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.

Immobilization of lipase in hierarchically ordered macroporous/mesoporous silica with improved catalytic performance
Publication date: Available online 19 May 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Yanjun Jiang, Pengju Zheng, Liya Zhou, Weixi Kong, Jing Gao, Jinxia Wang, Jinyan Gu, Xu Zhang, Xiaomei Wang Hierarchically ordered macroporous/mesoporous silica (3DOM/m-S) material was prepared through the dual templating method with polystyrene (PS) colloidal crystals as the hard template and amphiphilic triblock copolymers (P123) as the soft template. The achieved 3DOM/m-S possesses ordered macropores of 400nm and mesopores of 5.1nm, which provides a promising platform for enzyme immobilizati...
Source: Journal of Molecular Catalysis B: Enzymatic - May 19, 2016 Category: Biochemistry Source Type: research

Cashew apple bagasse as a support for the immobilization of lipase B from Candida antarctica: Application to the chemoenzymatic production of (R)-Indanol
Publication date: Available online 16 May 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Ticiane C. de Souza, Thiago de S. Fonseca, Jessyca A. da Costa, Maria Valderez Ponte Rocha, Marcos Carlos de Mattos, Roberto Fernandez-Lafuente, Luciana R.B. Gonçalves, Jose C. S. dos Santos Lipase B from Candida antarctica lipase expressed in Aspergillus niger has been covalently immobilized on cashew apple bagasse, and it stability and performance in the chemoenzymatic synthesis of (R)-Indano has been evaluated. The cashew apple bagasse (CAB) has been treated with alkaline hydrogen peroxide an...
Source: Journal of Molecular Catalysis B: Enzymatic - May 16, 2016 Category: Biochemistry Source Type: research

Enzymatic deglycosylation of flavonoids in deep eutectic solvents − aqueous mixtures: Paving the way for sustainable flavonoid chemistry
Publication date: Available online 13 May 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Gisela Weiz, Lucas Braun, Rosana Lopez, Pablo Domínguez de María, Javier D. Breccia The low solubility of glycosylated flavonoids represents a hurdle to conduct efficient enzymatic deglycosylations in aqueous media. To overcome this drawback, environmentally-unfriendly dimethylsulfoxide (DMSO) is typically used as co-solvent. Using a specific diglycosidase from Acremonium sp. DSM24697 for the deglycosylation of the rutinosylated flavonoid (hesperidin) as model reaction, this communication explores th...
Source: Journal of Molecular Catalysis B: Enzymatic - May 13, 2016 Category: Biochemistry Source Type: research

Covalent immobilization of Candida methylica formate dehydrogenase on short spacer arm aldehyde group containing supports
In this study, three different aldehyde group containing supports, such as glyoxyl silica, glyoxyl agarose and aldehyde-functionalized Immobead 150 were evaluated for the covalent immobilization of formate dehydrogenase from Candida methylica. The immobilization−activity yields were determined as 75−68%, 60−84%, and 90−132%, respectively for glyoxyl silica, glyoxyl agarose and aldehyde-functionalized Immobead 150 supports for formate oxidation. The formate production activity of Candida methylica formate dehydrohenase was tested for different initial bicarbonate concentrations; however, no product was determined. T...
Source: Journal of Molecular Catalysis B: Enzymatic - May 13, 2016 Category: Biochemistry Source Type: research

Investigation of the transglycosylation potential of ß-Galactosidase from Aspergillus oryzae in the presence of the ionic liquid [Bmim][PF6]
Publication date: Available online 13 May 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Regina Brakowski, Katrin Pontius, Matthias Franzreb Finding efficient and simple methods for the synthesis of oligosaccharides is a relevant question for both pharmaceutical and food industry. An interesting route is transglycosylation by glycosidases due to their availability and cheap substrates. In this work transglycosylation by means of ß-galactosidase from Aspergillus oryzae was investigated at pH 4.5 using ONPG as glycosyl donor and several saccharides in different concentrations as acceptor. As th...
Source: Journal of Molecular Catalysis B: Enzymatic - May 13, 2016 Category: Biochemistry Source Type: research

