Results 111 to 120 of about 1,091 (160)

Hyperactivation of Rhizomucor miehei lipase by hydrophobic xerogels

Biotechnology and Bioengineering, 2004
AbstractAlthough a variety of approaches exist for the immobilization of enzymes, the “science” of enzyme immobilization is still in its infancy. In recent years, considerable interest has developed regarding the use of xerogels for enzyme immobilization.
Marc G, Aucoin, Frank A, Erhardt, Raymond L, Legge   +2 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, Shaowei Huang, Zhiyuan Wang, Junying Fu, Pengmei Lv, Changlin Miao, Tao Liu, Lingmei Yang, Wen Luo   +8 more
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Preservation of rennet producing Rhizomucor miehei strain

Biotechnology Techniques, 1994
Different methods are compared for the preservation of a Rhizomucor miehei strain used for the production of rennet, which is used in the dairy industry. The best method was found to be preservation under mineral oil, After 2 years of storage, R. miehei kept its original milk clotting activity, had a lowered non-specific proteolytic activity and ...
J. Blatnik, N. Gunde-Cimerman, A. Cimerman   +2 more
openaire   +1 more source

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, Rong Bai, Na Wu, Yumin Zhang, Lili Hu   +4 more
openaire   +2 more sources

Activity and stability of a Rhizomucor miehei lipase in hydrophobic media

Biotechnology and Applied Biochemistry, 1997
The 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, R C, Martins, W L, Rocha, A P, Dias   +3 more
openaire   +2 more sources

Characterization of a β-glucosidase with transgalactosylation capacity from the zygomycete Rhizomucor miehei [PDF]

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, Bencsik Ottó, Papp Tamás, Vágvölgyi Csaba, Takó Miklós   +4 more
openaire   +3 more sources

Crystal Structure of The Rhizomucor miehei Aspartic Proteinase

1998
The composition of milk has been reviewed by Jenness (1). It is an extremely complex mixture of components, consisting of water, lipids, carbohydrates, proteins, salts and many miscellaneous compounds. The largest component is water. The lipids are 98% triglycerides, mostly as globules. Carbohydrate is mainly as lactose.
J W, Quail, J, Yang, P, Schneider, Z, Jia   +3 more
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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., Toxvaerd, Søren, Andersen, Kim Vilbour, Svendsen, A.   +3 more
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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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Modeling of solvent effects in the activation of the lipase from Rhizomucor miehei

Bioorganic & Medicinal Chemistry Letters, 1996
the 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, BERTI, FEDERICO, LINDA, PAOLO, S. MIERTUS, SABOT, ANDREA   +4 more
openaire   +2 more sources