scholarly journals Furaldehyde substrate specificity and kinetics of Saccharomyces cerevisiae alcohol dehydrogenase 1 variants

2014 ◽  
Vol 13 (1) ◽  
Author(s):  
Boaz Laadan ◽  
Valeria Wallace-Salinas ◽  
Åsa Janfalk Carlsson ◽  
João RM Almeida ◽  
Peter Rådström ◽  
...  
Biologia ◽  
2014 ◽  
Vol 69 (6) ◽  
Author(s):  
Pavol Utekal ◽  
Csaba Tóth ◽  
Anikó Illésová ◽  
Pavol Koiš ◽  
Lucia Bocánová ◽  
...  

AbstractSix-carbon aldehydes and alcohols belong to flavours and fragrances with wide application in the food, feed, cosmetic, chemical and pharmaceutical sectors. In the present study, we prepared the expression system for production of recombinant yeast alcohol dehydrogenase 1 (YADH1) from Saccharomyces cerevisiae which is suitable also for catalysis of the interconversion of C-6 aldehydes and alcohols. We have demonstrated that an effective three-step strategy can overcome the insolubility problems during YADH1 production in Escherichia coli. We used trxB and gor deficient expression strain, decreased concentration of isopropyl β-D-1-thiogalactopyranoside and lowered temperature to 20°C during induction. Finally, kinetic parameters of recombinant YADH1 were determined and we concluded it is a promising enzyme also for the interconversion of C-6 alcohols/aldehydes in green note volatile production.


Microbiology ◽  
2007 ◽  
Vol 153 (11) ◽  
pp. 3667-3676 ◽  
Author(s):  
Gemma Reverter-Branchat ◽  
Elisa Cabiscol ◽  
Jordi Tamarit ◽  
M. Alba Sorolla ◽  
M. Ángeles de la Torre ◽  
...  

1980 ◽  
Vol 45 (5) ◽  
pp. 1601-1607 ◽  
Author(s):  
Marie Stiborová ◽  
Sylva Leblová

Iodoacetate inactivates rape alcohol dehydrogenase (ADH, EC 1.1.1.1). The inactivation rate follows the kinetics of the first order, is pH-dependent, and decreases below pH 7.5. Besides irreversible alkylation of the sulfhydryl groups of the enzyme iodoacetate also forms a reversible complex with rape ADH. The coenzyme (NAD) and its analogs (ATP, ADP, AMP) competitively protect the enzyme against alkylation; o-phenanthroline also protects the enzyme against alkylation yet noncompetitively with respect to iodoacetate. Imidazole and o-phenanthroline compete with one another for binding to the protein molecule of rape ADH. Whereas o-phenanthroline decreases the inactivation rate imidazole increases the rate of iodoacetate inactivation.


ChemBioChem ◽  
2015 ◽  
Vol 16 (10) ◽  
pp. 1512-1519 ◽  
Author(s):  
Christoph Loderer ◽  
Gaurao V. Dhoke ◽  
Mehdi D. Davari ◽  
Wolfgang Kroutil ◽  
Ulrich Schwaneberg ◽  
...  

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