53651-70-0Relevant articles and documents
Poly(3-hydroxyoctanoate) depolymerase from Pseudomonas fluorescens GK13: Catalysis of ester-forming reactions in non-aqueous media
Santos, Marta,Gangoiti, Joana,Llama, Maria J.,Serra, Juan L.,Keul, Helmut,Moeller, Martin
experimental part, p. 81 - 86 (2012/06/29)
Several industrial processes based on lipase catalysis have been established. However, since there are still a vast number of catalytic processes that lack a suitable enzyme, the discovery of new biocatalysts is required to fulfil this purpose. The potential of using the medium-chain-length (mcl)-PHA depolymerase from Pseudomonas fluorescens GK13 in anhydrous media to catalyze ester-forming reactions has been investigated and compared with that of Novozyme 435. The mcl-PHA depolymerase catalyzes the ring-opening polymerization of racemic β-butyrolactone (β-BL), l- and d-lactide (LLA, DLA) with high yield resulting in low molecular weight polymers. On the other hand, ε-caprolactone and pentadecalactone, which show high polymerizability using Novozyme 435 as catalyst, were not polymerized by mcl-PHA depolymerase. Besides, the activity of mcl-PHA depolymerase toward transesterification and esterification of ethyl-3-hydroxyoctanoate, lauric acid, (R,S)-β-BL, LLA and DLA has been studied.
Poly(3-hydroxybutyrate)-depolymerase from Pseudomonas lemoignei: Catalysis of esterifications in organic media
Kumar,Gross,Jendrossek
, p. 7800 - 7806 (2007/10/03)
Lipase catalysis in nonaqueous media is recognized as a powerful tool in organic and more recently polymer synthesis. Even though none of the currently known polyhydroxyalkanoate (PHA) depolymerases have lipase activity, they do have a catalytic center that resembles that of lipases. Motivated by the above, the potential of using the poly(3-hydroxybutyrate), PHB, depolymerase from Psuedomonas lemoignei in organic media to catalyze ester-forming reactions was investigated. The effect of different organic solvents (benzene-d6, cyclohexane-d12, and acetonitrile-d3) on the activity of the PHB-depolymerase toward propylation of L-lactide was studied. A significant difference in the catalytic rate was observed as a function of solvent polarity. The selectivity of the PHB-depolymerase (P. lemoignei) to catalyze the propylation of a series of different lactones including ε-caprolactone, δ-butyrolactone, γ-butyrolactone, and D, L, meso, and racemic lactides has been studied with the PHB-depolymerase (P. lemoignei) in organic solvents. Important differences in the reactivity of these lactones, as well as selective hydrolysis of stereochemically different linear lactic acid dimers, were observed. Moreover, the ability of the PHB-depolymerase to catalyze the solventless polymerization of ε-caprolactone and trimethylene carbonate was investigated.
A boron analog of DIOP: Synthesis and properties
Borner,Ward,Kortus,Kagan
, p. 2219 - 2228 (2007/10/02)
A rhodium complex of a boron analog of DIOP, which is a model for a tailored bimetallic catalyst possessing dual functions, is an active catalyst for hydrogenation and hydrosilylation.
