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 transesterification reactions by Mucoromycotina lipases in non-aqueous media
Publication date: Available online 19 February 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Alexandra Kotogán, Anita Kecskeméti, András Szekeres, Tamás Papp, Muthusamy Chandrasekaran, Shine Kadaikunnan, Naiyf S. Alharbi, Csaba Vágvölgyi, Miklós Takó Transesterification properties of Rhizomucor, Rhizopus, Mucor, Umbelopsis and Mortierella crude lipases were investigated in water-free systems using an UV spectrophotometric method. Conversion of p-nitrophenyl palmitate (pNPP) with ethanol was characterized under various reaction conditions. Best conversion yields were genera...
Source: Journal of Molecular Catalysis B: Enzymatic - February 21, 2016 Category: Biochemistry Source Type: research

Kinetics of lipase-catalyzed de-acidification of degummed rapeseed oil utilizing monoacylglycerol as acyl-group acceptor
Publication date: Available online 20 February 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Daniela von der Haar, Gabriele Gofferjé, Andreas Stäbler, Rolf Wichmann, Thomas Herfellner Due to an increasing awareness on ecological process management the substitution of conventional processes for the de-acidification of vegetable oils has been focused by research, recently. The present study examines the mechanism of enzymatic de-acidification in degummed rapeseed oil by esterification of free fatty acids with an acyl-group acceptor (monoacylglycerol) utilizing an immobilized lipase from R...
Source: Journal of Molecular Catalysis B: Enzymatic - February 21, 2016 Category: Biochemistry Source Type: research

Synthesis, characterization and kinetic analysis of chitosan coated magnetic nanobiocatalyst and its application on glucose oleate ester synthesis
Publication date: Available online 16 February 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Manisha Jain, A.Mariya Sebatini, P. Radha, S. Kiruthika, C. Muthukumaran, K. Tamilarasan In this work, we report the covalent immobilization of lipase enzyme on the surface of chitosan coated magnetic nanoparticles (MNPs) using N-(3-dimethylaminoproyl)-N-ethylcarbodiimide (EDC) and N-hydroxysuccinimide (NHS) as coupling agents. Surface functional groups of chitosan coated MNPs, lipase enzyme, and immobilized lipase enzyme were characterized by Fourier Transform Infrared Spectroscopic (FT-IR) ana...
Source: Journal of Molecular Catalysis B: Enzymatic - February 18, 2016 Category: Biochemistry Source Type: research

Preparation and characterization of sol-gel hybrid coating films for covalent immobilization of lipase enzyme
In this study UV-curable hybrid epoxy-silica polymer films were prepared via sol–gel method. Lipase (EC 3.1.1.3) from Candida rugosa was covalently immobilized onto hybrid epoxy-silica polymer films and immobilization capacity of polymer films was found 7.22mgg−1. The morphology of the polymeric support was characterized by scanning electron microscopy (SEM) and Fourier Transform Infrared Spectroscopy (FTIR). Immobilized and free enzymes were used in two different reaction systems: hydrolysis of p-nitrophenyl palmitate in aqueous medium and synthesis of p-nitrophenyl linoleate (from p-nitrophenol and linoleic acid) in ...
Source: Journal of Molecular Catalysis B: Enzymatic - February 18, 2016 Category: Biochemistry Source Type: research

Identification and thermoadaptation engineering of thermostability conferring residue of deep sea bacterial α-amylase AMY121
Publication date: April 2016 Source:Journal of Molecular Catalysis B: Enzymatic, Volume 126 Author(s): Jian Yang, Lizhen Li, Yunzhu Xiao, Jie Li, Lijuan Long, Fazuo Wang, Si Zhang Protein engineering on hotspot residues is acknowledged as an effective way to improve the stability and activity of enzymes. Searching for the key spot of a protein is a critically important but time-consuming process. In our previous study, an InDel site neighbouring residue Lys209 of the deep sea bacterial amylase AMY121 was proposed as one putative determinant for thermostability by homology sequence comparison and biochemic...
Source: Journal of Molecular Catalysis B: Enzymatic - February 18, 2016 Category: Biochemistry Source Type: research

