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 Supercharged Cellulase Activity and Stability in Ionic Liquids
Publication date: Available online 12 July 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Lucas B. Johnson, Sehoo Park, Lucas P. Gintner, Christopher D. Snow Ionic liquids (ILs) have many potential benefits in biochemical processes, including improved substrate or product solubility, increased enzyme selectivity, and higher yield. Varying ion substituents allow ILs to be tuned or optimized to achieve a specific goal. Unfortunately, optimization based on a single design criterion can have undesirable side effects on other process components. For example, hydrophilic ILs capable of efficiently...
Source: Journal of Molecular Catalysis B: Enzymatic - July 13, 2016 Category: Biochemistry Source Type: research

Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a
Publication date: Available online 23 June 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Nikola Lončar, Nataša Božić, Zoran Vujčić Bacterial laccases have proven advantages over fungal and plant counterparts in terms of wider pH optimum, higher stability and broader biocatalytic scope. In this work, Bacillus licheniformis ATCC 9945a laccase is produced heterologously in Escherichia coli. Produced laccase exhibits remarkably high temperature optimum at 90°C and possess significant thermostability and resistance to inactivation by organic solvents. Laccase has an apparent melting tempera...
Source: Journal of Molecular Catalysis B: Enzymatic - July 7, 2016 Category: Biochemistry Source Type: research

Purification and characterization of a high-salt-resistant microbial transglutaminase from Streptomyces mobaraensis
Publication date: Available online 7 July 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Mingfei Jin, Jinge Huang, Zhengpei Pei, Jing Huang, Hongliang Gao, Zhongyi Chang A novel microbial transglutaminase (MTG-TX) was obtained from Streptomyces mobaraensis by fermentation and purification. The enzyme was purified by ethanol precipitation via a two-step purification method, with a 44.0% yield and a specific activity of 39.2Umg−1. The purified enzyme exhibited stable performance over a range of pH 5.0–pH 10.0 and displayed maximal activity at pH 6 and 48°C. We verified through biochem...
Source: Journal of Molecular Catalysis B: Enzymatic - July 7, 2016 Category: Biochemistry Source Type: research

Characterization of a thermostable, CaCl2-activated and raw-starch hydrolyzing alpha-amylase from Bacillus licheniformis AT70: Production under solid state fermentation by utilizing agricultural wastes
Publication date: Available online 5 July 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Saideh Afrisham, Arastoo Badoei-Dalfard, Abdolhamid Namaki-Shoushtari, Zahra Karami B. licheniformis AT70 which produced a thermophilic, raw-starch degrading alpha-amylase was isolated from Gorooh hot springs in Kerman province. Maximum production of AT70 alpha-amylase was obtained in the presence of starch (as a carbon source) and ammonium chloride (as a nitrogen source) with 388 and 329U/ml enzyme yield, respectively. SSF was also carried out using various agricultural and kitchen wastes and results s...
Source: Journal of Molecular Catalysis B: Enzymatic - July 5, 2016 Category: Biochemistry Source Type: research

Biochemical characterization and gene cloning of a novel alkaline endo-1-4-glucanase from Bacillus subtilis DR8806
Publication date: Available online 5 July 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Somayeh Ramezani, Ahmad Asoodeh In the present study, an endo-1-4-glucanase was isolated from Bacillus subtilis DR8806. The enzyme was purified to homogeneity via salt precipitation and ion-exchange chromatography. SDS-PAGE analysis revealed a molecular mass of 52kDa. Optimum pH of enzyme was 9.5 and the enzyme was stable at pH range of 8.5 to 10.5. The optimum temperature of enzyme was found to be 55°C and it showed a remarkable stability at temperatures between 40–60°C. The enzyme activity was stimulat...
Source: Journal of Molecular Catalysis B: Enzymatic - July 5, 2016 Category: Biochemistry Source Type: research

