Home > Chemistry > Biochemistry > Volume-2 > Issue-5 > Prunin Production From Orange Peel Naringin Hydrolyzed By a-L-rhamnosidase from Aspergillus Flavipus MTCC- 4644

Prunin Production From Orange Peel Naringin Hydrolyzed By a-L-rhamnosidase from Aspergillus Flavipus MTCC- 4644

Call for Papers

Volume-4 | Issue-4

Last date : 26-Jun-2020

Best International Journal
Open Access | Peer Reviewed | Best International Journal | Indexing & IF | 24*7 Support | Dedicated Qualified Team | Rapid Publication Process | International Editor, Reviewer Board | Attractive User Interface with Easy Navigation

Journal Type : Open Access

Processing Charges : 700/- INR Only OR 25 USD (for foreign users)

Paper Publish : Within 2-4 Days after submitting

Submit Paper Online

For Author

IJTSRD Publication

Research Area


Prunin Production From Orange Peel Naringin Hydrolyzed By a-L-rhamnosidase from Aspergillus Flavipus MTCC- 4644


Sarita Yadav

https://doi.org/10.31142/ijtsrd16969



Sarita Yadav "Prunin Production From Orange Peel Naringin Hydrolyzed By a-L-rhamnosidase from Aspergillus Flavipus MTCC- 4644" Published in International Journal of Trend in Scientific Research and Development (ijtsrd), ISSN: 2456-6470, Volume-2 | Issue-5, August 2018, pp.1271-1278, URL: https://www.ijtsrd.com/papers/ijtsrd16969.pdf

An orange (Citrus sinensis) is the most common fruits in the world. The wastes generated from the orange fruit needs to be put in to beneficial use. In this study the primary wastes (peel) of orange is use for preparation of prunin. a-L-Rhamnosidase (EC 3.2.1.40) secreted by Aspergillus flavipus MTCC-4644 are potential catalysis in hydrolysis of naringin content present in orange peels. a-L-rhamnosidase from the culture filtrate of a fungal strain, Aspergillus flavipus MTCC-4446 has been purified to homogeneity. The procedure involved concentration by ultra filtration and cation-exchange chromatography on carboxymethyl cellulose. The purified enzyme gave a single protein band corresponding to molecular mass of 40.0 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-nitro phenyl -a-L-rhamnopyranoside as substrate, Km and kcat values of the enzyme were 0.48 mM and 28. 4 s-1 respectively. The pH and temperature optima of the enzyme were 5.0 and 50 °C, respectively. The enzyme is stable below10ºC and at pH 4.5. The energy of activation for thermal denaturation of enzyme determined by Arrhenius plot was 32.06 k J mol-1.The enzyme hydrolyzed naringin content of orange peel to L-rhamnose and prunin.

Citrus sinansis, Naringin, a-L-Rhamnosidase, Prunin, Aspergillus flavipus, L- rhamnose


IJTSRD16969
Volume-2 | Issue-5, August 2018
1271-1278
IJTSRD | www.ijtsrd.com | E-ISSN 2456-6470
Copyright © 2019 by author(s) and International Journal of Trend in Scientific Research and Development Journal. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (CC BY 4.0) (http://creativecommons.org/licenses/by/4.0)

International Journal of Trend in Scientific Research and Development - IJTSRD having online ISSN 2456-6470. IJTSRD is a leading Open Access, Peer-Reviewed International Journal which provides rapid publication of your research articles and aims to promote the theory and practice along with knowledge sharing between researchers, developers, engineers, students, and practitioners working in and around the world in many areas like Sciences, Technology, Innovation, Engineering, Agriculture, Management and many more and it is recommended by all Universities, review articles and short communications in all subjects. IJTSRD running an International Journal who are proving quality publication of peer reviewed and refereed international journals from diverse fields that emphasizes new research, development and their applications. IJTSRD provides an online access to exchange your research work, technical notes & surveying results among professionals throughout the world in e-journals. IJTSRD is a fastest growing and dynamic professional organization. The aim of this organization is to provide access not only to world class research resources, but through its professionals aim to bring in a significant transformation in the real of open access journals and online publishing.

Thomson Reuters
Google Scholer
Academia.edu

ResearchBib
Scribd.com
archive

PdfSR
issuu
Slideshare

WorldJournalAlerts
Twitter
Linkedin