A new extracellular thermo-solvent-stable lipase from Burkholderia ubonensis SL-4: Identification, characterization and application for biodiesel production
Publication date: Available online 11 February 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Wenjuan Yang, Yaojia He, Li Xu, Houjin Zhang, Yunjun Yan In the present study, a new lipase SL-4 from Burkholderia ubonensis SL-4, was purified by 80% ammonium sulphate precipitation, Q Sepharose FF anion exchange and Superdex 75 gel filtration chromatography finally leading to 68.5-fold purification and 13.34% recovery. It had a molecular mass of ca. 33kDa and the whole gene (1,095-bp) was cloned by using degenerate primers. Amino acid sequence analysis revealed that lipase SL-4 is a new member o...
Source: Journal of Molecular Catalysis B: Enzymatic - February 12, 2016 Category: Biochemistry Source Type: research

Characterization of commercially available peptidases in respect of the production of protein hydrolysates with defined compositions using a three-step methodology
Publication date: Available online 12 February 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Michael Merz, Wolfgang Claaßen, Daniel Appel, Pieter Berends, Swen Rabe, Imre Blank, Timo Stressler, Lutz Fischer Enzymatic hydrolysis of food proteins is an effective way to implement a desired functionality into protein containing foods. Since these functionalities are highly dependent on the degree of hydrolysis (DH) of the hydrolysates, the enzymatic hydrolysis process must be carefully controlled. Hydrolysates with both free amino acids and long-chain peptides are usually not desirable...
Source: Journal of Molecular Catalysis B: Enzymatic - February 12, 2016 Category: Biochemistry Source Type: research

Title page/Editorial Board
Publication date: March 2016 Source:Journal of Molecular Catalysis B: Enzymatic, Volume 125 (Source: Journal of Molecular Catalysis B: Enzymatic)
Source: Journal of Molecular Catalysis B: Enzymatic - February 11, 2016 Category: Biochemistry Source Type: research

Optimisation, Purification and Characterisation of Extracellular Lipase from Botryococcus sudeticus (UTEX 2629)
Publication date: Available online 8 February 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Suh Kuan Yong, Boon Hoe Lim, Saleh Said, Lai-Hock Tey Lipases are ubiquitous esterase enzymes which have many industrial and environmental applications. Currently, bacterial and fungal lipases have been widely studied and researched for biodiesel production. However, the cost of production for those enzymes is still high and the efficiencies of the enzymes are moderate. Alternative producers need to be explored. In this paper, extracellular lipase of Botryococcus sudeticus UTEX 2629 (B. sudeticus) wa...
Source: Journal of Molecular Catalysis B: Enzymatic - February 10, 2016 Category: Biochemistry Source Type: research

Study of laccase activity and stability in the presence of ionic and non-ionic surfactants and the bioconversion of indole in laccase-TX-100 system
Publication date: Available online 8 February 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Maryam Azimi, Nastaran Nafissi-Varcheh, Mehdi Mogharabi, Mohammad Ali Faramarzi, Reza Aboofazeli The aim of this study was to characterize the stability and activity of laccase from Trametes versicolor in the presence of three different surfactants, namely sodium di-2-ethylhexylsulfosuccinate (AOT), Triton X- 100 (TX-100), and cetyltrimethylammonium bromide (CTAB). The kinetic parameters (such as K m, k cat, k cat/K m ratio, optimal pH and temperature and the thermostability of the enzyme at differ...
Source: Journal of Molecular Catalysis B: Enzymatic - February 10, 2016 Category: Biochemistry Source Type: research

