Partition of horseradish peroxidase in aqueous two-phase systems containing polyvinylpyrrolidone View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1998-01

AUTHORS

María V. Miranda, Osvaldo Cascone

ABSTRACT

Growing peroxidase utilisation in different industries encourages the search for high benefit/cost ratio purification methods such as aqueous two-phase partition. In this way, the partitioning behaviour of peroxidase from Armoracia rusticanaroots in polyvinylpirrolidone/Reppal and polyvinylpirrolidone/salt aqueous two-phase systems was investigated. Based on these results, a two-step purification process was developed. In the first system (polyvinylpyrrolidone K30/Reppal PES 200, pH 7.0), cell debris and some contaminating proteins were shifted to the bottom phase while peroxidase concentrated in the top phase. After discarding the bottom phase, the second step involved addition of magnesium sulphate thus forming a second aqueous two-phase system. At this step, the enzyme was extracted into the salt-rich bottom phase. The overall yield was 75% and the purification factor 7.3. More... »

PAGES

25-30

Identifiers

URI

http://scigraph.springernature.com/pub.10.1023/a:1007913300427

DOI

http://dx.doi.org/10.1023/a:1007913300427

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1006600209


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