Methods and substrates for feruloyl esterase activity detection, a review
Publication date: Available online 14 May 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Ana Mayela Ramos-de-la-Peña, Juan Carlos Contreras-Esquivel Ferulic acid esterases (FAEs) are enzymes with high potential in biochemistry and biotechnology due to its role in the hydroxycinnamic acids liberation from agro industrial waste materials. These enzymes play a key role in the non woody plants delignification, in the saccharification processes, in the increase of waste products digestibility and in the esterification of hydroxycinnamic acids. Because of this, different industries have focused their...
Source: Journal of Molecular Catalysis B: Enzymatic - May 13, 2016 Category: Biochemistry Source Type: research

Improving enantioselectivity of lipase from Candida rugosa by carrier-bound and carrier-free immobilization
Publication date: Available online 12 May 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Susana Velasco-Lozano, Fernando López-Gallego, Javier Rocha-Martin, José Manuel Guisán, Ernesto Favela-Torres The enantioselectivity of carrier-bound and carrier-free immobilized lipase from Candida rugosa (CRL) was studied. CRL was immobilized in six agarose-based carriers functionalized with different reactive groups and in two different CRL cross-linked aggregates. Both, activity and enantioselectivity of all the immobilized lipase preparations were evaluated with different racemic esters under d...
Source: Journal of Molecular Catalysis B: Enzymatic - May 12, 2016 Category: Biochemistry Source Type: research

Biosynthesis of oleyl oleate in solvent-free system by Candida rugosa Lipase (CRL) immobilized in macroporous resin with cross-linking of aldehyde-dextran
Publication date: Available online 10 May 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Yicheng Bi, Min Yu, Haiyan Zhou, Hua Zhou, Ping Wei In our study, oleyl oleate was synthesized through enzymatic esterification of oleic acid with oleyl alcohol using Candida rugosa lipase (CRL) immobilized on macroporous resin in a solvent-free system. CRL was immobilized flexibly on the support via aldehyde-dextran, and the effectiveness of aldehyde-dextrans, as cross-linking agents with different molecular weights, was compared and discussed. The impact of various factors, such as different molecula...
Source: Journal of Molecular Catalysis B: Enzymatic - May 10, 2016 Category: Biochemistry Source Type: research

Microbial transformation of Pseudoprotodioscin by Chaetomium olivaceum
Publication date: Available online 10 May 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Xinran Dong, Zhaohui Gao, Hongxiu Hu, Ranran Gao, Dian Sun Pseudoprotodioscin (1) is a steroidal saponin from plants with diverse biological activities. In order to obtain new and useful derivatives for further study, Chaetomium olivaceum was used to transform pseudoprotodioscin. Five new (4, 5, 6, 8, and 9) and three known (2, 3 and 7) steroidal saponins were obtained in this study. These reactions were hard to be achieved through chemical modification. The structures of these metabolites were elucida...
Source: Journal of Molecular Catalysis B: Enzymatic - May 10, 2016 Category: Biochemistry Source Type: research

Efficient enzymatic preparation of Esculentoside B following condition optimization by response surface methodology
This study aims to provide a practical method for highly efficient preparation of EsB using esculentoside A (EsA, phytolaccagenin 3-O-β-D-glucopyranosyl (1→4)-β-D-xylopyranoside) as the starting material. β-D-glucosidase from snailase was used to catalyze the formation of EsB, and the product was then purified and fully characterized by both HRMS and NMR. To prepare EsB in a more cost-effective way, response surface methodology (RSM) was used to explore the potential effects of the reaction conditions (such as reaction temperature, pH, enzyme load, and reaction time) on the conversion rates of EsA. The highest EsB yie...
Source: Journal of Molecular Catalysis B: Enzymatic - May 9, 2016 Category: Biochemistry Source Type: research