Tuning lipase-catalysed kinetic resolution of 2-substituted thiophenes and furans: A scalable chemoenzymatic route to masked γ-bis-oxo-alcohols
Publication date: April 2016 Source:Journal of Molecular Catalysis B: Enzymatic, Volume 126 Author(s): Dartagnan S.P. Ferreira, Jeiely G. Ferreira, Everaldo F.S. Filho, Jefferson L. Princival The demand for greener and applicable approaches aiming at the synthesis of optically active compounds as single enantiomers has seen a significant growth worldwide. Since most of the chemically synthesized compounds are produced as racemates their kinetic resolution has been of great interest. For this purpose a number of chemo-enzymatic approaches were proposed. One of such approaches, the use of isolated lipases, is a w...
Source: Journal of Molecular Catalysis B: Enzymatic - February 10, 2016 Category: Biochemistry Source Type: research

Enzyme-catalyzed asymmetric construction of chiral tertiary alcohols via aldol reaction using proteinase
Publication date: Available online 6 February 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Rui Li, Zhi-Lin Li, Hai-Yan Zhou, Yan-Hong He, Zhi Guana A new enzyme-catalyzed asymmetric construction of chiral tertiary alcohols via asymmetric aldol reactions between β,γ-unsaturated α-keto esters and ketones was reported. Proteinase from Aspergillus melleus (AMP) was used as a sustainable biocatalyst. The best results can be obtained with yields of up to 90%, diastereoselectives of up to 93:7 dr, and enantioselectivities of up to 70% ee. This work not only expands the application of enzymat...
Source: Journal of Molecular Catalysis B: Enzymatic - February 7, 2016 Category: Biochemistry Source Type: research

Study on Lipozyme TL IM-catalyzed esterification of oleic acid and glycerol for 1,3-diolein preparation
Publication date: Available online 6 February 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Zitian Wang, Wei Du, Lingmei Dai, Dehua Liu It is well recognized that oils with a high 1,3-diacylglycerol content has the advantage of suppressing the accumulation of visceral fat and preventing the increase of body weight, and the synthesis of 1,3-diacylglycerol has attracted considerable attention. It is important to explore various methods for 1,3-diacylglycerol synthesis. In this work, the potential of using lipase Lipozyme TL IM-mediated esterification of oleic acid with glycerol for 1,3-diolei...
Source: Journal of Molecular Catalysis B: Enzymatic - February 7, 2016 Category: Biochemistry Source Type: research

Aminolysis of linoleic and salicylic acid derivatives with Candida antarctica lipase B: A solvent-free process to obtain amphiphilic amides for cosmetic application
Publication date: Available online 6 February 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Ana Maria Mouad, Delphine Taupin, Laurent Lehr, Florent Yvergnaux, André Luiz Meleiro Porto In this biotechnological process, the fatty amides (9Z,12Z)-N-dodecyloctadeca-9,12-dienamide (3) and N-dodecyl-2-hydroxybenzamide (5), respectively derived from linoleic acid and salicylic acid were synthesized through aminolysis reactions catalyzed by Candida antarctica lipase B. These amphiphilic compounds receive great attention from cosmetic industry due to a range of beneficial properties for skin. The...
Source: Journal of Molecular Catalysis B: Enzymatic - February 7, 2016 Category: Biochemistry Source Type: research

Enhancement of Glucose Isomerase activity by immobilizing on silica/chitosan hybrid microspheres
In this study, GI was immobilized on silica/chitosan hybrid microspheres via simple process through in situ encapsulation. Enhanced rate of reaction was observed when the conversion of glucose to fructose was completed in 10 mins catalyzed by immobilized GI because most GI was located on the shell of the support. Moreover, it was found that immobilized GI exhibited better pH, temperature, ions, storage and operation stability when compared to free GI. The relative enzyme activity was found to be above 90% with a wide pH range of 5.8∼8.0, temperature range of 40∼80°C, storage range of 3 months and an increase in operat...
Source: Journal of Molecular Catalysis B: Enzymatic - February 5, 2016 Category: Biochemistry Source Type: research