Please use this identifier to cite or link to this item: https://hdl.handle.net/11147/5261
Title: Immobilization of thermoalkalophilic recombinant esterase enzyme by entrapment in silicate coated Ca-alginate beads and its hydrolytic properties
Authors: Gülay, Seçkin
Şanlı Mohamed, Gülşah
Gülay, Seçkin
Şanlı Mohamed, Gülşah
Izmir Institute of Technology. Chemistry
Keywords: Calcium alginate
Esterase
Immobilization
Silicate coating
Issue Date: Apr-2012
Publisher: Elsevier Ltd.
Source: Gülay, S. and Şanlı Mohamed, G. (2012). Immobilization of thermoalkalophilic recombinant esterase enzyme by entrapment in silicate coated Ca-alginate beads and its hydrolytic properties. International Journal of Biological Macromolecules, 50(3), 545-551. doi:10.1016/j.ijbiomac.2012.01.017
Abstract: Thermoalkalophilic esterase enzyme from Balçova (Agamemnon) geothermal site were aimed to be immobilized effectively via a simple and cost-effective protocol in silicate coated Calcium alginate (Ca-alginate) beads by entrapment. The optimal immobilization conditions of enzyme in Ca-alginate beads were investigated and obtained with 2% alginate using 0.5mg/ml enzyme and 0.7M CaCl 2 solution. In order to prevent enzyme from leaking out of the gel beads, Ca-alginate beads were then coated with silicate. Enzyme loading efficiency and immobilization yield for silicate coated beads was determined as 98.1% and 71.27%, respectively and compared with non-coated ones which were 68.5% and 45.80%, respectively. Surface morphologies, structure and elemental analysis of both silicate coated and non-coated alginate beads were also compared using Fourier Transform Infrared Spectroscopy (FT-IR) and Scanning Electron Microscope (SEM) equipped with Energy-dispersive X-ray spectroscopy (EDX). Moreover, silicate coated alginate beads enhanced reusability of esterase in continuous processes compared to non-coated beads. The hydrolytic properties of free and immobilized enzyme in terms of storage and thermal stability as well as the effects of the temperature and pH were determined. It was observed that operational, thermal and storage stabilities of the esterase were increased with immobilization.
URI: http://dx.doi.org/10.1016/j.ijbiomac.2012.01.017
http://hdl.handle.net/11147/5261
ISSN: 0141-8130
1879-0003
Appears in Collections:Chemistry / Kimya
Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection

Files in This Item:
File Description SizeFormat 
5261.pdfMakale939.86 kBAdobe PDFThumbnail
View/Open
Show full item record

CORE Recommender

SCOPUSTM   
Citations

31
checked on Sep 25, 2021

WEB OF SCIENCETM
Citations

35
checked on Sep 25, 2021

Page view(s)

20
checked on Sep 28, 2021

Download(s)

26
checked on Sep 28, 2021

Google ScholarTM

Check

Altmetric


Items in GCRIS Repository are protected by copyright, with all rights reserved, unless otherwise indicated.