Biochemical characterization of an azoreductase from Rhodococcus opacus 1CP possessing methyl red degradation ability
Publication date: Available online 2 May 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Jingxian Qi, Michael Schlömann, Dirk Tischler Azo dyes, characterized by one or more R1 NN-R2 bonds, could be enzymatically metabolized. A flavin-containing oxygen-insensitive azoreductase designated as AzoRo (25 KDa) from strain Rhodococcus opacus 1CP was identified and catalyses the initial degradation step of azo dyes. Protein sequence of AzoRo shared best identity of 33% to PaAzo1 from Pseudomonas aeruginosa for which the structure was solved, but clearly forms an own branch in the dendrogram. Thus Azo...
Source: Journal of Molecular Catalysis B: Enzymatic - May 2, 2016 Category: Biochemistry Source Type: research

Gene cloning, expression and characterization of a novel cold-adapted protease from Planococcus sp.
Publication date: Available online 30 April 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Huitu Zhang, Huiyan Mu, Qingshan Mo, Tongwei Sun, Yang Liu, Mingyu Xu, Haikuan Wang, Yujie Dai, Fuping Lu A psychrophilic bacterium strain named M7 was isolated from the deep-sea mud of Eastern Indian Ocean and identified as Planococcus sp. A novel protease gene, cpls8, was cloned from the newly isolated bacterium and successfully expressed in Escherchia coli. The open reading frame of cpls8 gene encodes a 329-amino acid polypeptide with a molecular weight of approximately 35.6kDa. Sequence a...
Source: Journal of Molecular Catalysis B: Enzymatic - April 29, 2016 Category: Biochemistry Source Type: research

Identification and characterization of a novel Old Yellow Enzyme from Bacillus subtilis str.168
Publication date: Available online 27 April 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Xiqian Sheng, Ming Yan, Lin Xu, Miao Wei We identified and characterized YqiG, a novel Old Yellow Enzyme (OYE) from Bacillus subtilis str.168, as a member of the “thermophilic-like” subfamily. It is most related to XenA from Pseudomonas putida, with 37.9% identity, but it exhibits certain differences in sequence and enzyme properties. The YqiG can reduce various activated alkenes and exhibits high temperature (60°C for 12h) and pH stability (pH 4.0 and 9.0 for 12h), which indicates that it has a g...
Source: Journal of Molecular Catalysis B: Enzymatic - April 27, 2016 Category: Biochemistry Source Type: research

Purification, characterization, and molecular cloning of the xylanase from Streptomyces thermovulgaris TISTR1948 and its application to xylooligosaccharide production
Publication date: Available online 23 April 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Pinpanit Boonchuay, Shinji Takenaka, Ampin Kuntiya, Charin Techapun, Noppol Leksawasdi, Phisit Seesuriyachan, Thanongsak Chaiyaso A crude xylanase preparation from Streptomyces thermovulgaris TISTR1948 was able to hydrolyze KOH-treated corncob and to produce bioactive xylooligosaccharides (XOs). A thermostable cellulase-free endo-xylanase from strain TISTR1948 was purified 15.0-fold from the crude preparation, with a recovery yield of 13.0%. On SDS-PAGE, the purified enzyme had an apparent molecu...
Source: Journal of Molecular Catalysis B: Enzymatic - April 23, 2016 Category: Biochemistry Source Type: research

Production of cinnamoyl lipids using immobilized Proteus vulgaris K80 lipase and an evaluation of their antioxidant activity
In this study, ethyl cinnmate (40mM) and triolein (240mM) were used as substrates and immobilized Proteus vulgaris K80 lipase (1U) was used as enzyme catalyst. When the interesterification reaction was performed in 5mL n-hexame/toluene (85:15, v/v) at 35°C for 72h, cinnamoyl monooleyl glycerol (CMOG) and cinnamoyl dioleyl glycerol (CDOG) were produced and the conversion yield was 70%. These cinnamoylated lipid products were collected by preparative liquid chromatography and identified using high resonance mass spectrometry. CMOG and CDOG showed radical scavenging activities of 45% and 69%, respectively, in n-hexane system...
Source: Journal of Molecular Catalysis B: Enzymatic - April 22, 2016 Category: Biochemistry Source Type: research