Follow
International Journal of Current Microbiology and Applied Sciences (IJCMAS)
IJCMAS is now DOI (CrossRef) registered Research Journal. The DOIs are assigned to all published IJCMAS Articles.
Index Copernicus ICI Journals Master List 2018 - IJCMAS--ICV 2018: 95.39 For more details click here
National Academy of Agricultural Sciences (NAAS) : NAAS Score: *5.38 (2020) [Effective from January 1, 2020]For more details click here

Login as a Reviewer

Indexed in



National Academy of Agricultural Sciences (NAAS)
NAAS Score: *5.38 (2019)
[Effective from January 1, 2019]
For more details click here

ICV 2018: 95.39
Index Copernicus ICI Journals Master List 2017 - IJCMAS--ICV 2018: 95.39
For more details click here

See Guidelines to Authors
Current Issues

Original Research Articles

PRINT ISSN : 2319-7692
Online ISSN : 2319-7706
Issues : 12 per year
Publisher : Excellent Publishers
Email : editorijcmas@gmail.com / submit@ijcmas.com
Editor-in-chief: Dr.M.Prakash
Index Copernicus ICV 2018: 95.39
NAAS RATING 2020: 5.38

Int.J.Curr.Microbiol.App.Sci.2018.7(3): 1952-1968
DOI: https://doi.org/10.20546/ijcmas.2018.703.231


De-rhamnosylation of Hesperidin to Hesperitin-7-O-Glucoside by Alkali Tolerant α-L-rhamnosidase from Fusarium poae MTCC-2086
Sarita Yadav*, Dhirendra Kumar, Sudha Yadava and K.D.S. Yadav
Department of Chemistry, DDU Gorakhpur University Gorakhpur, Gorakhpur-273009, Uttar Pradesh, India
*Corresponding author
Abstract:

An alkali tolerant α-L-rhamnosidase from the culture filtrate of a fungal strain, Fusarium poae MTCC-2086 has been purified to homogeneity. The procedure involved concentration by ultrafiltration and cation-exchange chromatography on carboxymethyl cellulose. The purified enzyme gave a single protein band corresponding to molecular mass of 51.0 kDa in SDS-PAGE analysis showing that the enzyme preparation was pure. The native PAGE analysis of the purified enzyme also gave single protein band confirming the purity of the enzyme preparation. Using p-nitrophenyl -α-L-rhamnopyranoside as substrate, Km and kcat values of the enzyme were 0.49 mM and 30.4s-1, respectively. The pH and temperature optima of the enzyme were 10.0 and 55 °C, respectively. The enzyme is stable below 10ºC and at pH 10.0. The energy of activation for thermal denaturation of enzyme determined by Arrhenius plot was 26.06 k J mol-1.The enzyme hydrolysed hesperidin to L-rhamnose and hesperitin-7-O-glucoside but it did not hydrolyse naringin and rutin.


Keywords: Hesperidin, Fusarium poae, PNPR, α-L-Rhamnosidase, L-Rhamnose
Download this article as Download

How to cite this article:

Sarita Yadav, Dhirendra Kumar, Sudha Yadava and Yadav, K.D.S. 2018. De-rhamnosylation of Hesperidin to Hesperitin-7-O-Glucoside by Alkali Tolerant α-L-rhamnosidase from Fusarium poae MTCC-2086.Int.J.Curr.Microbiol.App.Sci. 7(3): 1952-1968. doi: https://doi.org/10.20546/ijcmas.2018.703.231