Journal of Molecular Catalysis B: Enzymatic 
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This is an RSS file. You can use it to subscribe to this data in your favourite RSS reader or to display this data on your own website or blog.High overexpression of dye decolorizing peroxidase TfuDyP leads to the incorporation of heme precursor protoporphyrin IX
Publication date: Available online 30 August 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Dana I. Colpa, Marco W. Fraaije The heterologous overexpression level of the bacterial dye decolorizing peroxidase TfuDyP in Escherichia coli was increased sixty fold to approximately 200mg of purified enzyme per liter culture broth by fusing the enzyme to the small ubiquitin-related modifier protein (SUMO). The highly overexpressed SUMO-TfuDyP was, however, almost inactive. Analysis of the enzyme by UV–vis absorption spectroscopy and high-resolution mass spectrometry showed that a large fraction of the hig...
Source: Journal of Molecular Catalysis B: Enzymatic - August 30, 2016 Category: Biochemistry Source Type: research
Kinetic-mechanistic studies of P. cepacia lipase catalyzed corona charge selective micelle degradation
Publication date: Available online 29 August 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Xiaobo Zhu, Michael Fryd, Carlos Barrero, Salim Merali, Chiara Fecchio, Ann M. Valentine, Bradford B. Wayland The polyester cores of micelles that self-assemble from poly(caprolactone)-poly(ethylene oxide) block copolymers (HO-PCL-b-PEO-X) are substrates for P. cepacia lipase-catalyzed hydrolytic degradation. The charge on the micelle corona can be modified by varying the PEO end group (X) with neutral (-CH2CHCH2, −OMe), positively charged (-NH3 +), or negatively charged (-CO2 −,-SO3 −) groups. The...
Source: Journal of Molecular Catalysis B: Enzymatic - August 29, 2016 Category: Biochemistry Source Type: research
Identification and characterization of a FAD-dependent putrescine N-hydroxylase (GorA) from Gordonia rubripertincta CWB2
Publication date: Available online 28 August 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Catherine O. Esuola, Olubukola O. Babalola, Thomas Heine, Ringo Schwabe, Micheal Schlömann, Dirk Tischler A putrescine N-hydroxylase from Gordonia rubripertincta CWB2 (GorA), a microbial N-hydroxylating monooxygenase (NMO), specific for a range of diamines (putrescine>cadaverine>hexamethylenediamine) was identified. This NMO clustered together with some known but yet to be characterized diamine NMOs which are RhbE, from Sinorhizobium meliloti 1021; AlcA, from Bordetella bronchiseptica RB50,...
Source: Journal of Molecular Catalysis B: Enzymatic - August 28, 2016 Category: Biochemistry Source Type: research
Cyclodextrin glycosyltransferase variants experience different modes of product inhibition
Publication date: Available online 24 August 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Caiming Li, Qi Xu, Zhengbiao Gu, Shuangdi Chen, Jing Wu, Yan Hong, Li Cheng, Zhaofeng Li Cyclodextrin glycosyltransferase (CGTase) can be used for the industrial production of cyclodextrins. However, product inhibition by cyclodextrins largely restrains the cyclization activities of CGTase and severely limits the application of cyclodextrins. In this paper, the kinetic mechanisms of the three kinds of cyclization reaction were studied, and the product inhibition modes of two CGTases from different sourc...
Source: Journal of Molecular Catalysis B: Enzymatic - August 24, 2016 Category: Biochemistry Source Type: research
New developments in nucleoside analogues biosynthesis: A review
Publication date: Available online 24 August 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): María J. Lapponi, Cintia W. Rivero, María A. Zinni, Claudia N. Britos, Jorge A. Trelles The present review deals with current advances in the chemoenzymatic synthesis of biologically important nucleoside analogues (NA), either by the use of microorganisms or enzymes as biocatalysts. The interest in exploiting these biocatalysts is constantly increasing nowadays because of the advantages they have with respect to classic organic chemistry synthesis, such as a fewer number of synthesis steps, an improved c...
