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Dissertation
Master thesis : Anycast-based DNS in Mobile Networks
Authors: --- --- --- ---
Year: 2017 Publisher: Liège Université de Liège (ULiège)

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Abstract

Anycast offers a method for making a service IP address available to a routing system from several locations at once. It is used today to provide important services, such as naming and content delivery, in an economic, scalable, and simple to operate manner. The appeal and clear benefits of anycast to service providers have motivated a number of recent experimental studies on its potential performance impact. All studies have, to the best of our knowledge, focused on wired networks, despite the growing dominance of mobile as the most common and sometimes only form of Internet access. In this paper, we present the first study of anycast performance for mobile users. In particular, our evaluation focuses on three distinct anycast services, K- and F-Root, each providing part the DNS root zone, and Google DNS. 

Our research revolves around three axes. First, we show that mobile clients are frequently routed to suboptimal replicas in terms of latency and that this issue is not limited to specific regions or ASes of the world. Second, we find that clients are often redirected to a DNS server hosted very far away from her. This happens more frequently while on a cellular connection than on WiFi, with a significant impact on performance. Our study reveals that this is not simply an issue of not having better alternatives, and that the problem is not localised to particular geographic areas or particular ASes. We investigate root causes of this phenomenon and describe three of the major detected classes of anycast anomalies. Third and finally, we explore IP assignment dynamics of mobile clients and find that recurrent IP changes on the client side lead to significant perceived variations of anycast latency.


Book
Novel Enzyme and Whole-Cell Biocatalysts
Authors: ---
Year: 2020 Publisher: Basel, Switzerland MDPI - Multidisciplinary Digital Publishing Institute

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Abstract

The concept of a circular economy relies on waste reduction, valorization, and recycling. Global trends for “green” synthesis of chemicals have positioned the field of enzyme technology and biocatalysis (multi-enzymes and whole-cells) as an alternative for the synthesis of more social- and environmentally-responsible bio-based chemicals. Recent advances in synthetic biology, computational tools, and metabolic engineering have supported the discovery of new enzymes and the rational design of whole-cell biocatalysts. In this book, we highlight these current advances in the field of biocatalysis, with special emphasis on novel enzymes and whole-cell biocatalysts for applications in several industrial biotechnological applications.

Keywords

Technology: general issues --- 2G ethanol --- hemicellulose usage --- S. cerevisiae --- enzyme immobilization --- cell immobilization --- SHIF --- mannonate dehydratase --- mannose metabolism --- Thermoplasma acidophilum --- mannono-1,4-lactone --- 2-keto-3-deoxygluconate --- aldohexose dehydrogenase --- cyclodextrin glucanotransferases --- large-ring cyclodextrins --- semi rational mutagenesis --- carbohydrate active enzymes --- archaea --- glycosidase --- Sulfolobus solfataricus --- Saccharolobus solfataricus --- Lactobacillus --- β-galactosidase --- immobilization --- cell surface display --- LysM domains --- biocatalysis --- extremophile --- 5-hydroxymethylfurfural --- 5-hydroxymethylfuroic acid --- platform chemicals --- whole cells --- New Delhi metallo-β-lactamase --- NDM-24 --- kinetic profile --- secondary structure --- glycoside hydrolase --- thioglycosides --- Fervidobacterium --- endo-β-1,3-glucanase --- laminarinase --- thermostable --- gene duplication --- cofactor F420 --- deazaflavin --- oxidoreductase --- hydride transfer --- hydrogenation --- asymmetric synthesis --- cofactor biosynthesis --- ω-transaminase --- α-methylbenzylamine --- chiral amine --- biotransformation --- biodiesel --- waste cooking oil --- lipase immobilization --- interfacial activation --- functionalized magnetic nanoparticles --- DNase --- kinetic profiles --- RNase --- semi-rational mutagenesis --- substrate specificity --- engineered Escherichia coli --- flavonoid glucuronides --- multienzyme whole-cell biocatalyst --- organic solvents --- psychrophilic yeast --- hormone-sensitive lipase --- Glaciozyma antarctica --- Antarctica and homology modelling --- keratinase --- serine protease --- metalloprotease --- peptidase --- keratin hydrolysis --- keratin waste --- valorisation --- bioactive peptides --- ene reductase --- enzyme sourcing --- old yellow enzyme --- solvent stability --- machine learning --- flux optimization --- artificial neural network --- synthetic biology --- glycolysis --- metabolic pathways optimization --- cell-free systems --- hydrolase --- lipase --- esterase --- Bacillus subtilis lipase A --- transesterification --- organic solvent --- water activity --- immobilized lipase --- RSM --- fuel properties --- chemo-enzymatic synthesis --- glycosyl transferases --- protein engineering --- carbohydrates --- industrial enzymes --- thermostable enzymes --- glycoside hydrolases --- cell-free biocatalysis --- natural and non-natural multi-enzyme pathways --- bio-based chemicals


