Modification of Silica Xerogels with Polydopamine for Lipase B from Candida antarctica Immobilization
Silica xerogels have been proposed as a potential support to immobilize enzymes. Improving xerogels’ interactions with such enzymes and their mechanical strengths is critical to their practical applications. Herein, based on the mussel-inspired chemistry, we demonstrated a simple and highly effectiv...
Published in: | Catalysts |
---|---|
Main Authors: | , , , , , |
Format: | Text |
Language: | English |
Published: |
Multidisciplinary Digital Publishing Institute
2021
|
Subjects: | |
Online Access: | https://doi.org/10.3390/catal11121463 |
id |
ftmdpi:oai:mdpi.com:/2073-4344/11/12/1463/ |
---|---|
record_format |
openpolar |
spelling |
ftmdpi:oai:mdpi.com:/2073-4344/11/12/1463/ 2023-08-20T04:02:26+02:00 Modification of Silica Xerogels with Polydopamine for Lipase B from Candida antarctica Immobilization Honghai Wang Wenda Yue Shuling Zhang Yu Zhang Chunli Li Weiyi Su 2021-11-30 application/pdf https://doi.org/10.3390/catal11121463 EN eng Multidisciplinary Digital Publishing Institute Catalytic Materials https://dx.doi.org/10.3390/catal11121463 https://creativecommons.org/licenses/by/4.0/ Catalysts; Volume 11; Issue 12; Pages: 1463 Candida antarctica lipase B silica xerogel enzyme immobilization polydopamine modification Text 2021 ftmdpi https://doi.org/10.3390/catal11121463 2023-08-01T03:24:56Z Silica xerogels have been proposed as a potential support to immobilize enzymes. Improving xerogels’ interactions with such enzymes and their mechanical strengths is critical to their practical applications. Herein, based on the mussel-inspired chemistry, we demonstrated a simple and highly effective strategy for stabilizing enzymes embedded inside silica xerogels by a polydopamine (PDA) coating through in-situ polymerization. The modified silica xerogels were characterized by scanning and transmission electron microscopy, Fourier tranform infrared spectroscopy, X-ray diffraction, X-ray photoelectron spectroscopy and pore structure analyses. When the PDA-modified silica xerogels were used to immobilize enzymes of Candida antarctica lipase B (CALB), they exhibited a high loading ability of 45.6 mg/gsupport, which was higher than that of immobilized CALB in silica xerogels (28.5 mg/gsupport). The immobilized CALB of the PDA-modified silica xerogels retained 71.4% of their initial activities after 90 days of storage, whereas the free CALB retained only 30.2%. Moreover, compared with the immobilization of enzymes in silica xerogels, the mechanical properties, thermal stability and reusability of enzymes immobilized in PDA-modified silica xerogels were also improved significantly. These advantages indicate that the new hybrid material can be used as a low-cost and effective immobilized-enzyme support. Text Antarc* Antarctica MDPI Open Access Publishing Catalysts 11 12 1463 |
institution |
Open Polar |
collection |
MDPI Open Access Publishing |
op_collection_id |
ftmdpi |
language |
English |
topic |
Candida antarctica lipase B silica xerogel enzyme immobilization polydopamine modification |
spellingShingle |
Candida antarctica lipase B silica xerogel enzyme immobilization polydopamine modification Honghai Wang Wenda Yue Shuling Zhang Yu Zhang Chunli Li Weiyi Su Modification of Silica Xerogels with Polydopamine for Lipase B from Candida antarctica Immobilization |
topic_facet |
Candida antarctica lipase B silica xerogel enzyme immobilization polydopamine modification |
description |
Silica xerogels have been proposed as a potential support to immobilize enzymes. Improving xerogels’ interactions with such enzymes and their mechanical strengths is critical to their practical applications. Herein, based on the mussel-inspired chemistry, we demonstrated a simple and highly effective strategy for stabilizing enzymes embedded inside silica xerogels by a polydopamine (PDA) coating through in-situ polymerization. The modified silica xerogels were characterized by scanning and transmission electron microscopy, Fourier tranform infrared spectroscopy, X-ray diffraction, X-ray photoelectron spectroscopy and pore structure analyses. When the PDA-modified silica xerogels were used to immobilize enzymes of Candida antarctica lipase B (CALB), they exhibited a high loading ability of 45.6 mg/gsupport, which was higher than that of immobilized CALB in silica xerogels (28.5 mg/gsupport). The immobilized CALB of the PDA-modified silica xerogels retained 71.4% of their initial activities after 90 days of storage, whereas the free CALB retained only 30.2%. Moreover, compared with the immobilization of enzymes in silica xerogels, the mechanical properties, thermal stability and reusability of enzymes immobilized in PDA-modified silica xerogels were also improved significantly. These advantages indicate that the new hybrid material can be used as a low-cost and effective immobilized-enzyme support. |
format |
Text |
author |
Honghai Wang Wenda Yue Shuling Zhang Yu Zhang Chunli Li Weiyi Su |
author_facet |
Honghai Wang Wenda Yue Shuling Zhang Yu Zhang Chunli Li Weiyi Su |
author_sort |
Honghai Wang |
title |
Modification of Silica Xerogels with Polydopamine for Lipase B from Candida antarctica Immobilization |
title_short |
Modification of Silica Xerogels with Polydopamine for Lipase B from Candida antarctica Immobilization |
title_full |
Modification of Silica Xerogels with Polydopamine for Lipase B from Candida antarctica Immobilization |
title_fullStr |
Modification of Silica Xerogels with Polydopamine for Lipase B from Candida antarctica Immobilization |
title_full_unstemmed |
Modification of Silica Xerogels with Polydopamine for Lipase B from Candida antarctica Immobilization |
title_sort |
modification of silica xerogels with polydopamine for lipase b from candida antarctica immobilization |
publisher |
Multidisciplinary Digital Publishing Institute |
publishDate |
2021 |
url |
https://doi.org/10.3390/catal11121463 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Catalysts; Volume 11; Issue 12; Pages: 1463 |
op_relation |
Catalytic Materials https://dx.doi.org/10.3390/catal11121463 |
op_rights |
https://creativecommons.org/licenses/by/4.0/ |
op_doi |
https://doi.org/10.3390/catal11121463 |
container_title |
Catalysts |
container_volume |
11 |
container_issue |
12 |
container_start_page |
1463 |
_version_ |
1774712893797826560 |