Autore: |
Trincone Antonio
|
Titolo: |
Marine Enzymes : Sources, Biochemistry and Bioprocesses for Marine Biotechnology
|
Pubblicazione: |
Basel, Switzerland, : MDPI - Multidisciplinary Digital Publishing Institute, 2020 |
Descrizione fisica: |
1 electronic resource (378 p.) |
Soggetto topico: |
Research & information: general |
|
Biology, life sciences |
Soggetto non controllato: |
metalloprotease |
|
adsorption analysis |
|
molecular docking |
|
affinity purification |
|
aminophenylboronic acid |
|
alginate degradation |
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4-deoxy-l-erythro-5-hexoseulose uronic acid (DEH) metabolism |
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Bacteroidetes |
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Proteobacteria |
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Flavobacterium |
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2-keto-3-deoxy-d-gluconate (KDG) kinase |
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2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase |
|
alginate-derived products |
|
marine enzymes |
|
biocatalysts |
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bioprocesses |
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biorefinery |
|
seafood |
|
marine biomarkers |
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collagenase |
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fermentation optimization |
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collagen |
|
Pseudoalteromonas |
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antioxidant peptides |
|
microcystin-degrading bacteria |
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mycotoxin |
|
protease |
|
esterase |
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inhibitor |
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marine agent |
|
Catenovulum |
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alkaline and cold-adapted dextranase |
|
isomaltoogligosaccharides |
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biofilm |
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dental caries |
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growing cells |
|
resting cells |
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asymmetric reduction |
|
marine fungi |
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chiral alcohols |
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alginate lyase |
|
marine bacterium |
|
Bacillus sp. Alg07 |
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purification |
|
alginate oligosaccharides |
|
Vibrio weizhoudaoensis |
|
PL7 family |
|
salt-activated enzyme |
|
Serratia marcescens |
|
polyM-specific |
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oligosaccharides |
|
Isoptericola halotolerans |
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bifunctional alginate lyase |
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α-d-galactosidase |
|
homology model |
|
GH 36 family |
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mutation |
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transglycosylation |
|
marine bacteria |
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Pseudoalteromonas sp. KMM 701 |
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leucine dehydrogenase |
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cold-adapted |
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Antarctic bacterium |
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sea-ice |
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homology modeling |
|
fucoidan |
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endo-fucoidanase |
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galactofucan |
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molecular stabilisation |
|
Sargassum mcclurei |
|
Turbinaria ornata |
|
Alteromonas |
|
deep sea |
|
cold-adapted enzyme |
|
β-galactosidase |
|
lactose-free milk |
|
chitosanases |
|
chitin deacetylase |
|
deacetylation patterns |
|
chitooligosaccharides |
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separating |
|
detecting |
|
expression |
|
deep-sea enzyme |
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pCold vector |
|
Ascophyllum nodosum |
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algal cell wall degrading enzymes |
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enzyme-assisted extraction |
|
ichip device |
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quorum quenching enzyme |
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error prone PCR |
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high-throughput screening |
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site-directed mutagenesis |
|
catalytic ability |
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Pectobacterium carotovorum subsp. carotovorum (Pcc) |
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Alginate lyase |
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Thermo-tolerant |
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pH-stability |
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Endo-manner |
|
Vibrio sp. SY01 |
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polysaccharide lyase of family 6 |
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characterization |
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degradation pattern |
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microalgae |
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enzymes |
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marine biotechnology |
|
-omics technologies |
|
heterologous expression |
|
homologous expression |
Persona (resp. second.): |
TrinconeAntonio |
Sommario/riassunto: |
This book presents contributions from scientists who are directly involved in the potential of marine enzymes as useful tools in biocatalysis; the results of enzymatic bioprospecting in gross marine environments are acknowledged, including two review articles on general enzymatic processes and microalgal enzymes. In addition, studies on structural characterizations, biological functions and aspects related to the complexity of marine enzyme-based bioprocesses are discussed. Prominent conclusions by many scientists in the field of marine biotechnology emphasize that, due to marine biological diversity and the specificity of biological marine metabolisms, the study of biocatalysts on a global scale from this environment is just starting, and possesses huge potential for the development of applications with industrial benefits. |
Altri titoli varianti: |
Marine Enzymes |
Titolo autorizzato: |
Marine Enzymes |
Formato: |
Materiale a stampa |
Livello bibliografico |
Monografia |
Lingua di pubblicazione: |
Inglese |
Record Nr.: | 9910557671503321 |
Lo trovi qui: | Univ. Federico II |
Opac: |
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