Book
Novel Enzyme and Whole-Cell Biocatalysts
Authors: ---
Year: 2020 Publisher: Basel, Switzerland MDPI - Multidisciplinary Digital Publishing Institute

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Abstract

The concept of a circular economy relies on waste reduction, valorization, and recycling. Global trends for “green” synthesis of chemicals have positioned the field of enzyme technology and biocatalysis (multi-enzymes and whole-cells) as an alternative for the synthesis of more social- and environmentally-responsible bio-based chemicals. Recent advances in synthetic biology, computational tools, and metabolic engineering have supported the discovery of new enzymes and the rational design of whole-cell biocatalysts. In this book, we highlight these current advances in the field of biocatalysis, with special emphasis on novel enzymes and whole-cell biocatalysts for applications in several industrial biotechnological applications.

Keywords

2G ethanol --- hemicellulose usage --- S. cerevisiae --- enzyme immobilization --- cell immobilization --- SHIF --- mannonate dehydratase --- mannose metabolism --- Thermoplasma acidophilum --- mannono-1,4-lactone --- 2-keto-3-deoxygluconate --- aldohexose dehydrogenase --- cyclodextrin glucanotransferases --- large-ring cyclodextrins --- semi rational mutagenesis --- carbohydrate active enzymes --- archaea --- glycosidase --- Sulfolobus solfataricus --- Saccharolobus solfataricus --- Lactobacillus --- β-galactosidase --- immobilization --- cell surface display --- LysM domains --- biocatalysis --- extremophile --- 5-hydroxymethylfurfural --- 5-hydroxymethylfuroic acid --- platform chemicals --- whole cells --- New Delhi metallo-β-lactamase --- NDM-24 --- kinetic profile --- secondary structure --- glycoside hydrolase --- thioglycosides --- Fervidobacterium --- endo-β-1,3-glucanase --- laminarinase --- thermostable --- gene duplication --- cofactor F420 --- deazaflavin --- oxidoreductase --- hydride transfer --- hydrogenation --- asymmetric synthesis --- cofactor biosynthesis --- ω-transaminase --- α-methylbenzylamine --- chiral amine --- biotransformation --- biodiesel --- waste cooking oil --- lipase immobilization --- interfacial activation --- functionalized magnetic nanoparticles --- DNase --- kinetic profiles --- RNase --- semi-rational mutagenesis --- substrate specificity --- engineered Escherichia coli --- flavonoid glucuronides --- multienzyme whole-cell biocatalyst --- organic solvents --- psychrophilic yeast --- hormone-sensitive lipase --- Glaciozyma antarctica --- Antarctica and homology modelling --- keratinase --- serine protease --- metalloprotease --- peptidase --- keratin hydrolysis --- keratin waste --- valorisation --- bioactive peptides --- ene reductase --- enzyme sourcing --- old yellow enzyme --- solvent stability --- machine learning --- flux optimization --- artificial neural network --- synthetic biology --- glycolysis --- metabolic pathways optimization --- cell-free systems --- hydrolase --- lipase --- esterase --- Bacillus subtilis lipase A --- transesterification --- organic solvent --- water activity --- immobilized lipase --- RSM --- fuel properties --- chemo-enzymatic synthesis --- glycosyl transferases --- protein engineering --- carbohydrates --- industrial enzymes --- thermostable enzymes --- glycoside hydrolases --- cell-free biocatalysis --- natural and non-natural multi-enzyme pathways --- bio-based chemicals


Book
Novel Enzyme and Whole-Cell Biocatalysts
Authors: ---
Year: 2020 Publisher: Basel, Switzerland MDPI - Multidisciplinary Digital Publishing Institute

Loading...
Export citation

Choose an application

Bookmark

Abstract

The concept of a circular economy relies on waste reduction, valorization, and recycling. Global trends for “green” synthesis of chemicals have positioned the field of enzyme technology and biocatalysis (multi-enzymes and whole-cells) as an alternative for the synthesis of more social- and environmentally-responsible bio-based chemicals. Recent advances in synthetic biology, computational tools, and metabolic engineering have supported the discovery of new enzymes and the rational design of whole-cell biocatalysts. In this book, we highlight these current advances in the field of biocatalysis, with special emphasis on novel enzymes and whole-cell biocatalysts for applications in several industrial biotechnological applications.

