Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.1.1.74 extracted from

  • Melo, E.P.; Baptista, R.P.; Cabral, J.M.S.
    Improving cutinase stability in aqueous solution and in reverse micelles by media engineering (2003), J. Mol. Catal. B, 22, 299-306.
No PubMed abstract available

Application

Application Comment Organism
biotechnology use of enzyme in a membrane reactor in presence of 1-hexanol, operational half-life of 674 days Fusarium solani

General Stability

General Stability Organism
encapsulation of enzyme in bis(2-ethylhexyl) sodium sulfosuccinate reverse micelles induces unfolding at room temperature, presence of 1-hexanol delays or even prevents unfolding Fusarium solani
unfolding of enzyme induced by guanidinium hydrochloride shows a stable intermediate, molten globule Fusarium solani

Organism

Organism UniProt Comment Textmining
Fusarium solani
-
-
-

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
38.5
-
50% unfolding at pH 10.9 Fusarium solani
38.5
-
50% unfolding at pH 10.9, presence of 0.5 M trehalose Fusarium solani
42
-
50% unfolding at pH 10.5 Fusarium solani
42
-
50% unfolding at pH 10.5, presence of 0.5 M trehalose Fusarium solani
49.8
-
50% unfolding at pH 4.5 Fusarium solani
49.8
-
50% unfolding at pH 4.5, presence of 0.5 M trehalose Fusarium solani
52.6
-
50% unfolding at pH 9.2 Fusarium solani
52.6
-
50% unfolding at pH 9.2, presence of 0.5 M trehalose Fusarium solani