Enzymatic Synthesis of Glucose‐ and Xylose Laurate Esters Using Different Acyl Donors, Higher Substrate Concentrations, and Membrane Assisted Solvent Recovery

2020 ◽  
pp. 2000225
Author(s):  
Marta Martinez‐Garcia ◽  
Winnie Dejonghe ◽  
Lieve Cauwenberghs ◽  
Miranda Maesen ◽  
Karolien Vanbroekhoven ◽  
...  
Keyword(s):  
Enzymatic Synthesis ◽  
Solvent Recovery ◽  
Acyl Donors ◽  
Substrate Concentrations

Enantioselective Enzymatic Synthesis of ( R )‐Phenyl Alkyl Esters and Their Analogue Amides using Fatty Acids as Green Acyl Donors.

2021 ◽  
Vol 6 (48) ◽  
pp. 13941-13946
Author(s):  
Nour ElHouda Benamara ◽  
Mounia Merabet‐Khelassi ◽  
Samia Guezane Lakoud ◽  
Louisa Aribi‐Zouioueche ◽  
Olivier Riant
Keyword(s):  
Fatty Acids ◽  
Enzymatic Synthesis ◽  
Alkyl Esters ◽  
Acyl Donors

Enzymatic synthesis of benzyl benzoate using different acyl donors: Comparison of solvent-free reaction techniques

2020 ◽  
Vol 92 ◽  
pp. 261-268
Author(s):  
Alessandra Cristina de Meneses ◽  
Manuela Balen ◽  
Elaine de Andrade Jasper ◽  
Ilka Korte ◽  
Pedro Henrique Hermes de Araújo ◽  
...  
Keyword(s):  
Enzymatic Synthesis ◽  
Solvent Free ◽  
Benzyl Benzoate ◽  
Acyl Donors ◽  
Solvent Free Reaction

Enzymatic Synthesis of Sorbitan Methacrylate According to Acyl Donors

2006 ◽  
Vol 129 (1-3) ◽  
pp. 265-277 ◽  
Author(s):  
Gwi-Taek Jeong ◽  
Hye-Jin Lee ◽  
Hae-Sung Kim ◽  
Don-Hee Park
Keyword(s):  
Enzymatic Synthesis ◽  
Acyl Donors

Enzymatic Synthesis o f Sinapoyl-L-M alate from 1-Sinapoylglucose and L-M alate by a Protein Preparation from Raphanus sativus Cotyledons

1980 ◽  
Vol 35 (9-10) ◽  
pp. 835-837 ◽  
Author(s):  
Norbert Tkotz ◽  
Dieter Strack
Keyword(s):  
Enzymatic Synthesis ◽  
Raphanus Sativus ◽  
Protein Preparation ◽  
Sugar Derivatives ◽  
Acyl Donors ◽  
First Time ◽  
Acylation Reactions

Abstract Protein preparations from cotyledons of Raphanus sativus transfer the sinapoyl moiety of 1 -sinapoylglucose to L-malate to form sinapoyl-L-malate. To our knowledge this is the first time that this type of reaction has been found to be involved in phenylpropanoid depside formation. Most acylation reactions have so far been demonstrated to depend on acyl-CoAs and only one example is known describing 1-O-acyl sugar derivatives as acyl donors.

Chromatographic Isolation of the LDH-Isoenzymes of Human Blood Platelets and an Investigation of Their Enzyme Kinetics

1968 ◽  
Vol 20 (03/04) ◽  
pp. 301-313 ◽  
Author(s):  
W Schneider ◽  
K Schumacher ◽  
B Thiede ◽  
R Gross
Keyword(s):  
Human Blood ◽  
Blood Platelets ◽  
Deae Cellulose ◽  
Order Reaction ◽  
Kinetic Properties ◽  
Ldh Isoenzymes ◽  
Kinetic Investigations ◽  
Substrate Concentrations ◽  
Chromatographic Isolation ◽  
Human Blood Platelets

SummaryThe LDH-isoenzymes of human blood platelets show a distinct predominance of the isoenzymes 2 and 3 upon chromatography on DEAE-cellulose. Small amounts of LDH-1 are also present, while only traces of LDH-4 and -5 can be detected.Enzyme kinetic investigations of the principal isoenzymes LDH-1, -2 and -3 clearly show that the differences in inhibition constants with pyruvate as substrate which are demonstrable at 25° largely disappear at 37°. On the other hand, the differences among the isoenzymes in their affinity for pyruvate and lactate as substrate as well as in with respect to the optimal substrate concentrations of pyruvate are more marked at 37° than at 25°. Also, the type of inhibition found with lactate as substrate is increasingly the expression of a higher order reaction in going from LDH-1 to LDH-3. A dependence of the LDH distribution pattern upon the metabolism of the cell is discussed. A comparison of our results with thrombocytes with those of other workers with erythrocytes and leucocytes makes it unlikely that the LDH pattern is directly dependent upon the existence of an oxidative metabolism. Rather, the redox potential of the cell could be of importance for the nature of the pattern of isoenzymes and for their differing kinetic properties.

Enzymatic Synthesis of Enantiomerically Pure Chiral Synthons: Lipase-Catalyzed Resolution of (R/S, 4E)-2-Methyl-4-hexen-l-ol

Synlett ◽  
1991 ◽  
Vol 1991 (04) ◽  
pp. 310-312
Author(s):  
Patrizia Ferraboschi ◽  
Daria Brembilla ◽  
Paride Grisenti ◽  
Enzo Santaniello
Keyword(s):  
Enzymatic Synthesis ◽  
Enantiomerically Pure

THE INFLUENCE OF ETHANOL ON THE CONVERSION OF PREGNENOLONE TO PROGESTERONE BY HUMAN PLACENTAL MICROSOMES

1974 ◽  
Vol 76 (1) ◽  
pp. 178-188 ◽  
Author(s):  
H. Lübbert ◽  
K. Pollow ◽  
R. Wagner ◽  
J. Hammerstein
Keyword(s):  
Kinetic Parameters ◽  
Enzyme Preparation ◽  
Ethanol Concentration ◽  
Hydroxysteroid Dehydrogenase ◽  
Product Formation ◽  
Linear Increase ◽  
Maximal Velocity ◽  
Microsomal Enzyme ◽  
Temperature Optima ◽  
Substrate Concentrations

ABSTRACT The effects of ethanol on kinetic parameters of placental Δ5-3β-hydroxysteroid dehydrogenase were studied. In the presence of high pregnenolone concentrations (50 μm, [S] > Km) the microsomal enzyme preparation exhibited an almost linear increase in activity as the ethanol concentration in the medium was raised from 2.5 to 15 % (v/v). At lower substrate concentrations ([S] << Km) ethanol caused inhibition. Other effects of ethanol were: linearity of product formation with time was prolonged; the maximal velocity was markedly increased; the Km for pregnenolone slightly decreased with increasing ethanol concentrations (2.5 to 10 %, v/v) whereas the Km for NAD remained the same. The pH and temperature optima of the reaction were unaffected by ethanol. Other organic solvents caused similar effects.

Sign in / Sign up

Export Citation Format

Share Document