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 Chemjournal_title
Bioorganic chemistryauthors
Kumar D,Yadav S,Yadava S,Yadav KDSdoi
10.1016/j.bioorg.2018.11.027subject
Has Abstractpub_date
2019-03-01 00:00:00pages
24-31eissn
0045-2068issn
1090-2120pii
S0045-2068(18)30282-7journal_volume
84pub_type
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