CHARACTERISTICS OF THE BINDING BETWEEN THE ENZYME PREPARATION RAPHANUS SATIVUS L. AND NATURAL LAYERED ALUMOSILICA IN THE PRESENCE OF IRON OXIDES

IR and X-ray analyses of bentonite modified with magnetite and enzyme established the dependence of enzyme immobilization on the presence of iron oxides. IR studies have proven that the binding of the enzyme to the carrier is adsorption in nature without stable chemical interactions. This type of bi...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Datum:2023
Hauptverfasser: Boychuk, Oleksandr, Pershina, Katherine, Kolomiets, Eugene, Pletenets, Yelyzaveta
Format: Artikel
Sprache:English
Veröffentlicht: V.I.Vernadsky Institute of General and Inorganic Chemistry 2023
Online Zugang:https://ucj.org.ua/index.php/journal/article/view/546
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Назва журналу:Ukrainian Chemistry Journal

Institution

Ukrainian Chemistry Journal
id oai:ojs2.1444248.nisspano.web.hosting-test.net:article-546
record_format ojs
spelling oai:ojs2.1444248.nisspano.web.hosting-test.net:article-5462023-07-11T08:16:58Z CHARACTERISTICS OF THE BINDING BETWEEN THE ENZYME PREPARATION RAPHANUS SATIVUS L. AND NATURAL LAYERED ALUMOSILICA IN THE PRESENCE OF IRON OXIDES Boychuk, Oleksandr Pershina, Katherine Kolomiets, Eugene Pletenets, Yelyzaveta bentonite, magnetite, modification, Raphanus Sativus L., IR-spectroscopy, XRD-analysis. IR and X-ray analyses of bentonite modified with magnetite and enzyme established the dependence of enzyme immobilization on the presence of iron oxides. IR studies have proven that the binding of the enzyme to the carrier is adsorption in nature without stable chemical interactions. This type of binding does not significantly affect the change in the structure of the enzyme module. Characte­ristic bands of vibrations of amide groups of proteins were detected at 1637 cm-1 ( ν-vibrations of C=O bonds (amide I)), 713 cm-1 (δ – vibrations of O=C-N in the plane (amide IV)), which can participate in the sorption binding of the enzyme to bentonite and the SiO2 group, which is characterized by a weak connection of the outer part of protein with the formation of a surface structure, which disappears over time due to the diffusion of molecules into the pores of the mineral. Comparison of the basal distances in the samples established the following dependence: 12.43 Å bentonite+ Fe3O4+enz (48 h) > 12.38; Å natural bentoni­te> 12.31; Å bentonite+ Fe3O4+enz (2 hours) > 11.91; Å bentonite+ Fe3O4 , which indicates a high probability of iron compounds entering the interlayer space due to the hydrolysis of magnetite with the formation of Fe-(OH)n bonds and unstable compounds. According to the research results, a scheme of the interaction of the enzyme with modified layered iron aluminosilicate is proposed: 1 – transport of the enzyme to the surface (phase distribution boundaries); 2 – deformation of the enzyme under the action of the surface as a result of a polycondensation reaction with the formation of water molecules; 3 – entry of water molecules into the interlayer space; 4 – hydrolysis of magnetite particles; 5 – extraction of iron hydroxide from the interlayer space due to the formation of aggregates with an enzyme molecule that has a related adsorption center. V.I.Vernadsky Institute of General and Inorganic Chemistry 2023-05-25 Article Article Physical chemistry Физическая xимия Фізична xімія application/pdf https://ucj.org.ua/index.php/journal/article/view/546 10.33609/2708-129X.89.04.2023.90-101 Ukrainian Chemistry Journal; Vol 89 No 4 (2023): Ukrainian Chemistry Journal; 90-101 Украинский химический журнал; Том 89 № 4 (2023): Ukrainian Chemistry Journal; 90-101 Український хімічний журнал; Том 89 № 4 (2023): Ukrainian Chemistry Journal; 90-101 2708-129X 2708-1281 en https://ucj.org.ua/index.php/journal/article/view/546/277
institution Ukrainian Chemistry Journal
baseUrl_str
datestamp_date 2023-07-11T08:16:58Z
collection OJS
language English
topic_facet bentonite
magnetite
modification
Raphanus Sativus L.
IR-spectroscopy
XRD-analysis.
format Article
author Boychuk, Oleksandr
