Please use this identifier to cite or link to this item: https://hdl.handle.net/11147/11421
Title: Thermoalkalophilic recombinant esterase entrapment in chitosan/calcium/alginate-blended beads and its characterization
Authors: Tercan, Cisem
Sürmeli, Yusuf
Şanlı Mohamed, Gülşah
Keywords: Esterase
Geobacillus sp.
Immobilization
Chitosan
Calcium
Alginate-blended bead
Publisher: Wiley
Abstract: BACKGROUND Esterases (EC 3.1.1.1), a class of hydrolases, degrade the ester bonds of lipids into alcohol and carboxylic acids and synthesize carboxylic ester bonds. They are used in a variety of biotechnological, industrial, environmental, and pharmaceutical applications due to their many valuable properties. Particularly, extremophilic esterases with many superior properties are of great interest for various reactions. Immobilization of enzymes may provide some advantages over free enzymes not only to improve the properties of enzymes but also to increase the reusability of biocatalyst in industrial applications. Therefore, many different immobilization applications for enzymes have been reported in various studies. To our knowledge, a thermophilic esterase has not so far been immobilized by entrapment using chitosan/calcium/alginate-blended beads. Here, we reported the immobilization of thermoalkalophilic recombinant esterase by entrapment using chitosan/calcium/alginate-blended beads, and then the entrapped esterase was characterized biochemically in details. RESULTS In the present study, a thermophilic recombinant esterase was immobilized by entrapment in chitosan/calcium/alginate-blended beads for the first time. The 0.5 mg mL(-1) purified recombinant esterase was entrapped in 1% chitosan, 2% alginate, and 0.7 M CaCl2 blended beads. The results showed that immobilization yield and entrapment efficiency of the entrapped esterase were 69.5% and 80.4%, respectively. SEM micrograph showed that the surface of the beads resembled a mesh and very compact structures. Chitosan/calcium/alginate-blended beads exhibited an 18.8% swelling ratio and had a moderate porous structure. The entrapment technique highly enhanced the thermostability of the esterase and shifted its optimum temperature from 65 to 80 degrees C. The immobilized esterase was very stable in a wide range of pH (8.5-11) displaying maximum activity at pH 9. ZnCl2 slightly increased the activity of immobilized esterase whereas several metal ions reduced the enzyme activity. When the enzyme was immobilized in chitosan/calcium/alginate-blended beads, its K-m increased about 2 times and V-max value decreased almost 1.5 times. Immobilization allowed repeated uses of the esterase having good operational stability in a continuous process. CONCLUSION The results revealed that the immobilization of a thermophilic recombinant esterase by entrapment in chitosan/calcium/alginate-blended beads exhibited considerably better compared to other immobilization processes with various entrapment strategies. (c) 2021 Society of Chemical Industry (SCI).
URI: https://doi.org/10.1002/jctb.6750
https://hdl.handle.net/11147/11421
ISSN: 0268-2575
1097-4660
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 SizeFormat 
J of Chemical Tech Biotech.pdf838.18 kBAdobe PDFView/Open
Show full item record



CORE Recommender

SCOPUSTM   
Citations

3
checked on Mar 22, 2024

WEB OF SCIENCETM
Citations

3
checked on Mar 16, 2024

Page view(s)

20,676
checked on Mar 25, 2024

Download(s)

4
checked on Mar 25, 2024

Google ScholarTM

Check




Altmetric


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