Immobilization of Purified Pectin Lyase from Acinetobacter calcoaceticus onto Magnetic Carboxymethyl Cellulose Nanoparticles and Its Usability in Food Industry

An important component of the pectinase enzyme complex is pectin lyase (polymethylgalacturonate lyase; EC 4.2.2.10). In this study, extracellular pectin lyase enzyme was produced from Acinetobacter calcoaceticus bacteria. Pectin lyase was then purified using three-phase precipitation (TPP) technique...

Full description

Saved in:
Bibliographic Details
Main Authors: Esen Tasgin, Aynur Babagil, Hayrunnisa Nadaroglu
Format: Article
Language:English
Published: Wiley 2020-01-01
Series:Journal of Chemistry
Online Access:http://dx.doi.org/10.1155/2020/4791408
Tags: Add Tag
No Tags, Be the first to tag this record!
_version_ 1832560318143791104
author Esen Tasgin
Aynur Babagil
Hayrunnisa Nadaroglu
author_facet Esen Tasgin
Aynur Babagil
Hayrunnisa Nadaroglu
author_sort Esen Tasgin
collection DOAJ
description An important component of the pectinase enzyme complex is pectin lyase (polymethylgalacturonate lyase; EC 4.2.2.10). In this study, extracellular pectin lyase enzyme was produced from Acinetobacter calcoaceticus bacteria. Pectin lyase was then purified using three-phase precipitation (TPP) technique with 25.5% yield. The pectin lyase was immobilized covalently via the L-glutaraldehyde spacer to the carboxymethyl cellulose. The immobilized pectin lyase was magnetized using Fe3O4 nanoparticles. Purified pectin lyase was connected to magnetized support material after 90 min at the rate of 80%. The most appropriate immobilization conditions were determined as pH 8 and 30°C. By characterizing the free and immobilized enzyme, KM, Vmax, and optimum pH and optimum temperature values were determined. It was optimum pH 8 and temperature 50°C for both free and immobilized pectin lyase. The structural characterization of the immobilized pectin lyase modified with Fe3O4 nanoparticles was carried out by SEM, FT-IR, and XRD chromatographic analyses. At the end of the study, free and immobilized enzymes were used for purification of some fruit juices and results were compared.
format Article
id doaj-art-7025db4e171346768362d52f6b4ea5c4
institution Kabale University
issn 2090-9063
2090-9071
language English
publishDate 2020-01-01
publisher Wiley
record_format Article
series Journal of Chemistry
spelling doaj-art-7025db4e171346768362d52f6b4ea5c42025-02-03T01:27:54ZengWileyJournal of Chemistry2090-90632090-90712020-01-01202010.1155/2020/47914084791408Immobilization of Purified Pectin Lyase from Acinetobacter calcoaceticus onto Magnetic Carboxymethyl Cellulose Nanoparticles and Its Usability in Food IndustryEsen Tasgin0Aynur Babagil1Hayrunnisa Nadaroglu2Department of Nutrition and Dietetics, Faculty of Health Sciences, Ataturk University, 25240 Erzurum, TurkeyDepartment of Nano-Science and Nano-Engineering, Institute of Science and Technology, Ataturk University, 25240 Erzurum, TurkeyDepartment of Nano-Science and Nano-Engineering, Institute of Science and Technology, Ataturk University, 25240 Erzurum, TurkeyAn important component of the pectinase enzyme complex is pectin lyase (polymethylgalacturonate lyase; EC 4.2.2.10). In this study, extracellular pectin lyase enzyme was produced from Acinetobacter calcoaceticus bacteria. Pectin lyase was then purified using three-phase precipitation (TPP) technique with 25.5% yield. The pectin lyase was immobilized covalently via the L-glutaraldehyde spacer to the carboxymethyl cellulose. The immobilized pectin lyase was magnetized using Fe3O4 nanoparticles. Purified pectin lyase was connected to magnetized support material after 90 min at the rate of 80%. The most appropriate immobilization conditions were determined as pH 8 and 30°C. By characterizing the free and immobilized enzyme, KM, Vmax, and optimum pH and optimum temperature values were determined. It was optimum pH 8 and temperature 50°C for both free and immobilized pectin lyase. The structural characterization of the immobilized pectin lyase modified with Fe3O4 nanoparticles was carried out by SEM, FT-IR, and XRD chromatographic analyses. At the end of the study, free and immobilized enzymes were used for purification of some fruit juices and results were compared.http://dx.doi.org/10.1155/2020/4791408
spellingShingle Esen Tasgin
Aynur Babagil
Hayrunnisa Nadaroglu
Immobilization of Purified Pectin Lyase from Acinetobacter calcoaceticus onto Magnetic Carboxymethyl Cellulose Nanoparticles and Its Usability in Food Industry
Journal of Chemistry
title Immobilization of Purified Pectin Lyase from Acinetobacter calcoaceticus onto Magnetic Carboxymethyl Cellulose Nanoparticles and Its Usability in Food Industry
title_full Immobilization of Purified Pectin Lyase from Acinetobacter calcoaceticus onto Magnetic Carboxymethyl Cellulose Nanoparticles and Its Usability in Food Industry
title_fullStr Immobilization of Purified Pectin Lyase from Acinetobacter calcoaceticus onto Magnetic Carboxymethyl Cellulose Nanoparticles and Its Usability in Food Industry
title_full_unstemmed Immobilization of Purified Pectin Lyase from Acinetobacter calcoaceticus onto Magnetic Carboxymethyl Cellulose Nanoparticles and Its Usability in Food Industry
title_short Immobilization of Purified Pectin Lyase from Acinetobacter calcoaceticus onto Magnetic Carboxymethyl Cellulose Nanoparticles and Its Usability in Food Industry
title_sort immobilization of purified pectin lyase from acinetobacter calcoaceticus onto magnetic carboxymethyl cellulose nanoparticles and its usability in food industry
url http://dx.doi.org/10.1155/2020/4791408
work_keys_str_mv AT esentasgin immobilizationofpurifiedpectinlyasefromacinetobactercalcoaceticusontomagneticcarboxymethylcellulosenanoparticlesanditsusabilityinfoodindustry
AT aynurbabagil immobilizationofpurifiedpectinlyasefromacinetobactercalcoaceticusontomagneticcarboxymethylcellulosenanoparticlesanditsusabilityinfoodindustry
AT hayrunnisanadaroglu immobilizationofpurifiedpectinlyasefromacinetobactercalcoaceticusontomagneticcarboxymethylcellulosenanoparticlesanditsusabilityinfoodindustry