Enhancement of the activity of renatured lysozyme by protein disulfide isomerase

The coexistence of protein disulfide isomerase (PDI) in the oxidative refolding of a fully reduced hen egg white lysozyme brought about a final recovered activity significantly exceeding 100% in addition to the expected acceleration effect. This increase could not be explained by the simple increase...

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Veröffentlicht in:	Journal of bioscience and bioengineering 2007-09, Vol.104 (3), p.235-237
Hauptverfasser:	Nohara, Daisuke, Hizikata, Hiroshi, Asami, Osamu
Format:	Artikel
Sprache:	eng
Schlagworte:	Biological and medical sciences Biotechnology BLANC D'OEUF chaperone CLARA DE HUEVO EGG WHITE enhancement of activity Enzyme Activation Enzyme Stability Fundamental and applied biological sciences. Psychology GLUTATHION GLUTATHIONE GLUTATION ISOMERASAS ISOMERASE ISOMERASES LISOZIMA LYSOZYME lysozyme refolding Muramidase - chemistry PROTEASAS PROTEASE PROTEASES Protein Denaturation protein disulfide isomerase Protein Disulfide-Isomerases - chemistry Protein Folding
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Beschreibung
Zusammenfassung:	The coexistence of protein disulfide isomerase (PDI) in the oxidative refolding of a fully reduced hen egg white lysozyme brought about a final recovered activity significantly exceeding 100% in addition to the expected acceleration effect. This increase could not be explained by the simple increase produced by suppressing aggregation. After examination of the starting material and assay system, it was concluded that PDI enhances the activity of renatured lysozyme.
ISSN:	1389-1723 1347-4421
DOI:	10.1263/jbb.104.235