Enhancing Catalytic Activity and Stability of Yeast Alcohol Dehydrogenase by Encapsulation in Chitosan-Calcium Phosphate Hybrid Beads

2015 ◽  
Vol 54 (2) ◽  
pp. 597-604 ◽  
Author(s):  
Pingping Han ◽  
Xiaokai Song ◽  
Hong Wu ◽  
Zhongyi Jiang ◽  
Jiafu Shi ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Calcium Phosphate ◽  
Alcohol Dehydrogenase ◽  
Yeast Alcohol Dehydrogenase

scholarly journals Activity and kinetics studies of yeast alcohol dehydrogenase in a reverse micelle formulated from functional surfactants

2009 ◽  
Vol 7 (4) ◽  
pp. 787-793 ◽  
Author(s):  
Yun Zhang ◽  
Xirong Huang ◽  
Guanglei Ji ◽  
Ying Li ◽  
Weifeng Liu ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Alcohol Dehydrogenase ◽  
Reverse Micelle ◽  
Catalytic Efficiency ◽  
Yeast Alcohol Dehydrogenase ◽  
Aot Reverse Micelles ◽  
Strong Electrostatic Interaction ◽  
Head Groups ◽  
Michaelis Constants ◽  
The Stability

AbstractYeast alcohol dehydrogenase (YADH) showed substantial decrease in its catalytic activity due to the strong electrostatic interaction between the head groups of sodium bis(2-ethylhexyl) sulfosuccinate (AOT) and YADH in AOT reverse micelles. However, the catalytic activity of YADH in a nonionic reverse micellar interface (GGDE/TX-100) obtained from a functional nonionic surfactant N-gluconyl glutamic acid didecyl ester (GGDE) and Triton X-100 (TX-100) was higher than that in AOT reverse micelle under the respective optimum conditions. A comparison of the kinetic parameters showed that the turnover number kcat in GGDE/TX-100 reverse micelle was 1.4 times as large as that in AOT reverse micelle, but the Michaelis constants in AOT reverse micelle for ethanol K mB was twice and for coenzyme NAD+ K mA was 5 times higher than their counterparts in GGDE/TX-100 reverse micelle. For the conversion of ethanol, the smaller K mB and larger kcat in GGDE/TX-100 reverse micelle resulted in higher catalytic efficiency kcat/K mB. The stability of YADH in GGDE/TX-100 reverse micelle was also found to be better than that in AOT reverse micelle. They were mainly attributed to the absence of electric charge on the head groups of GGDE and TX-100 in the GGDE/TX-100 reverse micelle.

scholarly journals Subunit conformation of yeast alcohol dehydrogenase.

1978 ◽  
Vol 253 (23) ◽  
pp. 8414-8419
Author(s):  
H. Jörnvall ◽  
H. Eklund ◽  
C.I. Brändén
Keyword(s):  
Alcohol Dehydrogenase ◽  
Yeast Alcohol Dehydrogenase

scholarly journals Isomerization of an enzyme-coenzyme complex in yeast alcohol dehydrogenase-catalysed reactions

2003 ◽  
Vol 68 (2) ◽  
pp. 77-84 ◽  
Author(s):  
Vladimir Leskovac ◽  
Svetlana Trivic ◽  
Draginja Pericin
Keyword(s):  
Alcohol Dehydrogenase ◽  
Rate Constants ◽  
Equilibrium Constants ◽  
Kinetic Mechanism ◽  
Yeast Alcohol Dehydrogenase ◽  
Catalyzed Reactions ◽  
The Individual ◽  
Individual Rate ◽  
Catalyzed Oxidation

In this work, all the rate constants in the kinetic mechanism of the yeast alcohol dehydrogenase-catalyzed oxidation of ethanol by NAD+, at pH 7.0, 25 ?C, have been estimated. The determination of the individual rate constants was achieved by fitting the reaction progress curves to the experimental data, using the procedures of the FITSIM and KINSIM software package of Carl Frieden. This work is the first report in the literature showing the internal equilibrium constants for the isomerization of the enzyme-NAD+ complex in yeast alcohol dehydrogenase-catalyzed reactions.

scholarly journals Binding of coenzymes to yeast alcohol dehydrogenase

2010 ◽  
Vol 75 (2) ◽  
pp. 185-194 ◽  
Author(s):  
Vladimir Leskovac ◽  
Svetlana Trivic ◽  
Draginja Pericin ◽  
Mira Popovic ◽  
Julijan Kandrac
Keyword(s):  
Alcohol Dehydrogenase ◽  
Equilibrium Constants ◽  
Point Mutations ◽  
Free Energies ◽  
Wild Type ◽  
Wild Type Enzyme ◽  
Mutant Type ◽  
Yeast Alcohol Dehydrogenase ◽  
Internal Equilibrium ◽  
Individual Reaction

In this work, the binding of coenzymes to yeast alcohol dehydrogenase (EC 1.1.1.1) were investigated. The main criterions were the change in the standard free energies for individual reaction steps, the internal equilibrium constants and the overall changes in the reaction free energies. The calculations were performed for the wild type enzyme at pH 6-9 and for 15 different mutant type enzymes, with single or double point mutations, at pH 7.3. The abundance of theoretical and experimental data enabled the binding of coenzymes to enzyme to be assessed in depth.

scholarly journals A possible connection between phosphate tungsten bronzes properties and Briggs-Rauscher oscillatory reaction response

2021 ◽  
Vol 53 (2) ◽  
pp. 223-235
Author(s):  
Tijana Maksimovic ◽  
Jelena Maksimovic ◽  
Pavle Tancic ◽  
Nebojsa Potkonjak ◽  
Zoran Nedic ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Calcium Phosphate ◽  
Active Site ◽  
Unit Cell Volume ◽  
Tungsten Bronze ◽  
Reaction Dynamics ◽  
Unit Cell ◽  
Oscillatory Reaction ◽  
Innovative Method ◽  
Cell Volumes

The calcium phosphate tungsten bronze (Ca-PWB) has been synthesized and characterized (TGA, DSC, XRPD, FTIR, SEM). The influence of solid insoluble materials Ca- PWB, as well as lithium doped (Li-PWB) and cation free phosphate tungsten (PWB) bronzes on the oscillatory Briggs-Rauscher (BR) reaction dynamics, is compared. The results show that doping with Li and Ca reduces sensitivity of the BR reaction towards bronzes addition. These findings suggest the usage of the BR reaction as an innovative method for testing of different properties of bronze material. The behavior of PWB in the BR reaction is significantly changed with divalent cation (Ca2+) doping. The reasons for the different bronzes behavior were found in their calculated unit cell volumes. Namely, the compressed Ca-PWB unit cell volume indicates the difficult availability of the active site for heterogeneous catalysis. Hence, the linear correlation (slope) of the BR oscillogram?s length (?osc) vs. mass of bronze in BR reaction might be considered as a new parameter for the evaluation of the bronzes catalytic activity.

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