Source: Journal of Molecular Catalysis B: Enzymatic - August 24, 2016 Category: Biochemistry Source Type: research
Characterization of EstQE, a new member of esterase family VIII from the quizalofop-P-ethyl-degrading bacterium Ochrobactrum sp. QE-9
Publication date: Available online 23 August 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Hui Zhang, Mengya Li, Chun Dai, Guangli Wang, Minghua Xiong, Feng Li, Yuan Liu, Dayong Xu Quizalofop-P-ethyl (QE) is a selective, systemic, post-emergence aryloxyphenoxy propanoate (AOPP) herbicide for the control of annual and perennial grassy weeds in a variety of crops. An efficient QE-degrading bacterial strain, QE-9, was isolated from a QE-manufacturing facility in China and identified as Ochrobactrum sp. A 4.0kb DNA fragment from QE-9 containing a full length esterase encoding gene was cloned and ...
Source: Journal of Molecular Catalysis B: Enzymatic - August 23, 2016 Category: Biochemistry Source Type: research
Synthesis of ethyl (R)-mandelate using recombinant Carboxydothermus hydrogenoformans alcohol dehydrogenase produced by two yeast species
Publication date: Available online 20 August 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Jakub Kasprzak, Marion Rauter, Sylvia Denter, Karin Becker, Kim Baronian, Rüdiger Bode, Frieder Schauer, Michael Piontek, H.-Matthias Vorbrodt, Gotthard Kunze Yeast cell catalysts carrying a recombinant Carboxydothermus hydrogenoformans alcohol dehydrogenase (ChADH) gene were used to synthesise ethyl (R)-mandelate. Transgenic Arxula adeninivorans and Hansenula polymorpha strains were constructed to produce recombinant ChADH at high concentrations. Biochemical parameters such as pH and temperature opt...
Source: Journal of Molecular Catalysis B: Enzymatic - August 20, 2016 Category: Biochemistry Source Type: research
Immobilization of SMG1-F278N lipase onto a novel epoxy resin: Characterization and its application in synthesis of partial glycerides
In this study, a mutant lipase of SMG1 from Malassezia globosa (SMG1-F278N) was immobilized directly from crude fermentation broth onto a novel epoxy resin (ECR8285). The obtained immobilized SMG1-F278N was characterized and its application in synthesis of partial glycerides was evaluated. The immobilization was best achieved by an initial buffer pH of 6.0, an ionic strength of 1.5mol/L and a lipase/support ratio of 20mg/g. Several analytical approaches such as Scanning electron microscope (SEM) and Fourier transform infrared (FT-IR) spectroscopy showed that SMG1-F278N was successfully immobilized onto ECR8285. Besides, th...
Source: Journal of Molecular Catalysis B: Enzymatic - August 20, 2016 Category: Biochemistry Source Type: research
Two- way dynamics in β-glucosidase catalysis
Publication date: Available online 17 August 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Sneha Sawant, Sachin Bihrade, Annamma Anil, Harry Gilbert, Arvind Lali Product inhibition of β-glucosidase is considered as one of the central rate limiting steps as it starts accumulation of intermediates responsible for the slowdown of the cellulose hydrolysis. Feedback inhibitions exhibited by glucose and other oligosaccharides on the cellulose hydrolyzing enzyme reduces the rate of hydrolysis bringing the entire process to standstill. However, the exact mechanism of this catalytic slowdown is still el...
Source: Journal of Molecular Catalysis B: Enzymatic - August 17, 2016 Category: Biochemistry Source Type: research
Conjugate addition of malononitrile on chalcone: Biocatalytic CC bond formation
Publication date: November 2016 Source:Journal of Molecular Catalysis B: Enzymatic, Volume 133 Author(s): Nitesh D. Punyapreddiwar, Sangesh P. Zodape, Atul V. W.hade, Umesh R. Pratap An efficient, cost effective and environmentally friendly protocol has been developed for the Michael addition of malononitrile on 1,3-diaryl-2-propen-1-ones (Chalcones) using very cheaper, easily available natural catalyst, baker’s yeast. The whole cells of yeast excellently worked in nonaqueous medium, ethanol without decrease in catalytic activity. Graphical abstract (Source: Journal of Molecular Catalysis B: Enzymatic)
Source: Journal of Molecular Catalysis B: Enzymatic - August 16, 2016 Category: Biochemistry Source Type: research
Evaluation of different immobilized lipases in transesterification reactions using tributyrin: Advantages of the heterofunctional octyl agarose beads
Publication date: Available online 11 August 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Daniela B. Hirata, Tiago L. Albuquerque, Nazzoly Rueda, Jose J. Virgen-Ortíz, Veymar G. Tacias-Pascacio, Roberto Fernandez-Lafuente Lipases from Candida antarctica (A and B) (CALA and CALB), Candida rugosa (CRL), Thermomyces lanuginosus (TLL) and Rhizomucor miehei (RML), as well as the chimeric phospholipase Lecitase Ultra (LU) were immobilized on octyl agarose or on heterofunctional octyl supports. RML, CRL and TLL were covalently immobilized on octyl agarose beads activated with divinyl sulfone (OCDVS)...
