Journal of Molecular Catalysis B: Enzymatic 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.

Characterization of a new lysine decarboxylase from Aliivibrio salmonicida for cadaverine production at alkaline pH
In this study, a new LDC from Aliivibrio salmonicida (AsLdc) was discovered, expressed, and characterized. Compared to the LDCs from Escherichia coli, LdcC and CadA, the latter was frequently used for cadaverine production, the purified AsLdc showed much higher activities at alkaline pH 7.0–8.5, for instance, 205.1U/mg at pH 7.5 with 10μg/mL enzyme, in comparison to 68.3 and 51.5U/mg for CadA and LdcC, respectively. The activities of AsLdc and CadA correlated well with the proportions of decamers at the pH range of 5.0 to 8.5. AsLdc with a melting temperature of 79°C was more thermostable than CadA (73.6°C). When used...
Source: Journal of Molecular Catalysis B: Enzymatic - November 29, 2016 Category: Biochemistry Source Type: research

Characterization of a bacterial Pyranose 2-Oxidase from Arthrobacter siccitolerans
In this study we provide the first biochemical characterization of a bacterial pyranose 2-oxidase (AsP2Ox) from Arthrobacter siccitolerans. The enzyme catalyzes the oxidation of several aldopyranoses at the C-2 position, coupling it to the reduction of dioxygen to hydrogen peroxide. Pyranose 2-oxidases belong to the glucose-methanol-choline oxidoreductase family. A structural model based on the known X-ray structure of P2Ox from Phanerochaete chrysosporium supports that AsP2Ox shares structural features with well-characterized fungal P2Oxs. The gene coding for AsP2Ox was cloned and heterologously expressed in Escherichia c...
Source: Journal of Molecular Catalysis B: Enzymatic - November 28, 2016 Category: Biochemistry Source Type: research

Reaction investigation of lactulose-producing cellobiose 2-epimerases under operational relevant conditions
In conclusion, both CEs were of comparable aptitude for industrial application under the conditions tested and most probably catalyse the same course of reaction. Graphical abstract (Source: Journal of Molecular Catalysis B: Enzymatic)
Source: Journal of Molecular Catalysis B: Enzymatic - November 26, 2016 Category: Biochemistry Source Type: research

Magnetic cellulose nanocrystals: Synthesis by electrostatic self-assembly approach and efficient use for immobilization of papain
Publication date: Available online 18 November 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Feng Zhang, Ruonan Wang, Cheng Zhen, Bin Li Novel magnetic cellulose nanocrystals (MCNCs) prepared via electrostatic self-assembly approach were used as magnetic carriers for efficient immobilization of papain and facilitated recovery of this immobilized enzyme. Zeta potential measurements, Fourier transform infrared spectroscopy and Scanning electron microscope were applied to evaluate the forming mechanism and surface structure of MCNCs. Cellulose nanocrystals (CNCs) were successfully combined with cati...
Source: Journal of Molecular Catalysis B: Enzymatic - November 22, 2016 Category: Biochemistry Source Type: research

Characterization of a thermostable arginase from Rummeliibacillus pycnus SK31.001
Publication date: Available online 22 November 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Kai Huang, Tao Zhang, Bo Jiang, Wanmeng Mu, Ming Miao L-arginase from Rummeliibacillus pycnus SK31.001 is newly discovered. A 906bp complete open reading frame, which encodes a 301 amino acid protein, was identified using degenerate PCR and inverse PCR techniques. The arginase was found to have a conserved active site with 6 amino acid residues binding to 2 manganese ions: D123, H125, D228, D230, H100 and D127. Bioinformatics analysis revealed that R. pycnus arginase is a hexamer with a subunit molecular...
Source: Journal of Molecular Catalysis B: Enzymatic - November 21, 2016 Category: Biochemistry Source Type: research

Nitrilase induction and characterization from a newly isolated Stenotrophomonas maltophilia AC21 and its application for bench scale production of nicotinic acid from 3-cyanopyridine
Publication date: Available online 21 November 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Arastoo Badoei-Dalfard, Zahra Karami, Narjes Ramezani-pour A novel bacterial named AC21 having nitrile-converting activity was gained with acetonitrile as sole source of nitrogen, which was recognized by morphology and 16S rDNA gene sequence as Stenotrophomonas maltophilia. This intracellular nitrilase induced by acetonitrile (0.3%) catalyses the conversion of 3-cyanopyridine to nicotinic acid without noticeable production of nicotinamide. Optimal pH and temperature of Nitrilase AC21 was obtained at pH 8.0...
Source: Journal of Molecular Catalysis B: Enzymatic - November 20, 2016 Category: Biochemistry Source Type: research

A Green approach towards the synthesis of chiral alcohols using functionalized alginate immobilized Saccharomyces cerevisiae cells
In this study Saccharomyces cerevisiae cells immobilized on functionalized alginate beads, catalyze the bio-reduction of prochiral ketones 1a-12a to their corresponding chiral alcohols 1b-12b in higher yields of 60-99% and.excellent optical purity 75-97%. The synthesized chiral azido alcohols 10b-12b were further subjected to hydrogenation using Palladium(Pd) nanoparticles (≤5nm), to obtain chiral amino alcohols 10c-12c of therapeutic importance. Thus, a simple, green and inexpensive continuous chemo-enzymatic process has been developed in the synthesis of chiral alcohols/amino alcohols to enhance the scope of the method...
Source: Journal of Molecular Catalysis B: Enzymatic - November 17, 2016 Category: Biochemistry Source Type: research

