Conditions for immobilization of cyclodextrin glucanotransferase from

The aim of the research is investigation on the conditions for immobilization of cyclodextrin glucanotransferase (CGTase) produced by Bacillus megaterium on DEAE-cellulose activated with glutaraldehyde. The used support was chosen as the most suitable one, after testing different supports. Several factors that influence the immobilization process on DEAE-cellulose activated with glutaraldehyde were studied, including enzyme amount, pH, glutaraldehyde concentration and time of immobilization. All tested factors significantly affected the immobilization process of CGTase and the corresponding activity parameters of immobilized biocatalyst. The immobilization process of the enzyme was evaluated by calculating the immobilization yield, immobilization efficiency and activity recovery of CGTase. As a result of the performed studies the optimal conditions for CGTase immobilization on DEAE-cellulose were determined. They were as follows: CGTase enzyme amount 8 U, pH value during immobilization 7.0, 2 % (v/v) concentration of glutaraldehyde, immobilization time of 3 h. At these conditions immobilization yield was 71.87 %, immobilization efficiency was 10.49 %, and activity recovery was 7.54 %, which were significantly improved indicators for enzyme immobilization in comparison to the initial values before the optimization of the immobilization conditions.

Authors

Publication Details

Journal
Springer Link (Chiba Institute of Technology)
Published
2025-04-01
DOI
https://doi.org/10.1051/bioconf/202517002002/pdf
Primary Topic
Enzyme Production and Characterization
Type
article
Field-Weighted Citation Impact
0.00
Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Conditions for immobilization of cyclodextrin glucanotransferase from

Hristina Panajotova, Valentina Dobreva, Boriana Zhekova, Georgi Dobrev
Springer Link (Chiba Institute of Technology)
Enzyme Production and Characterization
article

Conditions for immobilization of cyclodextrin glucanotransferase from

Hristina Panajotova, Valentina Dobreva, Boriana Zhekova, Georgi Dobrev
article en

Abstract

The aim of the research is investigation on the conditions for immobilization of cyclodextrin glucanotransferase (CGTase) produced by Bacillus megaterium on DEAE-cellulose activated with glutaraldehyde. The used support was chosen as the most suitable one, after testing different supports. Several factors that influence the immobilization process on DEAE-cellulose activated with glutaraldehyde were studied, including enzyme amount, pH, glutaraldehyde concentration and time of immobilization. All tested factors significantly affected the immobilization process of CGTase and the corresponding activity parameters of immobilized biocatalyst. The immobilization process of the enzyme was evaluated by calculating the immobilization yield, immobilization efficiency and activity recovery of CGTase. As a result of the performed studies the optimal conditions for CGTase immobilization on DEAE-cellulose were determined. They were as follows: CGTase enzyme amount 8 U, pH value during immobilization 7.0, 2 % (v/v) concentration of glutaraldehyde, immobilization time of 3 h. At these conditions immobilization yield was 71.87 %, immobilization efficiency was 10.49 %, and activity recovery was 7.54 %, which were significantly improved indicators for enzyme immobilization in comparison to the initial values before the optimization of the immobilization conditions.

Springer Link (Chiba Institute of Technology)
Openalex Percentile: Top 28%
Enzyme Production and Characterization
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.