Solid–Liquid Equilibria for Five Binary Mixtures of Tetradecanoic Acid or Dodecanoic Acid with Three Heavy Paraffins Using DSC Measurements

2021 ◽  
Author(s):  
Jung-Chin Tsai ◽  
Shun-Zhou Bao
Keyword(s):  
Binary Mixtures ◽  
Dodecanoic Acid ◽  
Tetradecanoic Acid ◽  
Dsc Measurements ◽  
Solid Liquid

Solid-liquid phase equilibrium diagrams of binary mixtures containing fatty acids, fatty alcohol compounds and tripalmitin using differential scanning calorimetry

2019 ◽  
Vol 497 ◽  
pp. 19-32 ◽  
Author(s):  
Fernanda Paludetto Pelaquim ◽  
Flávio Cardoso de Matos ◽  
Lisandro Pavie Cardoso ◽  
Eduardo Augusto Caldas Batista ◽  
Antonio José de Almeida Meirelles ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Differential Scanning Calorimetry ◽  
Phase Equilibrium ◽  
Liquid Phase ◽  
Binary Mixtures ◽  
Fatty Alcohol ◽  
Scanning Calorimetry ◽  
Solid Liquid

Phase Diagrams of Binary Mixtures of Phenylenediamines and Dihydroxybenzenes

1977 ◽  
Vol 32 (1) ◽  
pp. 98-100
Author(s):  
M. S. Dhillon
Keyword(s):  
Phase Diagrams ◽  
Binary Mixtures ◽  
Melting Temperatures ◽  
Solid Liquid

Abstract Solid - liquid equilibria for o-phenylenediamine + resorcinol, m-phenylenediamine + pyrocatechol, + resorcinol and p-phenylenediamine + pyrocatechol, + resorcinol have been studied by the thaw-melt method. The types and melting temperatures of the complexes formed in theses mixtures were ascertained from the phase diagrams.

On the solid–liquid phase diagrams of binary mixtures of even saturated fatty alcohols: Systems exhibiting peritectic reaction

2014 ◽  
Vol 589 ◽  
pp. 137-147 ◽  
Author(s):  
Natália D.D. Carareto ◽  
Adenílson O. dos Santos ◽  
Marlus P. Rolemberg ◽  
Lisandro P. Cardoso ◽  
Mariana C. Costa ◽  
...  
Keyword(s):  
Liquid Phase ◽  
Phase Diagrams ◽  
Binary Mixtures ◽  
Peritectic Reaction ◽  
Fatty Alcohols ◽  
Solid Liquid

scholarly journals Structural insights into oxidation of medium-chain fatty acids and flavanone by myxobacterial cytochrome P450 CYP267B1

2018 ◽  
Vol 475 (17) ◽  
pp. 2801-2817 ◽  
Author(s):  
Ilona K. Jóźwik ◽  
Martin Litzenburger ◽  
Yogan Khatri ◽  
Alexander Schifrin ◽  
Marco Girhard ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Cytochrome P450 ◽  
Saturated Fatty Acids ◽  
Decanoic Acid ◽  
Dodecanoic Acid ◽  
Binding Modes ◽  
Cytochrome P450 Enzymes ◽  
Tetradecanoic Acid ◽  
Medium Chain ◽  
Pharmaceutical Industries

Oxidative biocatalytic reactions performed by cytochrome P450 enzymes (P450s) are of high interest for the chemical and pharmaceutical industries. CYP267B1 is a P450 enzyme from myxobacterium Sorangium cellulosum So ce56 displaying a broad substrate scope. In this work, a search for new substrates was performed, combined with product characterization and a structural analysis of substrate-bound complexes using X-ray crystallography and computational docking. The results demonstrate the ability of CYP267B1 to perform in-chain hydroxylations of medium-chain saturated fatty acids (decanoic acid, dodecanoic acid and tetradecanoic acid) and a regioselective hydroxylation of flavanone. The fatty acids are mono-hydroxylated at different in-chain positions, with decanoic acid displaying the highest regioselectivity towards ω-3 hydroxylation. Flavanone is preferably oxidized to 3-hydroxyflavanone. High-resolution crystal structures of CYP267B1 revealed a very spacious active site pocket, similarly to other P450s capable of converting macrocyclic compounds. The pocket becomes more constricted near to the heme and is closed off from solvent by residues of the F and G helices and the B–C loop. The crystal structure of the tetradecanoic acid-bound complex displays the fatty acid bound near to the heme, but in a nonproductive conformation. Molecular docking allowed modeling of the productive binding modes for the four investigated fatty acids and flavanone, as well as of two substrates identified in a previous study (diclofenac and ibuprofen), explaining the observed product profiles. The obtained structures of CYP267B1 thus serve as a valuable prediction tool for substrate hydroxylations by this highly versatile enzyme and will encourage future selectivity changes by rational protein engineering.

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