نتایج جستجو برای: enzyme stability

تعداد نتایج: 532979  

2013
Maija L. Mehtälä Marc F. Lensink Laura P. Pietikäinen J. Kalervo Hiltunen Tuomo Glumoff

Molecular basis of D-bifunctional protein (D-BP) deficiency was studied with wild type and five disease-causing variants of 3R-hydroxyacyl-CoA dehydrogenase fragment of the human MFE-2 (multifunctional enzyme type 2) protein. Complementation analysis in vivo in yeast and in vitro enzyme kinetic and stability determinants as well as in silico stability and structural fluctuation calculations wer...

2016
Claudio Wilian Victor dos Santos Maria Elizabeth da Costa Marques Humberto de Araújo Tenório Edma Carvalho de Miranda Hugo Juarez Vieira Pereira

Trypsin from L. alexandri was purified using only two purification processes: ammonium sulfate precipitation and anion exchange liquid chromatography in DEAE-Sepharose. Trypsin mass was estimated as 24 kDa through SDS-PAGE, which showed only one band in silver staining. The purified enzyme showed an optimum temperature and pH of 50 °C and 9.0, respectively. Stability was well maintained, with h...

2017
D F Silva A F A Carvalho T Y Shinya G S Mazali R D Herculano P Oliva-Neto

The immobilization of cellulases could be an economical alternative for cost reduction of enzyme application. The derivatives obtained in the immobilization derivatives were evaluated in recycles of paper filter hydrolysis. The immobilization process showed that the enzyme recycles were influenced by the shape (drop or sheet) and type of the mixture. The enzyme was recycled 28 times for sheets ...

Journal: :Blood 1996
C E Naylor P Rowland A K Basak S Gover P J Mason J M Bautista T J Vulliamy L Luzzatto M J Adams

Human glucose 6-phosphate dehydrogenase (G6PD) has a particularly large number of variants resulting from point mutations; some 60 mutations have been sequenced to date. Many variants, some polymorphic, are associated with enzyme deficiency. Certain variants have severe clinical manifestations; for such variants, the mutant enzyme almost always displays a reduced thermal stability. A homology m...

Journal: :Catalysts 2022

The first step of the inactivation enzyme D-amino acid oxidase (DAAO) from porcine kidney at pH 5 and 7 is subunit dissociation, while FAD dissociation has not a relevant role. At 9, both phenomena affect stability. A strong effect buffer nature concentration on stability was found, mainly 9 (it possible same temperature to have fully inactivated in mM Hepes maintaining 100% glycine). depended ...

2005
JOHN M. TURNER

1. Kinetic studies of ethanolamine ammonia-lyase formation by Escherichia coli suggested that coenzyme B12 (5'-deoxyadenosylcobalamin), with ethanolamine, is a co-inducer. 2. Enzymic and immunological tests failed to show the formation of complementary enzyme components induced separately by ethanolamine and cobalamin respectively. 3. Although specific for ethanolamine as the substrate, enzyme ...

Journal: :Indian journal of experimental biology 2012
Anupama P Pathak Kshipra B Deshmukh

A bacterium producing an alkaline protease was isolated from the Lonar soda lake, Buldhana district (19 degrees 58' N; 76 degrees 31' E), Maharashtra, India. The most appropriate medium for the growth and protease production was composed of (g/L): casein 10; yeast extract 4; KH2PO4 0.5, K2HPO4 0.5 and CaCl2 0.5. The enzyme showed maximum activity with and without 5 mM Ca2+ at 70 and 60 degrees ...

Journal: :Journal of diabetes science and technology 2013
James M Harris Catherine Reyes Gabriel P Lopez

Clinical management of diabetes must overcome the challenge of in vivo glucose sensors exhibiting lifetimes of only a few days. Limited sensor life originates from compromised enzyme stability of the sensing enzyme. Sensing enzymes degrade in the presence of low molecular weight materials (LMWM) and hydrogen peroxide in vivo. Sensing enzymes could be made to withstand these degradative effects ...

Journal: :Bioscience, biotechnology, and biochemistry 2007
Ali Akbar Moosavi-Movahedi Mojtaba Amani Seyedeh Zahra Moosavi-Nejad Sedigheh Hashemnia Faizan Ahmad Giovanni Floris Anna Mura Mostafa Rezaei-Tavirani Gholam Hossein Hakimelahi Ali Akbar Saboury Reza Yousefi

The relationships between the structural and energetic domains of lentil seedling amine oxidase (LSAO) were investigated using modifiers that target the active site and the carbohydrate moiety of the enzyme. An irreversible inhibitor, aminoguanidine, specifically modified the active site of the lentil enzyme, whereas sodium metaperiodate cleaves carbohydrate moieties covalently bound to the nat...

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