Immobilization of Lipase onto Functional Cyclomatrix Polyphosphazene Microspheres
Publication date: Available online 5 July 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Chen Chen, Xue-yan Zhu, Qiao-ling Gao, Fei Fang, Li-wei Wang, Xiao-Jun Huang Functional polyphosphazene cyclomatrix microspheres (PMS) containing glucose and dodecyl moieties were utilized for physical adsorption of lipase. In this regard, Candia Rugosa lipase was immobilized onto the above microspheres through physical adsorption, which exhibited catalytic hydrolysis of glycerol triacetate as the model reaction. As observed under transmission electron microscope (TEM) and scanning electron microscop...
Source: Journal of Molecular Catalysis B: Enzymatic - July 5, 2016 Category: Biochemistry Source Type: research

Hydroxylation of flavanones by Cytochrome P450 105D7 from Streptomyces avermitilis
Publication date: Available online 4 July 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Ling Liu, Qiuping Yao, Zhongjun Ma, Haruo Ikeda, Shinya Fushinobu, Lian-Hua Xu Flavanones have a wide range of pharmacological activities. Previously, we showed that CYP105D7, a cytochrome P450, from Streptomyces avermitilis can catalyze hydroxylation of diclofenac at the C4′ position. Here, we demonstrated that CYP105D7 also catalyzes hydroxylation of two flavanones, naringenin and pinocembrin. Naringenin was hydroxylated at the 3′-position in a regiospecific manner to yield eriodictyol. Spectro...
Source: Journal of Molecular Catalysis B: Enzymatic - July 4, 2016 Category: Biochemistry Source Type: research

Cloning, Expression and Characterization of aeruginosa EGYII L-Asparaginase from Pseudomonas aeruginosa strain EGYII DSM 101801 in E.coli BL21(DE3) pLysS
Publication date: Available online 21 June 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Amany S. El-Sharkawy, Aida M. Farag, Amira M. Embaby, Hesham Saeed, Mohamed El-Shenawy Shortcomings encountered in commercial L-Asparaginases greatly restrict their therapeutic potential and hence, searching for novel L-Asparaginases has become a mandatory issue. Present work highlights cloning, expression and characterization of L-Asparaginase open reading frame (ORF) from Pseudomonas aeruginosa strain EGYII DSM 101801 in E.coli BL21 (DE3) pLysS. A DNA fragment of 984bp encoding L-Asparaginase ORF wa...
Source: Journal of Molecular Catalysis B: Enzymatic - July 3, 2016 Category: Biochemistry Source Type: research

Kinetic resolution of (R,S)-α-tetralol catalyzed by crosslinked Candida antarctica lipase B enzyme supported on mesocellular foam: a nanoscale enzyme reactor approach
Publication date: Available online 22 June 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Manoj P. Kamble, Somnath D. Shinde, Ganapati D. Yadav Nanoscale enzyme reactors (NERs) of C. antarctica lipase B (CALB) were prepared by enzyme adsorption on to mesoporous microcellular foam (MCF) followed by enzyme crosslinking within the pores. NERs effectively prevents enzyme leaching and consequently improves thermal stability. MCF has a unique pore structure that is composed of spherical 40nm sized mesocellular pores connected by 5–20nm sized mesoporous window. These smaller connecting pores preven...
Source: Journal of Molecular Catalysis B: Enzymatic - July 3, 2016 Category: Biochemistry Source Type: research

Optimization and Characterization of Lipase Catalysed Synthesis Of Xylose Caproate Ester in Organic Solvents
Publication date: Available online 23 June 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Emilia Abdulmalek, Noor Fazrieyana Hamidon, Mohd Basyaruddin Abdul Rahman The lipase catalysed synthesis of xylose caproate ester was performed by condensation of xylose, an aldopentose and caproic acid in organic solvents. A dual-solvent system containing DMSO and acetone (1:10v/v) was used to determine the optimal conditions for the reaction. Different reaction parameters (solvent system, reaction time, substrate molar ratio and the amount of enzyme loaded) were studied. The highest conversion rate (64%...
Source: Journal of Molecular Catalysis B: Enzymatic - July 3, 2016 Category: Biochemistry Source Type: research

