Developing a Novel Enzyme Immobilization Process by Activation of Epoxy Carriers with Glucosamine for Pharmaceutical and Food Applications

In this paper, we describe the development of an efficient enzyme immobilization procedure based on the activation of epoxy carriers with glucosamine. This approach aims at both creating a hydrophilic microenvironment surrounding the biocatalyst and introducing a spacer bearing an aldehyde group for...

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Main Authors:	Immacolata Serra, Ilaria Benucci, Marina Simona Robescu, Claudio Lombardelli, Marco Esti, Cinzia Calvio, Massimo Pregnolato, Marco Terreni, Teodora Bavaro
Format:	Article
Language:	English
Published:	MDPI AG 2019-10-01
Series:	Catalysts
Subjects:	enzyme immobilization glucosamine epoxy carrier penicillin g acylase protease n bromelain γ-glutamyl transpeptidase
Online Access:	https://www.mdpi.com/2073-4344/9/10/843

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spelling	doaj-ae07a7497e034d69879668b5b31821b12020-11-24T22:10:24ZengMDPI AGCatalysts2073-43442019-10-0191084310.3390/catal9100843catal9100843Developing a Novel Enzyme Immobilization Process by Activation of Epoxy Carriers with Glucosamine for Pharmaceutical and Food ApplicationsImmacolata Serra0Ilaria Benucci1Marina Simona Robescu2Claudio Lombardelli3Marco Esti4Cinzia Calvio5Massimo Pregnolato6Marco Terreni7Teodora Bavaro8Department of Food, Environmental and Nutritional Sciences, University of Milan, Via Mangiagalli 25, I-20133 Milano, ItalyDepartment of Agriculture and Forestry Science (DAFNE), University of Tuscia, Via S. Camillo de Lellis snc, 01100 Viterbo, ItalyDepartment of Drug Sciences, University of Pavia, Viale Taramelli 12, I-27100 Pavia, ItalyDepartment of Agriculture and Forestry Science (DAFNE), University of Tuscia, Via S. Camillo de Lellis snc, 01100 Viterbo, ItalyDepartment of Agriculture and Forestry Science (DAFNE), University of Tuscia, Via S. Camillo de Lellis snc, 01100 Viterbo, ItalyDepartment of Biology and Biotechnology Lazzaro Spallanzani, University of Pavia, Via Ferrata 9, I-27100 Pavia, ItalyDepartment of Drug Sciences, University of Pavia, Viale Taramelli 12, I-27100 Pavia, ItalyDepartment of Drug Sciences, University of Pavia, Viale Taramelli 12, I-27100 Pavia, ItalyDepartment of Drug Sciences, University of Pavia, Viale Taramelli 12, I-27100 Pavia, ItalyIn this paper, we describe the development of an efficient enzyme immobilization procedure based on the activation of epoxy carriers with glucosamine. This approach aims at both creating a hydrophilic microenvironment surrounding the biocatalyst and introducing a spacer bearing an aldehyde group for covalent attachment. First, the immobilization study was carried out using penicillin G acylase (PGA) from <i>Escherichia coli</i> as a model enzyme. PGA immobilized on glucosamine activated supports has been compared with enzyme derivatives obtained by direct immobilization on the same non-modified carriers, in the synthesis of different 3′-functionalized cephalosporins. The derivatives prepared by immobilization of PGA on the glucosamine-carriers performed better than those prepared using the unmodified carriers (i.e., 90% versus 79% cefazolin conversion). The same immobilization method has been then applied to the immobilization of two other hydrolases (neutral protease from <i>Bacillus subtilis</i>, PN, and bromelain from pineapple stem, BR) and one transferase (γ-glutamyl transpeptidase from <i>Bacillus subtilis</i>, GGT). Immobilized PN and BR have been exploited in the synthesis of modified nucleosides and in a bench-scale packed-bed reactor for the protein stabilization of a Sauvignon blanc wine, respectively. In addition, in these cases, the new enzyme derivatives provided improved results compared to those previously described.https://www.mdpi.com/2073-4344/9/10/843enzyme immobilizationglucosamineepoxy carrierpenicillin g acylaseprotease nbromelainγ-glutamyl transpeptidase
