Heterofunctional Magnetic Metal-Chelate-Epoxy Supports for the Purification and Covalent Immobilization of Benzoylformate Decarboxylase From Pseudomonas Putida and Its Carboligation Reactivity

Chirality ◽  
2015 ◽  
Vol 27 (9) ◽  
pp. 635-642 ◽  
Author(s):  
Servet Tural ◽  
Bilsen Tural ◽  
Ayhan S. Demir
Keyword(s):  
Pseudomonas Putida ◽  
Metal Chelate ◽  
Covalent Immobilization ◽  
Benzoylformate Decarboxylase ◽  
Magnetic Metal

Alteration of the Substrate Specificity of Benzoylformate Decarboxylase from Pseudomonas putida by Directed Evolution

ChemBioChem ◽  
2003 ◽  
Vol 4 (8) ◽  
pp. 721-726 ◽  
Author(s):  
Bettina Lingen ◽  
Doris Kolter-Jung ◽  
Pascal Dünkelmann ◽  
Ralf Feldmann ◽  
Joachim Grötzinger ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Pseudomonas Putida ◽  
Directed Evolution ◽  
Benzoylformate Decarboxylase

Fabrication of a magnetic nanoparticle embedded NH2-MIL-88B MOF hybrid for highly efficient covalent immobilization of lipase

RSC Advances ◽  
2016 ◽  
Vol 6 (71) ◽  
pp. 66385-66393 ◽  
Author(s):  
Arpita Samui ◽  
Angshuman Ray Chowdhuri ◽  
Triveni Kumar Mahto ◽  
Sumanta Kumar Sahu
Keyword(s):  
Thermal Stability ◽  
Magnetic Nanoparticle ◽  
Immobilized Lipase ◽  
Metal Organic Framework ◽  
Covalent Immobilization ◽  
Lipase Immobilization ◽  
Highly Efficient ◽  
Amine Functionalized ◽  
Magnetic Metal ◽  
Metal Organic

We demonstrate an approach to synthesize an amine-functionalized magnetic metal-organic framework (MOF) for lipase immobilization. The activity of immobilized lipase is enhanced by different parameters like pH, temperature and thermal stability.

Immobilization and characterization of benzoylformate decarboxylase from Pseudomonas putida on spherical silica carrier

2011 ◽  
Vol 34 (6) ◽  
pp. 671-680 ◽  
Author(s):  
Stephanie Peper ◽  
Selin Kara ◽  
Wei Sing Long ◽  
Andreas Liese ◽  
Bernd Niemeyer
Keyword(s):  
Pseudomonas Putida ◽  
Benzoylformate Decarboxylase ◽  
Spherical Silica

scholarly journals Identification and Characterization of a Mandelamide Hydrolase and an NAD(P)+-Dependent Benzaldehyde Dehydrogenase from Pseudomonas putida ATCC 12633

2003 ◽  
Vol 185 (8) ◽  
pp. 2451-2456 ◽  
Author(s):  
Michael J. McLeish ◽  
Malea M. Kneen ◽  
Kota N. Gopalakrishna ◽  
Carolyn W. Koo ◽  
Patricia C. Babbitt ◽  
...  
Keyword(s):  
Pseudomonas Putida ◽  
Restriction Fragment ◽  
Regulatory Protein ◽  
Open Reading Frames ◽  
Sequence Alignments ◽  
Benzoylformate Decarboxylase ◽  
Mandelate Racemase ◽  
Genes Encoding ◽  
Benzaldehyde Dehydrogenase ◽  
Reading Frames

ABSTRACT The enzymes of the mandelate metabolic pathway permit Pseudomonas putida ATCC 12633 to utilize either or both enantiomers of mandelate as the sole carbon source. The genes encoding the mandelate pathway were found to lie on a single 10.5-kb restriction fragment. Part of that fragment was shown to contain the genes coding for mandelate racemase, mandelate dehydrogenase, and benzoylformate decarboxylase arranged in an operon. Here we report the sequencing of the remainder of the restriction fragment, which revealed three further open reading frames, denoted mdlX, mdlY, and mdlD. All were transcribed in the opposite direction from the genes of the mdlABC operon. Sequence alignments suggested that the open reading frames encoded a regulatory protein (mdlX), a member of the amidase signature family (mdlY), and an NAD(P)+-dependent dehydrogenase (mdlD). The mdlY and mdlD genes were isolated and expressed in Escherichia coli, and the purified gene products were characterized as a mandelamide hydrolase and an NAD(P)+-dependent benzaldehyde dehydrogenase, respectively.

scholarly journals Reversibility of asymmetric catalyzed C–C bond formation by benzoylformate decarboxylase

2015 ◽  
Vol 5 (4) ◽  
pp. 2418-2426 ◽  
Author(s):  
Marco Berheide ◽  
Selin Kara ◽  
Andreas Liese
Keyword(s):  
Pseudomonas Putida ◽  
Kinetic Resolution ◽  
Bond Formation ◽  
Hydroxy Ketone ◽  
Benzoylformate Decarboxylase

Benzoylformate decarboxylase (BFD) fromPseudomonas putidacatalyzed the formation of 2-hydroxy-1-phenylpropanone (2-HPP), a 2-hydroxy ketone, from the kinetic resolution ofrac-benzoin in the presence of acetaldehyde.

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