Results 131 to 140 of about 1,091 (160)
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Lipase from Rhizomucor miehei as an industrial biocatalyst in chemical process

Journal of Molecular Catalysis B: Enzymatic, 2010
The lipase from Rhizomucor miehei (formerly Mucor miehei) (RML) is a commercially available enzyme in both soluble and immobilized form with very high activity and good stability under diverse conditions (anhydrous organic solvents, supercritical fluids, etc.).
Rafael C. Rodrigues   +1 more
openaire   +1 more source

The crystal and molecular structure of the Rhizomucor miehei triacylglyceride lipase at 1.9 Å resolution

Journal of Molecular Biology, 1992
The crystal and molecular structure of a triacylglyceride lipase (EC 3.1.1.3) from the fungus Rhizomucor miehei was analyzed using X-ray single crystal diffraction data to 1.9 A resolution. The structure was refined to an R-factor of 0.169 for all available data.
Z S, Derewenda   +2 more
openaire   +2 more sources

Purification and characterization of a milk clotting protease from Rhizomucor miehei

World Journal of Microbiology and Biotechnology, 1997
Benzamidine, an inhibitor of serine proteases, was used as an affinity ligand for the purification of aspartyl protease from culture filtrate of Rhizomucor miehei. The two step purification protocol (ion-exchange and affinity chromatography) resulted in a homogenous enzyme preparation with seven-fold purification and a final recovery of 22%.
S. Preetha, R. Boopathy
openaire   +1 more source

Enhanced Activity of Rhizomucor miehei Lipase by Deglycosylation of Its Propeptide in Pichia pastoris

Current Microbiology, 2013
Many studies have demonstrated that the properties of enzymes expressed in eukaryotes can be affected by the position and extent of glycosylation on enzyme. In this study, two potential glycosylation sites (the 8th and the 58th asparagine) were identified and the effect of propeptide glycosylation on Rhizomucor miehei lipase (RML) expressed in Pichia ...
Yue, Liu, Wenping, Xie, Hongwei, Yu
openaire   +2 more sources

Rhizomucor miehei lipase as the catalyst in the resolution of chiral compounds: an overview

Chemistry and Physics of Lipids, 1998
Abstract Rhizomucor miehei lipase is probably the most used lipase obtained from fungi, even being used as a model for the determination of the structure of some other lipases due to the deep knowledge of its three dimensional structure. In this paper we present an overview of the use of this lipase for the obtention of homochiral compounds via ...
Andrés R Alcántara   +2 more
openaire   +1 more source

Identifying key electrostatic interactions in Rhizomucor miehei lipase: the influence of solvent dielectric

Theoretical Chemistry Accounts: Theory, Computation, and Modeling (Theoretica Chimica Acta), 1999
The conformational change associated with the interfacial activation of Rhizomucor miehei lipase involves the displacement of an α-helical lid (residues 82–96) away from the active site on moving from water (high dielectric) to lipid (low dielectric).
Sanna Jääskeläine   +3 more
openaire   +1 more source

Modification and simulation of Rhizomucor miehei lipase: the influence of surficial electrostatic interaction on enantioselectivity

Biotechnology Letters, 2015
Surface residues have a significant impact on the enantioselectivity of lipases. But the molecular basis of this has never been explained. In this work, transition state complexes of Rhizomucor miehei lipase (RmL) and (R)- or (S)-n-butyl 2-phenxypropinate were studied using molecular dynamics.
Gang, Xu   +5 more
openaire   +2 more sources

Enzymatic synthesis of isoamyl acetate using immobilized lipase from Rhizomucor miehei

Journal of Biotechnology, 2001
The effects of important reaction parameters for enhancing isoamyl acetate formation through lipase-catalyzed esterification of isoamyl alcohol were investigated in this study. Increase in substrate (acid) concentration led to decrease in conversions.
S, Hari Krishna   +3 more
openaire   +2 more sources

Highly thermostable xylanase purified fromRhizomucor mieheiNRL 3169

Acta Biologica Hungarica, 2011
A thermostable xylanase was purified and characterized from the thermophilic fungus Rhizomucor miehei (Cooney & Emerson) Schipper. The enzyme was purified to homogeneity by ammonium sulfate precipitation, sephadex G-100 gel filtration and diethylaminoethyl cellulose anion exchange chromatography with a 29.1-fold.
openaire   +3 more sources

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