Keywords

Technology: general issues --- 2G ethanol --- hemicellulose usage --- S. cerevisiae --- enzyme immobilization --- cell immobilization --- SHIF --- mannonate dehydratase --- mannose metabolism --- Thermoplasma acidophilum --- mannono-1,4-lactone --- 2-keto-3-deoxygluconate --- aldohexose dehydrogenase --- cyclodextrin glucanotransferases --- large-ring cyclodextrins --- semi rational mutagenesis --- carbohydrate active enzymes --- archaea --- glycosidase --- Sulfolobus solfataricus --- Saccharolobus solfataricus --- Lactobacillus --- β-galactosidase --- immobilization --- cell surface display --- LysM domains --- biocatalysis --- extremophile --- 5-hydroxymethylfurfural --- 5-hydroxymethylfuroic acid --- platform chemicals --- whole cells --- New Delhi metallo-β-lactamase --- NDM-24 --- kinetic profile --- secondary structure --- glycoside hydrolase --- thioglycosides --- Fervidobacterium --- endo-β-1,3-glucanase --- laminarinase --- thermostable --- gene duplication --- cofactor F420 --- deazaflavin --- oxidoreductase --- hydride transfer --- hydrogenation --- asymmetric synthesis --- cofactor biosynthesis --- ω-transaminase --- α-methylbenzylamine --- chiral amine --- biotransformation --- biodiesel --- waste cooking oil --- lipase immobilization --- interfacial activation --- functionalized magnetic nanoparticles --- DNase --- kinetic profiles --- RNase --- semi-rational mutagenesis --- substrate specificity --- engineered Escherichia coli --- flavonoid glucuronides --- multienzyme whole-cell biocatalyst --- organic solvents --- psychrophilic yeast --- hormone-sensitive lipase --- Glaciozyma antarctica --- Antarctica and homology modelling --- keratinase --- serine protease --- metalloprotease --- peptidase --- keratin hydrolysis --- keratin waste --- valorisation --- bioactive peptides --- ene reductase --- enzyme sourcing --- old yellow enzyme --- solvent stability --- machine learning --- flux optimization --- artificial neural network --- synthetic biology --- glycolysis --- metabolic pathways optimization --- cell-free systems --- hydrolase --- lipase --- esterase --- Bacillus subtilis lipase A --- transesterification --- organic solvent --- water activity --- immobilized lipase --- RSM --- fuel properties --- chemo-enzymatic synthesis --- glycosyl transferases --- protein engineering --- carbohydrates --- industrial enzymes --- thermostable enzymes --- glycoside hydrolases --- cell-free biocatalysis --- natural and non-natural multi-enzyme pathways --- bio-based chemicals --- 2G ethanol --- hemicellulose usage --- S. cerevisiae --- enzyme immobilization --- cell immobilization --- SHIF --- mannonate dehydratase --- mannose metabolism --- Thermoplasma acidophilum --- mannono-1,4-lactone --- 2-keto-3-deoxygluconate --- aldohexose dehydrogenase --- cyclodextrin glucanotransferases --- large-ring cyclodextrins --- semi rational mutagenesis --- carbohydrate active enzymes --- archaea --- glycosidase --- Sulfolobus solfataricus --- Saccharolobus solfataricus --- Lactobacillus --- β-galactosidase --- immobilization --- cell surface display --- LysM domains --- biocatalysis --- extremophile --- 5-hydroxymethylfurfural --- 5-hydroxymethylfuroic acid --- platform chemicals --- whole cells --- New Delhi metallo-β-lactamase --- NDM-24 --- kinetic profile --- secondary structure --- glycoside hydrolase --- thioglycosides --- Fervidobacterium --- endo-β-1,3-glucanase --- laminarinase --- thermostable --- gene duplication --- cofactor F420 --- deazaflavin --- oxidoreductase --- hydride transfer --- hydrogenation --- asymmetric synthesis --- cofactor biosynthesis --- ω-transaminase --- α-methylbenzylamine --- chiral amine --- biotransformation --- biodiesel --- waste cooking oil --- lipase immobilization --- interfacial activation --- functionalized magnetic nanoparticles --- DNase --- kinetic profiles --- RNase --- semi-rational mutagenesis --- substrate specificity --- engineered Escherichia coli --- flavonoid glucuronides --- multienzyme whole-cell biocatalyst --- organic solvents --- psychrophilic yeast --- hormone-sensitive lipase --- Glaciozyma antarctica --- Antarctica and homology modelling --- keratinase --- serine protease --- metalloprotease --- peptidase --- keratin hydrolysis --- keratin waste --- valorisation --- bioactive peptides --- ene reductase --- enzyme sourcing --- old yellow enzyme --- solvent stability --- machine learning --- flux optimization --- artificial neural network --- synthetic biology --- glycolysis --- metabolic pathways optimization --- cell-free systems --- hydrolase --- lipase --- esterase --- Bacillus subtilis lipase A --- transesterification --- organic solvent --- water activity --- immobilized lipase --- RSM --- fuel properties --- chemo-enzymatic synthesis --- glycosyl transferases --- protein engineering --- carbohydrates --- industrial enzymes --- thermostable enzymes --- glycoside hydrolases --- cell-free biocatalysis --- natural and non-natural multi-enzyme pathways --- bio-based chemicals

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