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Immacolata Serra Ilaria Benucci Marina Simona Robescu Claudio Lombardelli Marco Esti Cinzia Calvio Massimo Pregnolato Marco Terreni Teodora Bavaro
spellingShingle	Immacolata Serra Ilaria Benucci Marina Simona Robescu Claudio Lombardelli Marco Esti Cinzia Calvio Massimo Pregnolato Marco Terreni Teodora Bavaro Developing a Novel Enzyme Immobilization Process by Activation of Epoxy Carriers with Glucosamine for Pharmaceutical and Food Applications Catalysts enzyme immobilization glucosamine epoxy carrier penicillin g acylase protease n bromelain γ-glutamyl transpeptidase
author_facet	Immacolata Serra Ilaria Benucci Marina Simona Robescu Claudio Lombardelli Marco Esti Cinzia Calvio Massimo Pregnolato Marco Terreni Teodora Bavaro
author_sort	Immacolata Serra
title	Developing a Novel Enzyme Immobilization Process by Activation of Epoxy Carriers with Glucosamine for Pharmaceutical and Food Applications
title_short	Developing a Novel Enzyme Immobilization Process by Activation of Epoxy Carriers with Glucosamine for Pharmaceutical and Food Applications
title_full	Developing a Novel Enzyme Immobilization Process by Activation of Epoxy Carriers with Glucosamine for Pharmaceutical and Food Applications
title_fullStr	Developing a Novel Enzyme Immobilization Process by Activation of Epoxy Carriers with Glucosamine for Pharmaceutical and Food Applications
title_full_unstemmed	Developing a Novel Enzyme Immobilization Process by Activation of Epoxy Carriers with Glucosamine for Pharmaceutical and Food Applications
title_sort	developing a novel enzyme immobilization process by activation of epoxy carriers with glucosamine for pharmaceutical and food applications
publisher	MDPI AG
series	Catalysts
issn	2073-4344
publishDate	2019-10-01
description	In this paper, we describe the development of an efficient enzyme immobilization procedure based on the activation of epoxy carriers with glucosamine. This approach aims at both creating a hydrophilic microenvironment surrounding the biocatalyst and introducing a spacer bearing an aldehyde group for covalent attachment. First, the immobilization study was carried out using penicillin G acylase (PGA) from <i>Escherichia coli</i> as a model enzyme. PGA immobilized on glucosamine activated supports has been compared with enzyme derivatives obtained by direct immobilization on the same non-modified carriers, in the synthesis of different 3′-functionalized cephalosporins. The derivatives prepared by immobilization of PGA on the glucosamine-carriers performed better than those prepared using the unmodified carriers (i.e., 90% versus 79% cefazolin conversion). The same immobilization method has been then applied to the immobilization of two other hydrolases (neutral protease from <i>Bacillus subtilis</i>, PN, and bromelain from pineapple stem, BR) and one transferase (γ-glutamyl transpeptidase from <i>Bacillus subtilis</i>, GGT). Immobilized PN and BR have been exploited in the synthesis of modified nucleosides and in a bench-scale packed-bed reactor for the protein stabilization of a Sauvignon blanc wine, respectively. In addition, in these cases, the new enzyme derivatives provided improved results compared to those previously described.
topic	enzyme immobilization glucosamine epoxy carrier penicillin g acylase protease n bromelain γ-glutamyl transpeptidase
url	https://www.mdpi.com/2073-4344/9/10/843
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Developing a Novel Enzyme Immobilization Process by Activation of Epoxy Carriers with Glucosamine for Pharmaceutical and Food Applications

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