Expression and characterization of a thermostable organic solevent-tolerant laccase from Bacillus licheniformis ATCC 9945a
Publication date: Available online 23 June 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Nikola Lončar, Nataša Božić, Zoran Vujčić Bacterial laccases have proven advantages over fungal and plant counterparts in terms of wider pH optimum, higher stability and broader biocatalytic scope. In this work, Bacillus licheniformis ATCC 9945a laccase is produced heterologously in Escherichia coli. Produced laccase exhibits remarkably high temperature optimum at 90°C and possess significant thermostability and resistance to inactivation by organic solvents. Laccase has an apparent melting tempera...
Source: Journal of Molecular Catalysis B: Enzymatic - July 3, 2016 Category: Biochemistry Source Type: research

Expression, purification, and characterization of soluble and active glutamate-specific endopeptidase in Bacillus licheniformis and Pichia pastoris
In this study, recombinant gse-bl gene with full-length sequence was firstly expressed in the bacterium B. licheniformis (GSE-BL-B) and the yeast Pichia pastoris (GSE-BL-P) in a soluble and enzymatically active form. Pure GSE-BL-B and GSE-BL-P were obtained with yields of 62.5mg/L and 78.4mg/L, respectively, after one-step His6 tag chromatography. Mature GSE-BL-B and GSE-BL-P, with similar enzymatic properties as matured GSE-BL expressed in Escherichia coli (GSE-BL-E), were obtained with yields of 50.8mg/L and 63.2mg/L after different durations of trypsin treatment. PNGase treatment and the corresponding enzymatic assay we...
Source: Journal of Molecular Catalysis B: Enzymatic - July 3, 2016 Category: Biochemistry Source Type: research

Penicillin G acylase-mediated kinetic resolution of racemic 1-(N-acylamino)alkylphosphonic and 1-(N-acylamino)alkylphosphinic acids and their esters
Publication date: Available online 25 June 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Katarzyna Zielińska, Roman Mazurkiewicz, Katarzyna Szymańska, Andrzej Jarzębski, Sylwia Magiera, Karol Erfurt Extensive studies on the penicillin G acylase-mediated kinetic resolution of N-acylated 1-aminoalkylphosphonic and 1-aminoalkylphosphinic acids as well as their esters were carried out to recognise the relationships between the substrate structure, reaction conditions, and the enzymatic hydrolytic deacylation efficiency and stereoselectivity. Reactivity of 1-(N-acylamino)alkylphosphonic a...
Source: Journal of Molecular Catalysis B: Enzymatic - July 3, 2016 Category: Biochemistry Source Type: research

Rational Immobilization of Lipase by Combining the Structure Analysis and Unnatural Amino Acid Insertion
In this study, unnatural amino acid was introduced into a recombinant lipase and applied for the rational and smart covalent enzyme immobilization. In the first step, Tyr50, 137, 243, 274, and 355 of lipase were replaced with AzPhe unnatural amino acid based on the analysis of enzyme structure. Then, these novel recombinant lipases were coupled to support using strain-promoted azide–alkyne cycloaddition (SPAAC), respectively. Subsequently, both the effect of the immobilization site and the thermo-stability of immobilized lipases were also examined. The relative activities of the immobilized AzPhe-Lip243 and AzPhe-Lip274 ...
Source: Journal of Molecular Catalysis B: Enzymatic - July 3, 2016 Category: Biochemistry Source Type: research

Enzymatic methanolysis reaction of canola oil using capillary channel reactor: Determination of the kinetic constants-involved
Publication date: Available online 29 June 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Alireza Habibi, Sepideh Fahim, Nooshin Shirvani, Masoud Rahimi Enzymatic methanolysis reaction of canola oil utilizing Candida rugosa lipase in a solvent free system was studied in a shake flask as well as capillary channel reactors. The results demonstrated that pretreatment of the enzyme with the substrate, increased the stability of the enzyme by 21.2% during the methanolysis reaction. Performance of a capillary-channel reactor improved the yield of methanolysis up to 4-fold when compared with the sh...
Source: Journal of Molecular Catalysis B: Enzymatic - July 3, 2016 Category: Biochemistry Source Type: research