Pershina, Katherine
Kolomiets, Eugene
Pletenets, Yelyzaveta
spellingShingle Boychuk, Oleksandr
Pershina, Katherine
Kolomiets, Eugene
Pletenets, Yelyzaveta
CHARACTERISTICS OF THE BINDING BETWEEN THE ENZYME PREPARATION RAPHANUS SATIVUS L. AND NATURAL LAYERED ALUMOSILICA IN THE PRESENCE OF IRON OXIDES
author_facet Boychuk, Oleksandr
Pershina, Katherine
Kolomiets, Eugene
Pletenets, Yelyzaveta
author_sort Boychuk, Oleksandr
title CHARACTERISTICS OF THE BINDING BETWEEN THE ENZYME PREPARATION RAPHANUS SATIVUS L. AND NATURAL LAYERED ALUMOSILICA IN THE PRESENCE OF IRON OXIDES
title_short CHARACTERISTICS OF THE BINDING BETWEEN THE ENZYME PREPARATION RAPHANUS SATIVUS L. AND NATURAL LAYERED ALUMOSILICA IN THE PRESENCE OF IRON OXIDES
title_full CHARACTERISTICS OF THE BINDING BETWEEN THE ENZYME PREPARATION RAPHANUS SATIVUS L. AND NATURAL LAYERED ALUMOSILICA IN THE PRESENCE OF IRON OXIDES
title_fullStr CHARACTERISTICS OF THE BINDING BETWEEN THE ENZYME PREPARATION RAPHANUS SATIVUS L. AND NATURAL LAYERED ALUMOSILICA IN THE PRESENCE OF IRON OXIDES
title_full_unstemmed CHARACTERISTICS OF THE BINDING BETWEEN THE ENZYME PREPARATION RAPHANUS SATIVUS L. AND NATURAL LAYERED ALUMOSILICA IN THE PRESENCE OF IRON OXIDES
title_sort characteristics of the binding between the enzyme preparation raphanus sativus l. and natural layered alumosilica in the presence of iron oxides
description IR and X-ray analyses of bentonite modified with magnetite and enzyme established the dependence of enzyme immobilization on the presence of iron oxides. IR studies have proven that the binding of the enzyme to the carrier is adsorption in nature without stable chemical interactions. This type of binding does not significantly affect the change in the structure of the enzyme module. Characte­ristic bands of vibrations of amide groups of proteins were detected at 1637 cm-1 ( ν-vibrations of C=O bonds (amide I)), 713 cm-1 (δ – vibrations of O=C-N in the plane (amide IV)), which can participate in the sorption binding of the enzyme to bentonite and the SiO2 group, which is characterized by a weak connection of the outer part of protein with the formation of a surface structure, which disappears over time due to the diffusion of molecules into the pores of the mineral. Comparison of the basal distances in the samples established the following dependence: 12.43 Å bentonite+ Fe3O4+enz (48 h) > 12.38; Å natural bentoni­te> 12.31; Å bentonite+ Fe3O4+enz (2 hours) > 11.91; Å bentonite+ Fe3O4 , which indicates a high probability of iron compounds entering the interlayer space due to the hydrolysis of magnetite with the formation of Fe-(OH)n bonds and unstable compounds. According to the research results, a scheme of the interaction of the enzyme with modified layered iron aluminosilicate is proposed: 1 – transport of the enzyme to the surface (phase distribution boundaries); 2 – deformation of the enzyme under the action of the surface as a result of a polycondensation reaction with the formation of water molecules; 3 – entry of water molecules into the interlayer space; 4 – hydrolysis of magnetite particles; 5 – extraction of iron hydroxide from the interlayer space due to the formation of aggregates with an enzyme molecule that has a related adsorption center.
publisher V.I.Vernadsky Institute of General and Inorganic Chemistry
publishDate 2023
url https://ucj.org.ua/index.php/journal/article/view/546
work_keys_str_mv AT boychukoleksandr characteristicsofthebindingbetweentheenzymepreparationraphanussativuslandnaturallayeredalumosilicainthepresenceofironoxides
AT pershinakatherine characteristicsofthebindingbetweentheenzymepreparationraphanussativuslandnaturallayeredalumosilicainthepresenceofironoxides
AT kolomietseugene characteristicsofthebindingbetweentheenzymepreparationraphanussativuslandnaturallayeredalumosilicainthepresenceofironoxides
AT pletenetsyelyzaveta characteristicsofthebindingbetweentheenzymepreparationraphanussativuslandnaturallayeredalumosilicainthepresenceofironoxides
first_indexed 2025-09-24T17:43:50Z
last_indexed 2025-09-24T17:43:50Z
_version_ 1844168182387965952