Protein modification during antiviral heat bioprocessing

Smales, C. Mark and Pepper, Duncan S. and James, David C. (2000) Protein modification during antiviral heat bioprocessing. Biotechnology and Bioengineering, 67 (2). pp. 177-188. ISSN 0006-3592. (doi:<177::AID-BIT7>3.0.CO;2-3) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

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Heat treatment is routinely used in the preparation of:therapeutic protein biopharmaceuticals as a means of viral: inactivation. However, in undertaking virucidal :heat-treatments, a balance must be found between the bioprocessing conditions, virus kill, and the maintenance of protein integrity. In this study, we utilize a simple model protein, hen egg-white lysozyme, to investigate the relationship between antiviral bioprocess conditions(protein formulation and temperature) and the extent and type of protein modification. A variety of industrially relevant wet- and dry-heat treatments were undertaken, using formulations that included sucrose as a thermostabilizing excipient. Although there was no evidence of lysozyme aggregation or crosslinking during any of the heat-treatments, using liquid chromatography -electrospray ionization-mass spectroscopy (LC-ESI-MS) and peptide-mapping we show that protein modifications do occur with increasingly harsh heat treatment. Modifications were predominantly found after wet-heat treatment,the major covalent modification of lysozyme under these conditions being glycation of Lys(97), by either glucose-ar fructose derived from hydrolyzed sucrose. The extent of sucrose hydrolysis was itself dependent on both the duration of heat treatment and formulation composition. Advanced glycation end products (AGEs) and:additional unidentified products were also present in protein samples subjected to extended heat treatment. AGEs were; derived primarily from initial glycation by fructose and not glucose. These findings have implications for the improvement of bioprocesses to ensure protein product quality. (C) 2000 John Wiley & Sons, Inc.

Item Type: Article
Subjects: Q Science
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Mark Smales
Date Deposited: 30 May 2009 06:16 UTC
Last Modified: 23 May 2014 13:12 UTC
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