Cargando…
Temperature-Triggered Enzyme Immobilization and Release Based on Cross-Linked Gelatin Nanoparticles
A glucoamylase-immobilized system based on cross-linked gelatin nanoparticles (CLGNs) was prepared by coacervation method. This system exhibited characteristics of temperature-triggered phase transition, which could be used for enzyme immobilization and release. Their morphology and size distributio...
Autores principales: | , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2012
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3468439/ https://www.ncbi.nlm.nih.gov/pubmed/23071741 http://dx.doi.org/10.1371/journal.pone.0047154 |
_version_ | 1782245949283762176 |
---|---|
author | Gan, Zhenhai Zhang, Ting Liu, Yongchun Wu, Daocheng |
author_facet | Gan, Zhenhai Zhang, Ting Liu, Yongchun Wu, Daocheng |
author_sort | Gan, Zhenhai |
collection | PubMed |
description | A glucoamylase-immobilized system based on cross-linked gelatin nanoparticles (CLGNs) was prepared by coacervation method. This system exhibited characteristics of temperature-triggered phase transition, which could be used for enzyme immobilization and release. Their morphology and size distribution were examined by transmission electron microscopy and dynamic light scattering particle size analyzer. Their temperature-triggered glucoamylase immobilization and release features were also further investigated under different temperatures. Results showed that the CLGNs were regularly spherical with diameters of 155±5 nm. The loading efficiencies of glucoamylase immobilized by entrapment and adsorption methods were 59.9% and 24.7%, respectively. The immobilized enzyme was released when the system temperature was above 40°C and performed high activity similar to free enzyme due to the optimum temperature range for glucoamylase. On the other hand, there was no enzyme release that could be found when the system temperature was below 40°C. The efficiency of temperature-triggered release was as high as 99.3% for adsorption method, while the release of enzyme from the entrapment method was not detected. These results indicate that CLGNs are promising matrix for temperature-triggered glucoamylase immobilization and release by adsorption immobilization method. |
format | Online Article Text |
id | pubmed-3468439 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-34684392012-10-15 Temperature-Triggered Enzyme Immobilization and Release Based on Cross-Linked Gelatin Nanoparticles Gan, Zhenhai Zhang, Ting Liu, Yongchun Wu, Daocheng PLoS One Research Article A glucoamylase-immobilized system based on cross-linked gelatin nanoparticles (CLGNs) was prepared by coacervation method. This system exhibited characteristics of temperature-triggered phase transition, which could be used for enzyme immobilization and release. Their morphology and size distribution were examined by transmission electron microscopy and dynamic light scattering particle size analyzer. Their temperature-triggered glucoamylase immobilization and release features were also further investigated under different temperatures. Results showed that the CLGNs were regularly spherical with diameters of 155±5 nm. The loading efficiencies of glucoamylase immobilized by entrapment and adsorption methods were 59.9% and 24.7%, respectively. The immobilized enzyme was released when the system temperature was above 40°C and performed high activity similar to free enzyme due to the optimum temperature range for glucoamylase. On the other hand, there was no enzyme release that could be found when the system temperature was below 40°C. The efficiency of temperature-triggered release was as high as 99.3% for adsorption method, while the release of enzyme from the entrapment method was not detected. These results indicate that CLGNs are promising matrix for temperature-triggered glucoamylase immobilization and release by adsorption immobilization method. Public Library of Science 2012-10-10 /pmc/articles/PMC3468439/ /pubmed/23071741 http://dx.doi.org/10.1371/journal.pone.0047154 Text en © 2012 Gan et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Gan, Zhenhai Zhang, Ting Liu, Yongchun Wu, Daocheng Temperature-Triggered Enzyme Immobilization and Release Based on Cross-Linked Gelatin Nanoparticles |
title | Temperature-Triggered Enzyme Immobilization and Release Based on Cross-Linked Gelatin Nanoparticles |
title_full | Temperature-Triggered Enzyme Immobilization and Release Based on Cross-Linked Gelatin Nanoparticles |
title_fullStr | Temperature-Triggered Enzyme Immobilization and Release Based on Cross-Linked Gelatin Nanoparticles |
title_full_unstemmed | Temperature-Triggered Enzyme Immobilization and Release Based on Cross-Linked Gelatin Nanoparticles |
title_short | Temperature-Triggered Enzyme Immobilization and Release Based on Cross-Linked Gelatin Nanoparticles |
title_sort | temperature-triggered enzyme immobilization and release based on cross-linked gelatin nanoparticles |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3468439/ https://www.ncbi.nlm.nih.gov/pubmed/23071741 http://dx.doi.org/10.1371/journal.pone.0047154 |
work_keys_str_mv | AT ganzhenhai temperaturetriggeredenzymeimmobilizationandreleasebasedoncrosslinkedgelatinnanoparticles AT zhangting temperaturetriggeredenzymeimmobilizationandreleasebasedoncrosslinkedgelatinnanoparticles AT liuyongchun temperaturetriggeredenzymeimmobilizationandreleasebasedoncrosslinkedgelatinnanoparticles AT wudaocheng temperaturetriggeredenzymeimmobilizationandreleasebasedoncrosslinkedgelatinnanoparticles |