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Citation
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HERO ID
6155475
Reference Type
Journal Article
Title
Entrapment of alpha -Chymotrypsin into Hollow Polyelectrolyte
Author(s)
Antipov, AA; Larionova, NI; Lvov, Y; Mohwald, H; Sukhorukov, GB; Tiourina, OP
Year
2001
Is Peer Reviewed?
1
Journal
Macromolecular Bioscience
ISSN:
1616-5187
Volume
1
Issue
5
Page Numbers
209-214
DOI
10.1002/1616-5195(20010701)1:5<209::AID-MABbeta09>3.0.CO;2-Y
URL
https://search.proquest.com/docview/20867913?accountid=171501
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Abstract
Stable hollow polyelectrolyte capsules were produced by the layer-by-layer assembling of non-biodegradable polyelectrolytes - poly(allylamine) and poly(styrenesulfonate) on melamine formaldehyde microcores followed by the core decomposition at low pH. A proteolytic enzyme, -chymotrypsin, was encapsulated into these microcapsules with high yields of up to 100%. The encapsulation procedure was based on the protein adsorption onto the capsule shells and on the pH-dependent opening and closing of capsule wall pores. The protein in the capsules retained a high activity, and thermo- and storage stability. The nanostructured polyelectrolyte shell protected the proteinase from a high molecular weight inhibitor. Such enzyme-loaded capsules can be used as microreactors for biocatalysis.
Keywords
Biotechnology and Bioengineering Abstracts; Encapsulation; Macromolecules; Proteinase; Proteolytic enzymes; Polyelectrolytes; Shelf life; Decomposition; pH effects; Formaldehyde; Adsorption; alpha -Chymotrypsin; microcapsules; W 30900:Methods
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