2001
DOI: 10.1016/s0168-1656(01)00250-4
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Stability of an extreme halophilic alkaline phosphatase from Halobacterium salinarium in non-conventional medium

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Cited by 13 publications
(7 citation statements)
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“…Since solar salterns are exposed to intense sunlight, the enzymes of halophilic organisms have to endure high temperatures in their natural environments. This thermophilic nature has been reported not only for amylase but also for other halophilic enzymes in several organisms (22)(23)(24)(25).…”
Section: The Eff Ect Of Temperature On Purifi Ed Amylasesupporting
confidence: 58%
“…Since solar salterns are exposed to intense sunlight, the enzymes of halophilic organisms have to endure high temperatures in their natural environments. This thermophilic nature has been reported not only for amylase but also for other halophilic enzymes in several organisms (22)(23)(24)(25).…”
Section: The Eff Ect Of Temperature On Purifi Ed Amylasesupporting
confidence: 58%
“…However, in aqueous medium, the difference was approximately 85% (Bonet et al 1991), indicating that the reverse micellar system has a stabilizing effect on the halophilic enzyme (Marhuenda-Egea et al 2001a).…”
Section: Discussionmentioning
confidence: 93%
“…One region consists of water structured around the polar heads of the surfactant, whereas the other region consists of free water in the center of the water pool within the micelle (Bru et al 1995). At low w 0 values, all water is structured (i.e., arranged around the polar heads of surfactant molecules) and the stability of the enzyme increases (Marhuenda-Egea et al 2001a). When w 0 is increased, the structure of the water in the reverse micelles changes and the activity of the encapsulated enzyme increases (Tuena de Gómez-Puyou andGómez-Puyou 1998, Marhuenda-Egea et al 2000b) until high w 0 values are reached, at which point the proportion of free water increases and enzyme stability and activity decrease (Bru et al 1995).…”
Section: Discussionmentioning
confidence: 99%
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“…Changes in K m and V max in reversed micelles (Marhuenda-Egea et al, 2000), higher stability in reversed micelles than in aqueous media (Marhuenda-Egea et al, 2001a), and changes in the kinetic behavior at low salt concentration (Marhuenda-Egea et al, 2001b) suggested that pNPPase from H. salinarum was adapted to the microenvironment inside the reversed micelles. In this work we studied the changes in the catalytic mechanism of this halophilic enzyme when it was encapsulated in reversed micelles, and the role of water under these conditions.…”
Section: Introductionmentioning
confidence: 99%