Source: Journal of Molecular Catalysis B: Enzymatic - August 11, 2016 Category: Biochemistry Source Type: research
An overview of holocellulose-degrading enzyme immobilization for use in bioethanol production
Publication date: Available online 11 August 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Raissa Pieroni Vaz, Leonora Rios de Souza Moreira, Edivaldo Ximenes Ferreira Filho Enzymes are biocatalysts with huge potential for industry because they have specific catalytic properties, are easy to produce, and are environmentally friendly. These biocatalysts are remarkable molecules for use in the field of bioprocessing technology. However, for certain biocatalytic processes, native enzymes do not meet the requirements for large-scale application; therefore, their natural properties need to be modulated...
Source: Journal of Molecular Catalysis B: Enzymatic - August 11, 2016 Category: Biochemistry Source Type: research
Effects of different spacer arms on Cibacron Blue modification and protein affinity adsorption on magnetic microspheres
Publication date: Available online 11 August 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Dong-Hao Zhang, Na Chen, Mei-Na Yang, Yi-Fang Dou, Jie Sun, Ya-Dong Liu, Gao-Ying Zhi In order to obtain a deep insight into the effects of spacer arms on performing CB modification and dye-affinity adsorption, poly(methyl methacrylate) (PMMA) magnetic microspheres were prepared and modified respectively with poly(ethylene glycol) (PEG), poly(vinyl alcohol) (PVA) and ethylenediamine (EDA) as spacer arms. Then, an affinity dye-ligand, Cibacron Blue F3GA (CB), was coupled with these spacer arms to synthesi...
Source: Journal of Molecular Catalysis B: Enzymatic - August 11, 2016 Category: Biochemistry Source Type: research
Stability of immobilized porcine pancreas lipase on mesoporous chitosan beads: A comparative study
Publication date: Available online 11 August 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Saeedeh L. Gilani, Ghasem D. Najafpour, Aliakbar Moghadamnia, AzlinaHarun Kamaruddin Porcine pancreas lipase was immobilized on mesoporous chitosan beads. Glutaraldehyde as coupling agent was used through several immobilization techniques. With the aid of FESEM, BET and BJH analysis, the effect of glutaraldehyde on porosity of chitosan was evaluated. It was observed that the total surface area and pore volume of the carrier were significantly improved by addition of glutaraldehyde as cross-linking agent. Th...
Source: Journal of Molecular Catalysis B: Enzymatic - August 11, 2016 Category: Biochemistry Source Type: research
Conjugate addition of malononitrile on chalcone: Biocatalytic C-C bond formation
Publication date: Available online 10 August 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Nitesh D. Punyapreddiwar, Sangesh P. Zodape, Atul V. W.hade, Umesh R. Pratap An efficient, cost effective and environmentally friendly protocol has been developed for the Michael addition of malononitrile on 1,3-diaryl-2-propen-1-ones (Chalcones) using very cheaper, easily available natural catalyst, baker’s yeast. The whole cells of yeast excellently worked in nonaqueous medium, ethanol without decrease in catalytic activity. Graphical abstract (Source: Journal of Molecular Catalysis B: Enzymatic)
Source: Journal of Molecular Catalysis B: Enzymatic - August 10, 2016 Category: Biochemistry Source Type: research
