Results 191 to 200 of about 4,083 (211)
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Acrylamide-quenching of Rhizomucor miehei lipase

Journal of Photochemistry and Photobiology B: Biology, 2005
Steady-state and time-resolved fluorescence-quenching measurements have been performed to study multitryptophan lipase from filamentous fungus Rhizomucor miehei. Using the steady-state acrylamide fluorescence quenching data and the fluorescence-quenching-resolved-spectra (FQRS) method, the total emission spectrum of native ("closed-lid") lipase has ...
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A new β-glucosidase gene from the zygomycete fungus Rhizomucor miehei

Antonie van Leeuwenhoek, 2009
In this study, a beta-glucosidase coding gene (bgl) of the zygomycete fungus Rhizomucor miehei has been cloned and characterized. The gene comprises a total of 2,826 bp including the coding sequence of a 717 amino acids length putative protein and 10 introns dispersed in the whole coding region. The putative N-and C-terminal catalytic domains (aa 68 to
Miklós, Takó   +5 more
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Heat shock response in the thermophilic fungus Rhizomucor miehei

Microbiology, 2014
Changes in the composition of the membrane lipids and cytosol carbohydrates of the thermophilic fungus Rhizomucor miehei in response to heat shock were studied. Under optimal conditions (41–43°C), high trehalose content (8–11%) was found at all stages of growth of submerged culture.
E. A. Yanutsevich   +4 more
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Enhanced activity of Rhizomucor miehei lipase by directed saturation mutation of the propeptide

Enzyme and Microbial Technology, 2021
The propeptide is a short sequence that facilitates protein folding. In this study, four highly active Rhizomucor miehei lipase (RML) mutants were obtained through saturation mutagenesis at three propeptide positions: Ser8, Pro35, and Pro47. The enzyme activities of mutants P35 N, P47 G, P47 N, and S8E/P35S/P47A observed at 40 °C, and pH 8.0 were 10.19,
Miao Tian   +8 more
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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
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Effect of Propeptide Mutations on the Directed Evolution of Rhizomucor miehei Lipase

Protein & Peptide Letters, 2022
Background: A series of mutants of Rhizomucor miehei lipase (RML) screened through four rounds of directed evolution were studied. Mutants' triglyceride hydrolysis activity was assessed, and their genes were sequenced. Results showed that mutations in the propeptide can improve the activity of RML during evolution.
Jue Wang   +4 more
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Rhizomucor miehei Aspartic Proteinases Having Improved Properties

1998
Aspartic proteinases are widely spread in most organisms, where they carry out many different functions. The oldest and most well–known use of aspartic proteinases is as coagulants in cheese–making. The coagulants are probably still the only commercial products containing aspartic proteinases as the active substance.
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Characterization of two novel family 12 xyloglucanases from the thermophilic Rhizomucor miehei

Applied Microbiology and Biotechnology, 2013
Two novel glycoside hydrolase (GH) family 12 xyloglucanase genes (designated RmXEG12A and RmXEG12B) were cloned from the thermophilic fungus Rhizomucor miehei. Both genes contained open reading frames of 729 bp encoding 242 amino acids. Their deduced amino acid sequences shared 68% identity with each other and less than 60% with other xyloglucanases ...
Shuang, Song   +5 more
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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.
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Analysis of the Dynamics ofRhizomucor mieheiLipase at Different Temperatures

Journal of Biomolecular Structure and Dynamics, 1999
The dynamics of Rhizomucor miehei lipase has been studied by molecular dynamics simulations at temperatures ranging from 200-500K. Simulations carried out in periodic boundary conditions and using explicit water molecules were performed for 400 ps at each temperature.
Peters, Günther H.   +3 more
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