Publications

Design of a highly thermostable hemicellulose-degrading blend from Thermotoga neapolitana for the treatment of lignocellulosic biomass  (2019)

Authors:
Benedetti, Manuel; Vecchi, Valeria; Betterle, Nico; Natali, Alberto; Bassi, Roberto; Dall'Osto, Luca
Title:
Design of a highly thermostable hemicellulose-degrading blend from Thermotoga neapolitana for the treatment of lignocellulosic biomass
Year:
2019
Type of item:
Articolo in Rivista
Tipologia ANVUR:
Articolo su rivista
Language:
Inglese
Format:
Elettronico
Referee:
Name of journal:
JOURNAL OF BIOTECHNOLOGY
ISSN of journal:
0168-1656
N° Volume:
296
Page numbers:
42-52
Keyword:
CWDE; Cellulases; Hemicellulases; Hyperthermophilic enzyme; Lignocellulose; Thermotoga neapolitana; Biofuels; Biomass; Cellulase; Enzyme Stability; Escherichia coli; Fermentation; Glycoside Hydrolases; Hydrolysis; Lignin; Polysaccharides; Temperature; Thermotoga neapolitana
Short description of contents:
The biological conversion of lignocellulose into fermentable sugars is a key process for the sustainable production of biofuels from plant biomass. Polysaccharides in plant feedstock can be valorized using thermostable mixtures of enzymes that degrade the cell walls, thus avoiding harmful and expensive pre-treatments. (Hyper) thermophilic bacteria of the phylum Thermotogae provide a rich source of enzymes for such industrial applications. Here we selected T. neapolitana as a source of hyperthermophilic hemicellulases for the degradation of lignocellulosic biomass. Two genes encoding putative hemicellulases were cloned from T. neapolitana genomic DNA and expressed in Escherichia coli. Further characterization revealed that the genes encoded an endo-1,4-ss galactanase and an a-L-arabinofuranosidase with optimal temperatures of (similar to)90 degrees C and high turnover numbers during catalysis (kcat values of (similar to)177 and (similar to)133 s(-1), respectively, on soluble substrates). These enzymes were combined with three additional T. neapolitana hyperthermophilic hemicellulases -endo-1,4-beta-xylanase (XynA), endo-1,4-beta-mannanase (ManB/Man5A) and beta-glucosidase (GghA) -to form a highly thermostable hemicellulolytic blend. The treatment of barley straw and corn bran with this enzymatic cocktail resulted in the solubilization of multiple hemicelluloses and boosted the yield of fermentable sugars by up to 65% when the complex substrates were further degraded by cellulases.
Product ID:
110228
Handle IRIS:
11562/1000180
Last Modified:
November 15, 2022
Bibliographic citation:
Benedetti, Manuel; Vecchi, Valeria; Betterle, Nico; Natali, Alberto; Bassi, Roberto; Dall'Osto, Luca, Design of a highly thermostable hemicellulose-degrading blend from Thermotoga neapolitana for the treatment of lignocellulosic biomass «JOURNAL OF BIOTECHNOLOGY» , vol. 2962019pp. 42-52

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