Magnetic cellulose nanocrystals: Sythesis by electrostatic self-assembly approach and efficent use for immobilization of papain
Publication date: Available online 18 November 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Feng Zhang, Ruonan Wang, Cheng Zhen, Bin Li Novel magnetic cellulose nanocrystals (MCNCs) prepared via electrostatic self-assembly approach were used as magnetic carriers for efficient immobilization of papain and facilitated recovery of this immobilized enzyme. Zeta potential measurements, Fourier transform infrared spectroscopy and Scanning electron microscope were applied to evaluate the forming mechanism and surface structure of MCNCs. Cellulose nanocrystals (CNCs) were successfully combined with cati...
Source: Journal of Molecular Catalysis B: Enzymatic - November 17, 2016 Category: Biochemistry Source Type: research

A Secreted Staphylococcus aureus Lipase Engineered for Enhanced Alcohol Affinity for Fatty Acid Esterification
Publication date: Available online 18 November 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Benjamin D. Saylor, John J. Love Presently the production and use of biodiesel is not cost-effective in comparison to traditional fossil fuels. Naturally occurring enzymes, such as lipases and esterases, can potentially be engineered to lower the cost of certain steps in the biodiesel synthesis process that would otherwise be more costly. However, these enzymes have evolved to perform biologically relevant functions, and not necessarily to manufacture biodiesel under commercially viable conditions. To this ...
Source: Journal of Molecular Catalysis B: Enzymatic - November 17, 2016 Category: Biochemistry Source Type: research

Efficient biosynthesis of β-alanine with a tandem reaction strategy to eliminate amide by-product in the nitrilase-catalyzed hydrolysis
Publication date: Available online 18 November 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Yanyang Tao, Peiyuan Yao, Jing Yuan, Chao Han, Jinhui Feng, Min Wang, Qiaqing Wu, Dunming Zhu An efficient biosynthesis of β-alanine from 3-aminopropionitrile at high concentration has been developed using a one-pot bienzymatic cascade of a nitrilase and an amidase. The nitrilase BjNIT3397 from Bradyrhizobium japonicum strain USDA110 catalyzes the hydrolysis of 3-aminopropionitrile to β-alanine at the concentration up to 3.0mol/L with the formation 23% of 3-aminopropanamide. In order to eliminate th...
Source: Journal of Molecular Catalysis B: Enzymatic - November 17, 2016 Category: Biochemistry Source Type: research

Green routes towards industrial textile dyeing: a laccase based approach
Publication date: Available online 16 November 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Cinzia Pezzella, Simona Giacobbe, Valerio Guido Giacobelli, Lucia Guarino, Sibel Kylic, Mehmet Sener, Giovanni Sannia, Alessandra Piscitelli Laccase-catalyzed synthesis of dye molecules represents a green choice to reduce the environmental footprint of conventional synthetic processes. Textile industry will benefit from this green technology since the synthesized dyes can be exploited to colour different fabrics. This work describes the application of the Pleurotus ostreatus POXA1b laccase in polymeri...
Source: Journal of Molecular Catalysis B: Enzymatic - November 15, 2016 Category: Biochemistry Source Type: research

Isoquercitrin production from rutin catalyzed by naringinase under ultrasound irradiation
Publication date: Available online 14 November 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Dan Zhu, An Gong, Yan Xu, Kinfack Tsabing D’assise, Fuan Wu, Jun Wang Isoquercitrin, a rare flavonol glycoside with wide biological activities and key synthetic intermediate for the production of enzymatically modified isoquercitrin (EMIQ), was conducted by naringinase-catalyzed conversion of rutin under ultrasound irradiation. The maximum yields were obtained to 98.35±3.13% and 95.20±2.52% under conventional heating and ultrasound irradiation, respectively. The optimal results under ultrasound irra...
Source: Journal of Molecular Catalysis B: Enzymatic - November 14, 2016 Category: Biochemistry Source Type: research

Conversion of a Monascus ruber esterase into a lipase by disrupting a salt bridge
This study provides a way to alter the substrate preference of the Lip10 esterase as well as new insight into the structural basis of esterase substrate specificity. Graphical abstract (Source: Journal of Molecular Catalysis B: Enzymatic)
Source: Journal of Molecular Catalysis B: Enzymatic - November 14, 2016 Category: Biochemistry Source Type: research

In-silico driven engineering of enantioselectivity of a penicillin G acylase towards active pharmaceutical ingredients
In this study, we have evaluated effects of in-silico replacements of acyl-binding subsite residue Phe24β of the enzyme from Achromobacter sp. CCM 4824 to seven markedly smaller amino acids on its enantioselectivity towards industrially relevant compounds. Models of the two most promising mutants bearing substitutions Pheβ24Ala and Pheβ24Cys were investigated using molecular docking calculations. The Cys substitution revealed much better enantioselectivity traits with a set of seven substrates. To verify the relevance of in-silico predictions, we constructed a PGA A + Phe24βCys mutant and determined its enantioselecti...
Source: Journal of Molecular Catalysis B: Enzymatic - November 14, 2016 Category: Biochemistry Source Type: research

Recycling Rhizopus oryzae resting cells as biocatalyst to prepare near eutectic palmitic-stearic acid mixtures from non-edible fat
Publication date: Available online 15 November 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Pau Gallart-Sirvent, Edinson Yara, Gemma Villorbina, Mercè Balcells, Núria Sala, Ramon Canela-Garayoa Here we studied non-edible fat waste as a starting material to prepare eutectic mixtures of biomaterials. Initially, the fat was hydrolyzed using water and R. oryzae resting cells. The hydrolysis was performed in organic solvent-free media and the degree of hydrolysis at 1h was 42% while hydrolytic values of 86% and 98% were achieved at 12 and 48h, respectively. To recover the resting cells, they were...
Source: Journal of Molecular Catalysis B: Enzymatic - November 14, 2016 Category: Biochemistry Source Type: research