Deakin home > Deakin University Library > Deakin Research Online > Covalent immobilization of naringinase for the transformation of a flavonoid

Covalent immobilization of naringinase for the transformation of a flavonoid

Puri, Munish, Kaur, Harsimran and Kennedy, John F. 2005, Covalent immobilization of naringinase for the transformation of a flavonoid, Journal of chemical technology and biotechnology, vol. 80, no. 10, pp. 1160-1165.

Attached Files (Some files may be inaccessible until you login with your Deakin Research Online credentials)
Name Description MIMEType Size Downloads

Title Covalent immobilization of naringinase for the transformation of a flavonoid
Author(s) Puri, Munish
Kaur, Harsimran
Kennedy, John F.
Journal name Journal of chemical technology and biotechnology
Volume number 80
Issue number 10
Start page 1160
End page 1165
Publisher Blackwell Scientific
Place of publication Oxford, England
Publication date 2005-10
ISSN 0268-2575
1097-4660
0368-1084
Keyword(s) wood chips
covalent binding
naringinase
kinnow mandarin juice
Summary Naringinase (EC 3.2.1.40) from Penicillium sp was immobilized by covalent binding to woodchips to improve its catalytic activity. The immobilization of naringinase on glutaraldehyde-coated woodchips (600 mg woodchips, 10 U naringinase, 45 °C, pH 4.0 and 12h) through 1% glutaraldehyde cross-linking was optimized. The pH-activity curve of the immobilized enzyme shifted toward a lower pH compared with that of the soluble enzyme. The immobilization caused a marked increase in thermal stability of the enzyme. The immobilized naringinase was stable during storage at 4 °C. No loss of activity was observed when the immobilized enzyme was used for seven consecutive cycles of operations. The efficiency of immobilization was 120%, while soluble naringinase afforded 82% efficacy for the hydrolysis of standard naringin under optimal conditions. Its applicability for debittering kinnow mandarin juice afforded 76% debittering efficiency. 
Language eng
Field of Research 100301 Biocatalysis and Enzyme Technology
100302 Bioprocessing, Bioproduction and Bioproducts
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©2005, Society of Chemical Industry
Persistent URL http://hdl.handle.net/10536/DRO/DU:30019706

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

Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 15 times in TR Web of Science
Scopus Citation Count Cited 16 times in Scopus
Access Statistics: 400 Abstract Views, 1 File Downloads  -  Detailed Statistics
Created: Fri, 18 Sep 2009, 16:46:46 EST by Munish Puri