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.

Predicting the optimum temperature of β-agarase based on the relative solvent accessibility of amino acids
Publication date: July 2016 Source:Journal of Molecular Catalysis B: Enzymatic, Volume 129 Author(s): Yunmeng Chu, Zhiwei Yi, Runyin Zeng, Guangya Zhang It is of great significance to investigate the amino acids in different solvent accessibility parts of β-agarase responsible for its thermal stability, which may help for understanding the structural basis of thermophilic β-agarase and developing practical strategies for reengineering new one. We systematically analyzed the amino acids distributed in the internal, intermediate and external states of β-agarases and found 21 significant differences in the thre...
Source: Journal of Molecular Catalysis B: Enzymatic - April 22, 2016 Category: Biochemistry Source Type: research

Predicting the optimum temperature of <beta>-agarase based on the relative solvent accessibility of amino acids
Publication date: Available online 11 April 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Yunmeng Chu, Zhiwei Yi, Runyin Zeng, Guangya Zhang It is of great significance to investigate the amino acids in different solvent accessibility parts of β-agarase responsible for its thermal stability, which may help for understanding the structural basis of thermophilic β-agarase and developing practical strategies for reengineering new one. We systematically analyzed the amino acids distributed in the internal, intermediate and external states of β-agarases and found 21 significant differences in...
Source: Journal of Molecular Catalysis B: Enzymatic - April 19, 2016 Category: Biochemistry Source Type: research

Enzymatic Synthesis of 3-Hydroxypropionic Acid at High Productivity by Using Free or Immobilized cells of Recombinant Escherichia coli
Publication date: Available online 14 April 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Shanshan Yu, Peiyuan Yao, Jianjiong Li, Jie Ren, Jing Yuan, Jinhui Feng, Min Wang, Qiaqing Wu, Dunming Zhu 3-Hydroxypropionic acid (3-HP) is an important platform chemical for organic synthesis and high performance polymers. Despite a wealth of reports related to 3-HP biosynthesis in microorganisms, its industrial application still requires further research because of low titer and productivity. Herein an effective enzymatic method for the synthesis of 3-HP was achieved by using free or immob...
Source: Journal of Molecular Catalysis B: Enzymatic - April 19, 2016 Category: Biochemistry Source Type: research

Sulfation made easy: a new versatile donor for enzymatic sulfation by a bacterial arylsulfotransferase
Publication date: Available online 16 April 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Aloysius F. Hartog, Ron Wever An efficient and versatile donor for the sulfation by a bacterial arylsulfotransferase of various phenolic acceptor molecules is reported. Most studies in the past used toxic p-nitrophenyl sulfate as a sulfate donor for sulfation by this enzyme. However both the donor and p-nitrophenol are difficult to remove from the sulfated products. This new donor N-hydroxysuccinimide sulfate is easy to synthesize and has the advantage that at pH values above 7 it hydrolyzes to N-hydroxysu...
Source: Journal of Molecular Catalysis B: Enzymatic - April 19, 2016 Category: Biochemistry Source Type: research

Immobilisation and kinetics of monoamine oxidase (MAO-N-D5) enzyme in polyvinyl alcohol gels
This study focused on the production and immobilisation of the crude enzyme extract of recombinant monoamine oxidase (EC 1.4.3.4), originating from Aspergillus niger (MAO-N-D5) and expressed in Escherichia coli, in PVA gel using the LentiKats® technique. MAO-Ns are important enzymes in the chemical industry due to their stereoselectivity and they are often used for the deracemisation of non-optically pure mixtures of amines. Biomass production, enzyme preparation, enzyme immobilisation, process parameters for the immobilised enzyme and characterisation of the enzyme are described in detail here. The biomass was prepared i...
Source: Journal of Molecular Catalysis B: Enzymatic - April 19, 2016 Category: Biochemistry Source Type: research

