Effects of water activity and aqueous solvent ordering on thermal stability of lysozyme, α-chymotrypsinogen A, and alcohol dehydrogenase

2001 ◽  
Vol 28 (5) ◽  
pp. 343-349 ◽  
Author(s):  
Sueko Matsue ◽  
Tomoyuki Fujii ◽  
Osato Miyawaki
Keyword(s):  
Thermal Stability ◽  
Alcohol Dehydrogenase ◽  
Water Activity ◽  
Aqueous Solvent ◽  
Thermal Stability Of

Isolation and Partial Characterization of Alcohol Dehydrogenase From Broad Bean (Vicia faba)

1974 ◽  
Vol 1 (4) ◽  
pp. 579 ◽  
Author(s):  
S Leblova
Keyword(s):  
Thermal Stability ◽  
Alcohol Dehydrogenase ◽  
Broad Bean ◽  
Plant Tissues ◽  
Growth Substances ◽  
Ph Optimum ◽  
Alcohol Dehydrogenase Activity ◽  
Km Value ◽  
Thermal Stability Of

Alcohol dehydrogenase isolated from broad bean was found to have a Km value of 1.0 × 1.0 -2 M, a pH optimum of 8.7 and a molecular weight of 60 000 � 5000. The enzyme lost 55 % of its activity after being heated at 55�C, and was totally inactivated at 70°C. Thermal stability of the enzyme was not enhanced by NAD+ or ethanol. The substrate specificity of the enzyme is reported. Cysteine and mercaptoethanol activated the enzyme, whilep-chloromercuribenzoate, Cu2+, Hg2+, B4O72- -, Zn2+ and EDTA inhibited it. The influence of ethanol, acetaldehyde and growth substances on alcohol dehydrogenase activity in germinating broad bean seeds and plant tissues was also studied.

Thermal stability of alcohol dehydrogenase enzyme determined by activity assay and calorimetry

1998 ◽  
Vol 309 (1-2) ◽  
pp. 193-196 ◽  
Author(s):  
Sunil Nath ◽  
Gyana R. Satpathy ◽  
Rahul Mantri ◽  
Shashank Deep ◽  
Jagdish C. Ahluwalia
Keyword(s):  
Thermal Stability ◽  
Alcohol Dehydrogenase ◽  
Activity Assay ◽  
Dehydrogenase Enzyme ◽  
Thermal Stability Of ◽  
And Calorimetry
Sign in / Sign up

Export Citation Format

Share Document