Cargando…
Prevention of Bacterial Contamination of a Silica Matrix Containing Entrapped β-Galactosidase through the Action of Covalently Bound Lysozymes
β-galactosidase was successfully encapsulated within an amino-functionalised silica matrix using a “fish-in-net” approach and molecular imprinting technique followed by covalent binding of lysozyme via a glutaraldehyde-based method. Transmission electron microscopy (TEM), X-ray diffraction (XRD), sc...
Autores principales: | , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6155228/ https://www.ncbi.nlm.nih.gov/pubmed/28264511 http://dx.doi.org/10.3390/molecules22030377 |
_version_ | 1783357854605901824 |
---|---|
author | Li, Heng Li, Shuai Tian, Pu Wu, Zhuofu Li, Zhengqiang |
author_facet | Li, Heng Li, Shuai Tian, Pu Wu, Zhuofu Li, Zhengqiang |
author_sort | Li, Heng |
collection | PubMed |
description | β-galactosidase was successfully encapsulated within an amino-functionalised silica matrix using a “fish-in-net” approach and molecular imprinting technique followed by covalent binding of lysozyme via a glutaraldehyde-based method. Transmission electron microscopy (TEM), X-ray diffraction (XRD), scanning electron microscopy (SEM), and Fourier transform infrared (FTIR) spectroscopy were used to characterise the silica matrix hosting the two enzymes. Both encapsulated β-galactosidase and bound lysozyme exhibited high enzymatic activities and outstanding operational stability in model reactions. Moreover, enzyme activities of the co-immobilised enzymes did not obviously change relative to enzymes immobilised separately. In antibacterial tests, bound lysozyme exhibited 95.5% and 89.6% growth inhibition of Staphylococcus aureus ATCC (American type culture collection) 653 and Escherichia coli ATCC 1122, respectively. In milk treated with co-immobilised enzymes, favourable results were obtained regarding reduction of cell viability and high lactose hydrolysis rate. In addition, when both co-immobilised enzymes were employed to treat milk, high operational and storage stabilities were observed. The results demonstrate that the use of co-immobilised enzymes holds promise as an industrial strategy for producing low lactose milk to benefit people with lactose intolerance. |
format | Online Article Text |
id | pubmed-6155228 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-61552282018-11-13 Prevention of Bacterial Contamination of a Silica Matrix Containing Entrapped β-Galactosidase through the Action of Covalently Bound Lysozymes Li, Heng Li, Shuai Tian, Pu Wu, Zhuofu Li, Zhengqiang Molecules Article β-galactosidase was successfully encapsulated within an amino-functionalised silica matrix using a “fish-in-net” approach and molecular imprinting technique followed by covalent binding of lysozyme via a glutaraldehyde-based method. Transmission electron microscopy (TEM), X-ray diffraction (XRD), scanning electron microscopy (SEM), and Fourier transform infrared (FTIR) spectroscopy were used to characterise the silica matrix hosting the two enzymes. Both encapsulated β-galactosidase and bound lysozyme exhibited high enzymatic activities and outstanding operational stability in model reactions. Moreover, enzyme activities of the co-immobilised enzymes did not obviously change relative to enzymes immobilised separately. In antibacterial tests, bound lysozyme exhibited 95.5% and 89.6% growth inhibition of Staphylococcus aureus ATCC (American type culture collection) 653 and Escherichia coli ATCC 1122, respectively. In milk treated with co-immobilised enzymes, favourable results were obtained regarding reduction of cell viability and high lactose hydrolysis rate. In addition, when both co-immobilised enzymes were employed to treat milk, high operational and storage stabilities were observed. The results demonstrate that the use of co-immobilised enzymes holds promise as an industrial strategy for producing low lactose milk to benefit people with lactose intolerance. MDPI 2017-02-28 /pmc/articles/PMC6155228/ /pubmed/28264511 http://dx.doi.org/10.3390/molecules22030377 Text en © 2017 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Li, Heng Li, Shuai Tian, Pu Wu, Zhuofu Li, Zhengqiang Prevention of Bacterial Contamination of a Silica Matrix Containing Entrapped β-Galactosidase through the Action of Covalently Bound Lysozymes |
title | Prevention of Bacterial Contamination of a Silica Matrix Containing Entrapped β-Galactosidase through the Action of Covalently Bound Lysozymes |
title_full | Prevention of Bacterial Contamination of a Silica Matrix Containing Entrapped β-Galactosidase through the Action of Covalently Bound Lysozymes |
title_fullStr | Prevention of Bacterial Contamination of a Silica Matrix Containing Entrapped β-Galactosidase through the Action of Covalently Bound Lysozymes |
title_full_unstemmed | Prevention of Bacterial Contamination of a Silica Matrix Containing Entrapped β-Galactosidase through the Action of Covalently Bound Lysozymes |
title_short | Prevention of Bacterial Contamination of a Silica Matrix Containing Entrapped β-Galactosidase through the Action of Covalently Bound Lysozymes |
title_sort | prevention of bacterial contamination of a silica matrix containing entrapped β-galactosidase through the action of covalently bound lysozymes |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6155228/ https://www.ncbi.nlm.nih.gov/pubmed/28264511 http://dx.doi.org/10.3390/molecules22030377 |
work_keys_str_mv | AT liheng preventionofbacterialcontaminationofasilicamatrixcontainingentrappedbgalactosidasethroughtheactionofcovalentlyboundlysozymes AT lishuai preventionofbacterialcontaminationofasilicamatrixcontainingentrappedbgalactosidasethroughtheactionofcovalentlyboundlysozymes AT tianpu preventionofbacterialcontaminationofasilicamatrixcontainingentrappedbgalactosidasethroughtheactionofcovalentlyboundlysozymes AT wuzhuofu preventionofbacterialcontaminationofasilicamatrixcontainingentrappedbgalactosidasethroughtheactionofcovalentlyboundlysozymes AT lizhengqiang preventionofbacterialcontaminationofasilicamatrixcontainingentrappedbgalactosidasethroughtheactionofcovalentlyboundlysozymes |