نتایج جستجو برای: thermostable enzyme

تعداد نتایج: 243447  

2017
Hong Zhu L Bruce Reynolds Rima Menassa

BACKGROUND Alpha amylase hydrolyzes α-bonds of polysaccharides such as starch and produces malto-oligosaccharides. Its starch saccharification applications make it an essential enzyme in the textile, food and brewing industries. Commercially available α-amylase is mostly produced from Bacillus or Aspergillus. A hyper-thermostable and Ca 2++ independent α-amylase from Pyrococcus furiosus (PFA) e...

Journal: :Protein engineering, design & selection : PEDS 2012
Aurimas Baranauskas Sigitas Paliksa Gediminas Alzbutas Mindaugas Vaitkevicius Judita Lubiene Virginija Letukiene Sigitas Burinskas Giedrius Sasnauskas Remigijus Skirgaila

In vitro synthesis of cDNA is one of the most important techniques in present molecular biology. Faithful synthesis of long cDNA on highly structured RNA templates requires thermostable and processive reverse transcriptases. In a recent attempt to increase the thermostability of the wt Moloney Murine leukemia virus reverse transcriptase (M-MuLV RT), we have employed the compartmentalized riboso...

2015
Kun Cheng Fei Zhang Fangfang Sun Hongge Chen Y-H Percival Zhang

Biobattery, a kind of enzymatic fuel cells, can convert organic compounds (e.g., glucose, starch) to electricity in a closed system without moving parts. Inspired by natural starch metabolism catalyzed by starch phosphorylase, isoamylase is essential to debranch alpha-1,6-glycosidic bonds of starch, yielding linear amylodextrin - the best fuel for sugar-powered biobattery. However, there is no ...

2018
Caterina Martin Amaury Ovalle Maqueo Hein J. Wijma Marco W. Fraaije

Background HMF oxidase (HMFO) from Methylovorus sp. is a recently characterized flavoprotein oxidase. HMFO is a remarkable enzyme as it is able to oxidize 5-hydroxymethylfurfural (HMF) into 2,5-furandicarboxylic acid (FDCA): a catalytic cascade of three oxidation steps. Because HMF can be formed from fructose or other sugars and FDCA is a polymer building block, this enzyme has gained interest ...

2017
Martina Aulitto Salvatore Fusco Gabriella Fiorentino Danila Limauro Emilia Pedone Simonetta Bartolucci Patrizia Contursi

BACKGROUND The genus Thermus, which has been considered for a long time as a fruitful source of biotechnological relevant enzymes, has emerged more recently as suitable host to overproduce thermozymes. Among these, α-galactosidases are widely used in several industrial bioprocesses that require high working temperatures and for which thermostable variants offer considerable advantages over thei...

Journal: :Molecular biology and evolution 2013
Scott R Miller Michele A McGuirl Darla Carvey

A long-standing question in evolutionary biology is how organisms adapt to novel environments. In North American hot springs, diversification of a clade of the cyanobacterium Synechococcus into hotter environments has resulted in the unique innovation of a light-driven ecosystem at temperatures up to 74°C, and temperature adaptation of photosynthetic carbon fixation with the Calvin cycle contri...

Journal: :Biochemical Society transactions 2007
D Rochu E Chabrière F Renault M Elias C Cléry-Barraud P Masson

While there is a consensus that human PON1 (paraoxonase-1) has a protective role, its primary biological function remains unclear. A protective role against poisoning by organophosphates [OPs (organophosphorus compounds)] drove earlier works. Clinical interest has recently focused on a protective role of PON1 against vascular diseases. PON1 resides mainly on HDL (high-density lipoprotein) parti...

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