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[Purification and physico-chemical properties of Eupenicillium erubescens alpha-L- rhamnosidase].

Authors: E V, Gudzenko; L D, Varbanets;

[Purification and physico-chemical properties of Eupenicillium erubescens alpha-L- rhamnosidase].

Abstract

A scheme of isolation and purification of the enzyme with alpha-L-rhamnosidase activity has been developed. It included fractionation by ammonium sulfate and chromatography on TSK-gels Toyopearl HW-60, Fractogel TSK DEAE-650-s and Sepharose 6B. The enzyme was purified 60 times with the yield of 0.5%. The enzyme preparation did not contain any glycosidase and proteolytic activity. Molecular mass of the alpha-L-rhamnosidase enzyme on the data of Sepharose 6B gel-filtration was 35 kDa. The enzyme preparation was stable during 48 hours at 20 degrees C, its pH- and thermal optimum were 5 and 60 degrees C, correspondingly.

Keywords

Glycoside Hydrolases, Temperature, Hydrogen-Ion Concentration, Chromatography, Agarose, Culture Media, Fungal Proteins, Molecular Weight, Ammonium Sulfate, Enzyme Stability, Eupenicillium

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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
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popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
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