dc.contributor.author |
Tsitsimpikou, C |
en |
dc.contributor.author |
Voutou, D |
en |
dc.contributor.author |
Christakopoulos, P |
en |
dc.contributor.author |
Kekos, D |
en |
dc.contributor.author |
Macris, BJ |
en |
dc.contributor.author |
Kolisis, FN |
en |
dc.date.accessioned |
2014-03-01T01:10:18Z |
|
dc.date.available |
2014-03-01T01:10:18Z |
|
dc.date.issued |
1994 |
en |
dc.identifier.issn |
01415492 |
en |
dc.identifier.uri |
https://dspace.lib.ntua.gr/xmlui/handle/123456789/11361 |
|
dc.subject |
Organic Solvent |
en |
dc.subject.other |
beta glucosidase |
en |
dc.subject.other |
glucose |
en |
dc.subject.other |
hexane |
en |
dc.subject.other |
n,n dimethylformamide |
en |
dc.subject.other |
organic solvent |
en |
dc.subject.other |
pentanol |
en |
dc.subject.other |
tetrahydrofuran |
en |
dc.subject.other |
article |
en |
dc.subject.other |
enzyme activity |
en |
dc.subject.other |
enzyme stability |
en |
dc.subject.other |
freeze drying |
en |
dc.subject.other |
fusarium oxysporum |
en |
dc.subject.other |
hydrophobicity |
en |
dc.subject.other |
ph |
en |
dc.subject.other |
temperature |
en |
dc.title |
Studies of the effect of organic solvents on the stability of β-glucosidase from Fusarium oxysporum |
en |
heal.type |
journalArticle |
en |
heal.identifier.primary |
10.1007/BF01022624 |
en |
heal.identifier.secondary |
http://dx.doi.org/10.1007/BF01022624 |
en |
heal.publicationDate |
1994 |
en |
heal.abstract |
The effect of organic solvents on the stability of β-glucosidase in a powder form, isolated from Fusarium oxysporum, has been studied using several organic solvents of different degree of hydrophobicity. It was found that β-glucosidase remains quite stable after a prolonged incubation in the presence of most of the organic solvents used, even at temperatures as high as 70°C. Only dimethylformamide (DMF) and tetrahydrofuran (THF) reduce considerably the enzyme activity in a short preincubation period. Studies on the effect of the pH of the buffer used prior to lyophilization, as well as of exogenous added water to the incubation mixture, on enzyme stability show that it is more stable in pH 5.0 and in the lowest water content. In addition it was found that the presence of glucose in the lyophilization procedure gives a significant protection to the enzyme when it is incubated for 30 h in pentanol and n-hexane. |
en |
heal.journalName |
Biotechnology Letters |
en |
dc.identifier.doi |
10.1007/BF01022624 |
en |
dc.identifier.volume |
16 |
en |
dc.identifier.issue |
1 |
en |
dc.identifier.spage |
57 |
en |
dc.identifier.epage |
62 |
en |