Updates on naringinase : structural and biotechnological aspects

Puri, Munish 2012, Updates on naringinase : structural and biotechnological aspects, Applied microbiology and biotechnology, vol. 93, no. 1, pp. 49-60.

Attached Files
Name Description MIMEType Size Downloads

Title Updates on naringinase : structural and biotechnological aspects
Author(s) Puri, MunishORCID iD for Puri, Munish orcid.org/0000-0003-2469-3326
Journal name Applied microbiology and biotechnology
Volume number 93
Issue number 1
Start page 49
End page 60
Total pages 12
Publisher Springer
Place of publication Berlin, Germany
Publication date 2012
ISSN 0175-7598
Keyword(s) debittering
family 78 glycosides hydrolases
Summary Naringinases has attracted a great deal of attention in recent years due to its hydrolytic activities which include the production of rhamnose, and prunin and debittering of citrus fruit juices. While this enzyme is widely distributed in fungi, its production from bacterial sources is less commonly known. Fungal naringinase are very important as they are used industrially in large amounts and have been extensively studied during the past decade. In this article, production of bacterial naringinase and potential biotechnological applications are discussed. Bacterial rhamnosidases are exotype enzymes that hydrolyse terminal non-reducing α-l-rhamnosyl groups from α-l-rhamnose containing polysaccharides and glycosides. Structurally, they are classified into family 78 of glycoside hydrolases and characterized by the presence of Asp567 and Glu841 in their active site. Optimization of fermentation conditions and enzyme engineering will allow the development of improved rhamnosidases for advancing suggested industrial applications.
Language eng
Field of Research 100302 Bioprocessing, Bioproduction and Bioproducts
100301 Biocatalysis and Enzyme Technology
090805 Food Processing
Socio Economic Objective 860105 Nutraceuticals and Functional Foods
HERDC Research category C1 Refereed article in a scholarly journal
Copyright notice ©2011, Springer-Verlag
Persistent URL http://hdl.handle.net/10536/DRO/DU:30044169

Connect to link resolver
Unless expressly stated otherwise, the copyright for items in DRO is owned by the author, with all rights reserved.

Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 33 times in TR Web of Science
Scopus Citation Count Cited 46 times in Scopus
Google Scholar Search Google Scholar
Access Statistics: 431 Abstract Views, 9 File Downloads  -  Detailed Statistics
Created: Thu, 05 Apr 2012, 15:54:44 EST

Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.