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.

Stabilization of an Amine Transaminase for Biocatalysis
Publication date: Available online 2 December 2015 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Shan Chen, Henrik Land, Per Berglund, Maria Svedendahl Humble The amine transaminase from Chromobacterium violaceum (Cv -ATA) is a well-known enzyme to achieve chiral amines of high enantiomeric excess in laboratory scales. However, the low operational stability of Cv -ATA limits the enzyme applicability on larger scales. In order to improve the operational stability of Cv -ATA, and thereby extending its applicability, factors (additives, co-solvents, organic solvents and different temperatures) targ...
Source: Journal of Molecular Catalysis B: Enzymatic - December 4, 2015 Category: Biochemistry Source Type: research

Two-step enzymatic synthesis of tyramine from raw pyruvate fermentation broth
This study provides us with a green strategy for efficient preparation of tyramine. Graphical abstract (Source: Journal of Molecular Catalysis B: Enzymatic)
Source: Journal of Molecular Catalysis B: Enzymatic - December 4, 2015 Category: Biochemistry Source Type: research

Cheap and environmentally sustainable stereoselective arylketones reduction by Lactobacillus reuteri whole cells
Publication date: Available online 3 December 2015 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): F.M. Perna, M.A. Ricci, A. Scilimati, M.C. Mena, I. Pisano, L. Palmieri, G. Agrimi, P. Vitale Various Lactobacillus reuteri strains were investigated as whole cell catalysts for the bioreduction of acetophenone into optically active (R)-1-phenylethanol. Lactobacillus reuteri DSM 20016 strain gave an almost complete substrate conversion, in a short reaction time and enantiomeric excess up to 99%. The acetophenone bioreduction was used as a model reaction to optimize temperature and reducing eq...
Source: Journal of Molecular Catalysis B: Enzymatic - December 4, 2015 Category: Biochemistry Source Type: research

Tryptophan-surface modification of versatile peroxidase from Bjerkandera adusta enhances its catalytic performance
Publication date: Available online 3 December 2015 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Flor Sánchez-Alejandro, Karla Juarez-Moreno, Maria Camilla Baratto, Riccardo Basosi, Rafael Vazquez-Duhalt Versatile peroxidase (VP) from the fungus Bjerkandera adusta is able to transport electrons from a catalytic tryptophan residue placed in the protein surface to the activated heme prosthetic group by a long range electron transfer (LRET) process. In this work, the protein surface of VP was covalently modified with tryptophan (W-VP) in order to increase the number of catalytic sites on the pro...
Source: Journal of Molecular Catalysis B: Enzymatic - December 4, 2015 Category: Biochemistry Source Type: research

Enhancement of enzymatic synthesis of sucrose 6-acetate with Aspergillus oryzae fructosyltransferase using ionic liquid as a cosolvent
Publication date: Available online 1 December 2015 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Tao Wei, Weiwei Jia, Xuan Yu, Duobin Mao The aim of this study was to investigate the effects of using ionic liquids (ILs) as cosolvents on the enzymatic synthesis of sucrose 6-acetate (S6A) by Aspergillus oryzae fructosyltransferase (AoFT). Fifteen ILs were selected as IL-containing buffer systems to assist the catalytic reactions in the AoFT-catalyzed synthesis of S6A. An analysis of the catalytic efficiency and conformation of AoFT showed that the [Dmim][PF6]–phosphate buffer (20:80, v/v) system...
Source: Journal of Molecular Catalysis B: Enzymatic - December 2, 2015 Category: Biochemistry Source Type: research