Cutinase from Fusarium oxysporum catalyzes the acylation of tyrosol in an aqueous medium: optimization and thermodynamic study of the reaction
Publication date: Available online 7 April 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Efstratios Nikolaivits, Giannis-Florjan Norra, Epaminondas Voutsas, Evangelos Topakas Recently, tyrosol has gained attention as a result of its many pharmacological properties and due to the fact that it can be isolated from cheap and abundant resources. Lipophilic tyrosyl esters, which are scarce in nature, have proven in certain cases to acquire improved biological activity compared to tyrosol itself, increasing their potential use in the food and cosmeceutical industries. The enzymatic approach for t...
Source: Journal of Molecular Catalysis B: Enzymatic - April 7, 2016 Category: Biochemistry Source Type: research

De novo construction of multi-enzyme system for one-pot deracemization of (R,S)-1-phenyl-1,2-ethanediol by stereoinversion of (S)-enantiomer to the corresponding counterpart
Publication date: Available online 7 April 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Bin Li, Yao Nie, Xiao Qing Mu, Yan Xu Deracemization via oxidoreductive stereoinversion is one of the most attractive methods for the preparation of enantiomerically pure compounds. However, available enzymatic system is yet limited for efficiently catalyzing deracemization to produce optically pure alcohol in certain configuration. Through evaluation of available stereoselective oxidoreductases on activity, selectivity, and cofactor dependency, the suitable candidates were obtained to construct the enz...
Source: Journal of Molecular Catalysis B: Enzymatic - April 7, 2016 Category: Biochemistry Source Type: research

A novel member of family 30 glycoside hydrolase subfamily 8 glucuronoxylan endo-β-1,4-xylanase (CtXynGH30) from Clostridium thermocellum orchestrates catalysis on arabinose decorated xylans
Publication date: Available online 4 April 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Anil Kumar Verma, Arun Goyal A thermophilic enzyme, CtXynGH30 from Clostridium thermocellum was identified as glucuronoxylan endo-β-1,4-xylanase displayed activity extending to arabinose decorated xylans unlike other glucuronoxylan endo-β-1,4-xylanase from family 30 sub-family 8 of glycoside hydrolase. Modular CtXynGH30 comprises N-terminal catalytic module CtXyn30A and C-terminal carbohydrate binding module of family 6, (CtCBM6). The purified CtXynGH30 displayed molecular mass of approximately, 60kDa. Ct...
Source: Journal of Molecular Catalysis B: Enzymatic - April 4, 2016 Category: Biochemistry Source Type: research

Formation of amide bond catalyzed by lipase in aqueous phase for peptide synthesis
Publication date: Available online 2 April 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Chia-Hung Kuo, Lin Jer-An, Ching-Ming Chien, Chang-Han Tsai, Yung-Chuan Liu, Chwen-Jen Shieh A dipeptide N-acetyl-L-phenylalanyl-L-tyrosinamide (N-Ac-Phe-Tyr-NH2), with angiotensin I converting enzyme (ACE) inhibitor activatity, was synthesized via porcine pancreatic lipase catalyzed amidation of N-acetyl-phenylalanine ethyl ester with L-tyrosinamide in an aqueous phase. Response surface methodology was employed to evaluate the effects of synthesis parameters. The optimum synthesis conditions obtain...
Source: Journal of Molecular Catalysis B: Enzymatic - April 2, 2016 Category: Biochemistry Source Type: research

Development of heterogeneous preparation with inulinase for tubular reactor systems
Publication date: Available online 31 March 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): M.G. Holyavka, M.P. Evstigneev, V.G. Artyukhov, V.V. Savin We developed highly stable heterogeneous preparations of inulinase immobilized on the ion-exchange matrixes and show that such preparations effectively split the chemically pure inulin and the inulin contained in plant extracts. The optimal conditions of hydrolysis are created for the migration of inulin solution from top to bottom (the downsteam flow) through the column filled by immobilized compounds extracted from Kluyveromyces marxianus and...
Source: Journal of Molecular Catalysis B: Enzymatic - March 31, 2016 Category: Biochemistry Source Type: research

