An alkali tolerant α-l-rhamnosidase from Fusarium moniliforme MTCC-2088 used in de-rhamnosylation of natural glycosides.

Abstract:

:Analkali tolerant α-l-rhamnosidase has been purified to homogeneity from the culture filtrate of a new fungal strain, Fusarium moniliforme MTCC-2088, using concentration by ultrafiltration and cation exchange chromatography on CM cellulose column. The molecular mass of the purified enzyme has been found to be 36.0 kDa using SDS-PAGE analysis. The Km value using p-nitrophenyl-α-l-rhamnopyranoside as the variable substrate in 0.2 M sodium phosphate buffer pH10.5 at50 °C was 0.50 mM. The catalytic rate constant was15.6 s-1giving the values of kcat/Km is 3.12 × 104M-1 s-1. The pH and temperature optima of the enzyme were 10.5 and 50 °C, respectively. The purified enzyme had better stability at 10 °C in basic pH medium. The enzyme derhamnosylated natural glycosides like naringin to prunin, rutin to isoquercitrin and hesperidin to hesperetin glucoside. The purified α-l-rhamnosidase has potential for enhancement of wine aroma.

journal_name

Bioorg Chem

journal_title

Bioorganic chemistry

authors

Kumar D,Yadav S,Yadava S,Yadav KDS

doi

10.1016/j.bioorg.2018.11.027

subject

Has Abstract

pub_date

2019-03-01 00:00:00

pages

24-31

eissn

0045-2068

issn

1090-2120

pii

S0045-2068(18)30282-7

journal_volume

84

pub_type

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