Results 201 to 210 of about 4,083 (211)
Some of the next articles are maybe not open access.
Activity and stability of a Rhizomucor miehei lipase in hydrophobic media
Biotechnology and Applied Biochemistry, 1997The effects of detergents and organic solvents on a commercial lipase (Lipozyme) from Rhizomucor miehei were investigated. It was shown that the detergent sodium cholate is possibly an activator of the enzyme, increasing lipase activity 2.5 times (250% of the control) when the enzyme was preincubated with 7 mM cholate.
G M, Dellamora-Ortiz +3 more
openaire +2 more sources
Molecular modelling studies of substrate binding to the lipase from Rhizomucor miehei
Journal of Computer-Aided Molecular Design, 1997Lipase enzymes have found increasingly widespread use, especially in biotransformation reactions in organic synthesis. Due to their efficiency and high enantioselectivity, they can be employed in a variety of reactions to carry out asymmetric hydrolyses, esterifications and transesterifications. However, the reasons for their stereospecificity have not
A T, Yagnik +2 more
openaire +2 more sources
Biotransformation of oleanolic and maslinic methyl esters by Rhizomucor miehei CECT 2749
Phytochemistry, 2015The pentacyclic triterpenoids methyl oleanolate, methyl maslinate, methyl 3β-hydroxyolean-9(11),12-dien-28-oate, and methyl 2α,3β-dihydroxy-12β,13β-epoxyolean-28-oate were biotransformed by Rhizomucor miehei CECT 2749. Microbial transformation of methyl oleanolate produced only a 7β,30-dihydroxylated metabolite with a conjugated 9(11),12-diene system ...
Antonio, Martinez +5 more
openaire +2 more sources
Purification and characterization of a milk clotting protease from Rhizomucor miehei
World Journal of Microbiology and Biotechnology, 1997Benzamidine, 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
Lipase from Rhizomucor miehei as an industrial biocatalyst in chemical process
Journal of Molecular Catalysis B: Enzymatic, 2010The 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
Enzymatic Synthesis of Butyl Acetate Using Rhizomucor miehei Lipase: Parametric Study.
ChemInform, 2003AbstractFor Abstract see ChemInform Abstract in Full Text.
G. Vijay Kumar, M. Narasimha Rao
openaire +1 more source
Bioresource Technology, 2012
An extracellular β-glucosidase from the zygomycete Rhizomucor miehei NRRL 5282 cultivated in a wheat bran-based solid state fermentation system was characterized. The purified enzyme exhibited an optimum temperature of 68-70 °C and pH of 5.0. It efficiently hydrolyzed oligosaccharides having β-(1→4) glycosidic linkages and exhibited some β- and α ...
Krisch Judit +4 more
openaire +3 more sources
An extracellular β-glucosidase from the zygomycete Rhizomucor miehei NRRL 5282 cultivated in a wheat bran-based solid state fermentation system was characterized. The purified enzyme exhibited an optimum temperature of 68-70 °C and pH of 5.0. It efficiently hydrolyzed oligosaccharides having β-(1→4) glycosidic linkages and exhibited some β- and α ...
Krisch Judit +4 more
openaire +3 more sources
Modeling of solvent effects in the activation of the lipase from Rhizomucor miehei
Bioorganic & Medicinal Chemistry Letters, 1996the effects of water and hydrophobic solvents on the stability of the open and closed forms of R. miehei lipase were evaluated with different solvent models. Desolvation of arginine 86 at the water-lipid interface plays a key role in the activation process, while the contribution from hydrophobic stabilization of the open form is less important.
BENEDETTI, FABIO +4 more
openaire +2 more sources
Crystallization and preliminary X-ray structure solution ofRhizomucor mieheiaspartic proteinase
Acta Crystallographica Section D Biological Crystallography, 1995Rhizomucor miehei aspartic proteinase (M(r) = 38701, 361 residues) has been crystallized in a form suitable for analysis by X-ray diffraction. The flattened rod-shaped crystals were grown from polyethylene glycol 8000 using vapour-diffusion methods.
Z, Jia +3 more
openaire +2 more sources
Rhizomucor miehei lipazının çeşitli taşıyıcılara immobilize edilmesi ve karakterizasyonu
2020openaire +1 more source