Effect of deep eutectic solvent mixtures on lipase activity and stability
Publication date: Available online 30 March 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Sung Hee Kim, Saerom Park, Hyejeong Yu, Ji Hyun Kim, Hyung Joo Kim, Yung-Hun Yang, Yong Hwan Kim, Kwang Jin Kim, Eunsung Kan, Sang Hyun Lee DESs (deep eutectic solvents) have many potential applications as cosolvents or anhydrous reaction media for biocatalytic reactions, owing to their non-volatility, non-flammability, non-toxicity, biocompatibility, biodegradability, and low cost. In this work, choline chloride ([Ch]Cl)-based DESs and DES mixtures containing two hydrogen bond donors were ...
Source: Journal of Molecular Catalysis B: Enzymatic - March 30, 2016 Category: Biochemistry Source Type: research

Enhanced Catalytic Potentiality of Ganoderma lucidum IBL-05 Manganese Peroxidase Immobilized on Sol-Gel Matrix
Publication date: Available online 31 March 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Muhammad Bilal, Muhammad Asgher, Muhammad Shahid Sol-gel immobilization is an efficient approach to improve the catalytic and life-time properties of biocatalyst. A monomeric 43kDa manganese peroxidase (MnP) from Ganoderma lucidum IBL-05 was immobilized using hydrophobic sol–gel matrix of tetramethoxysilane and propyltrimethoxysilane. The method led to very effective MnP immobilization (91.0%), and imparted remarkable stability to the enzyme (82.7±0.9% after 2 months of storage at 4°C). The optimum p...
Source: Journal of Molecular Catalysis B: Enzymatic - March 30, 2016 Category: Biochemistry Source Type: research

Enantiopreference of Candida antarctica lipase B toward carboxylic acids: Substrate models and enantioselectivity thereof
Publication date: May 2016 Source:Journal of Molecular Catalysis B: Enzymatic, Volume 127 Author(s): Shau-Wei Tsai Free or immobilized Candida antarctica lipase B (CALB) is well recognized for tolerating polar organic solvents, low water activity, alkaline pH, and elevated temperature. It can exhibit a very high degree of activity and enantioselectivity for preparing optically active hydroxy and amino but not carboxylic acid compounds. Taking the current interests of preparing chiral carboxylic acids via CALB into account, this review is aimed to summarize the published articles related to the topic, and proposes com...
Source: Journal of Molecular Catalysis B: Enzymatic - March 30, 2016 Category: Biochemistry Source Type: research

Role of cyclic alkyl group in conformational instability of Tannase
Publication date: Available online 26 March 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Guangjun Nie, Rui Zhao, Wuyue Sun, Yu Gao, Xiangxiang Zhu, Zhiming Zheng, Wenjin Yue The conformational stability of enzyme has a crucial effect on its catalytic performance. The effects of six organic solvents with different structures on the conformational stability of tannase were studied using Fourier transform infrared spectroscopy in this work. This results indicated that the cyclic structure of organic solvent plays a negative role in the conformational stability of tannase. The alkyl grou...
Source: Journal of Molecular Catalysis B: Enzymatic - March 26, 2016 Category: Biochemistry Source Type: research

Homotropic allostery of nucleotidase activity of human prostatic acid phosphatase
Publication date: Available online 25 March 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Ewa Luchter-Wasylewska, Magdalena Górny, Tetyana Usachova, Valentyn Usachov The steady-state kinetics of hydrolysis of four purine ribonucleotides: 3′-AMP, 5′-AMP, 5′-GMP and 5′-IMP catalysed by human prostatic acid phosphatase (PAP; EC 3.1.3.2) in vitro was examined in this study. It has been shown for the first time that nucleotidase activity of PAP exhibits positive cooperativity, or homotropic allostery, in binding the purine ribonucleotides. Therefore, these substrates are homotropic posi...
Source: Journal of Molecular Catalysis B: Enzymatic - March 25, 2016 Category: Biochemistry Source Type: research