Mannanase Transfer into Hexane and Xylene by Liquid-Liquid Extraction
The formation of noncovalent complexes between glycosidase, endo-1,4-β-d-mannanase, and ionic surfactant di(2-ethylhexyl) sodium sulfosuccinate (AOT) was shown to promote protein transfer into organic solvents such as xylene and hexane. It was found that mannanase can be solubilized in hexane and in...
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Published in | Applied biochemistry and biotechnology Vol. 160; no. 4; pp. 1124 - 1129 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
New York
New York : Humana Press Inc
01.02.2010
Humana Press Inc Springer Springer Nature B.V |
Subjects | |
Online Access | Get full text |
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Summary: | The formation of noncovalent complexes between glycosidase, endo-1,4-β-d-mannanase, and ionic surfactant di(2-ethylhexyl) sodium sulfosuccinate (AOT) was shown to promote protein transfer into organic solvents such as xylene and hexane. It was found that mannanase can be solubilized in hexane and in xylene with concentration at least 2.5 and 2.0 mg/ml, respectively. The catalytic activity of the enzyme in hexane spontaneously increases with the concentration of AOT and is about 10% of the activity in aqueous system. In xylene, a catalytic activity higher than that in bulk aqueous conditions was found for the samples containing 0.1-0.3 mg/ml of mannanase, while for the samples with a higher concentration of enzyme, the activity was hardly detected. |
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Bibliography: | http://dx.doi.org/10.1007/s12010-009-8661-5 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0273-2289 1559-0291 |
DOI: | 10.1007/s12010-009-8661-5 |