Technology

American Chemical Society

Lugar: Washington, DC 20036; Año: 2022 vol. 2 p. 1141 - 1150

Actinoplanes missouriensis 431T(=NRRL B-3342) is a soil isolate, well known for its ability to degrade flavonoids. In this work, we identified an intracellular α-l-rhamnosidase from A. missouriensis 431Tin the genomic vicinity of the previously reported diglycosidase 6-O-α-l-rhamnosyl-β-d-glucosidase (αRβG). The α-l-rhamnosidase (BAL86047.1) was functionally expressed in Escherichia coli. The purified protein (94 kDa) was able to hydrolyze rutinose to the corresponding monosaccharides. The highest activity was found at 40 °C and pH 6 in sodium citrate buffer. Regarding substrate specificity, a preference for rutinose and 7-O-diglycosylated flavanones was observed, and only traces of activity (