Advances in the Catalytic Conversion of Biomass Components to Ester Derivatives: Challenges and Opportunities |
Autore | Licursi Domenico |
Pubbl/distr/stampa | Basel, : MDPI - Multidisciplinary Digital Publishing Institute, 2022 |
Descrizione fisica | 1 electronic resource (156 p.) |
Soggetto topico |
Research & information: general
Chemistry |
Soggetto non controllato |
eugenol
acetylation flint kaolin mesoporous aluminosilicate functionalization heterogeneous catalysis n-butyl levulinate alcoholysis butanolysis Eucalyptus nitens microwaves biorefinery diesel blends process intensification hydrolysis solvothermal process alkyl levulinate levulinic acid 5-hydroxymethylfurfural furfural humins biomass ester derivatives solvothermal processing γ-valerolactone Ni-Fe bimetallic catalysts ABE fermentation Ni-MgO-Al2O3 catalyst biofuel catalytic performance sewage scum methyl (R)-10-hydroxystearate FAMEs biodiesel estolides cardoon waste biomass bio-fuels heterogeneous catalysts combustion PEG transesterification |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Altri titoli varianti | Advances in the Catalytic Conversion of Biomass Components to Ester Derivatives |
Record Nr. | UNINA-9910576875903321 |
Licursi Domenico
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Basel, : MDPI - Multidisciplinary Digital Publishing Institute, 2022 | ||
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Lo trovi qui: Univ. Federico II | ||
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Carbohydrate-Active Enzymes : Structure, Activity and Reaction Products |
Autore | Benini Stefano |
Pubbl/distr/stampa | Basel, Switzerland, : MDPI - Multidisciplinary Digital Publishing Institute, 2020 |
Descrizione fisica | 1 electronic resource (408 p.) |
Soggetto topico |
Research & information: general
Biology, life sciences |
Soggetto non controllato |
glycoside hydrolase
xylanase carbohydrate-binding module CBM truncation halo-tolerant xylan hydrolysis pectate lyase Paenibacillus polymyxa pectins degradation Lactobacillus GH13_18 sucrose phosphorylase glycoside phosphorylase Ilumatobacter coccineus Thermoanaerobacterium thermosaccharolyticum crystallography galactosidase hydrolysis reaction mechanism complex structures cold-adapted GH2 Cellulase random mutagenesis cellulose degradation structural analysis α-amylase starch degradation biotechnology structure pyruvylation pyruvyltransferase exopolysaccharides capsular polysaccharides cell wall glycopolymers N-glycans lipopolysaccharides biosynthesis sequence space pyruvate analytics Nanopore sequencing ganoderic acid Bacillus thuringiensis biotransformation glycosyltransferase whole genome sequencing applied biocatalysis enzyme cascades chemoenzymatic synthesis sugar chemistry carbohydrate Leloir nucleotide Enzymatic glycosylation alkyl glycosides (AG)s Deep eutectic solvents (DES) Amy A alcoholysis methanol circular dichroism protein stability alpha-amylase biomass hemicellulose bioethanol xylanolytic enzyme hemicellulase lysozyme peptidoglycan cleavage avian gut GH22 crystal structure glycosylation UDP-glucose pyrophosphorylase UDP-glucose nucleotide donors Rhodococcus, Actinobacteria, gene redundancy Leloir glycosyltransferases activated sugar UTP thermophilic fungus β-glucosidases Chaetomium thermophilum protein structure fungal enzymes endo-α-(1→6)-d-mannase mannoside Mycobacterium lipomannan lipoarabinomannan phosphatidylinositol mannosides GH68 fructosyltransferase fructooligosaccharides FOS biosynthesis prebiotic oligosaccharides Arxula adeninivorans α-glucosidase maltose panose amylopectin glycogen inhibition by Tris transglycosylation glycoside hydrolyase Trichoderma harzianum complete saccharification lignocellulose N-acetylhexosamine specificity GH20 phylogenetic analysis NAG-oxazoline acceptor diversity lacto-N-triose II human milk oligosaccharides NMR molecular phylogeny α2,8-sialyltransferases polySia motifs evolution ST8Sia functional genomics |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Altri titoli varianti | Carbohydrate-Active Enzymes |
Record Nr. | UNINA-9910557134503321 |
Benini Stefano
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Basel, Switzerland, : MDPI - Multidisciplinary Digital Publishing Institute, 2020 | ||
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Lo trovi qui: Univ. Federico II | ||
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