Thermostable enzymes as biocatalysts in the biofuel industry

CJ Yeoman, Y Han, D Dodd, CM Schroeder… - Advances in applied …, 2010 - Elsevier
Lignocellulose is the most abundant carbohydrate source in nature and represents an ideal
renewable energy source. Thermostable enzymes that hydrolyze lignocellulose to its …

The crystal structures of Sinapis alba myrosinase and a covalent glycosyl–enzyme intermediate provide insights into the substrate recognition and active-site …

WP Burmeister, S Cottaz, H Driguez, R Iori, S Palmieri… - Structure, 1997 - cell.com
Background: Myrosinase is the enzyme responsible for the hydrolysis of a variety of plant
anionic 1-thio-β-D-glucosides called glucosinolates. Myrosinase and glucosinolates, which …

Crystal structure of the β-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus: resilience as a key factor in thermostability

CF Aguilar, I Sanderson, M Moracci… - Journal of molecular …, 1997 - Elsevier
Enzymes from hyperthermophilic organisms must operate at temperatures which rapidly
denature proteins from mesophiles. The structural basis of this thermostability is still poorly …

The mechanism of substrate (aglycone) specificity in β-glucosidases is revealed by crystal structures of mutant maize β-glucosidase-DIMBOA,-DIMBOAGlc, and …

M Czjzek, M Cicek, V Zamboni… - Proceedings of the …, 2000 - National Acad Sciences
The mechanism and the site of substrate (ie, aglycone) recognition and specificity were
investigated in maize β-glucosidase (Glu1) by x-ray crystallography by using crystals of a …

Molecular mechanism of Aspergillus fumigatus biofilm disruption by fungal and bacterial glycoside hydrolases

F Le Mauff, NC Bamford, N Alnabelseya… - Journal of Biological …, 2019 - ASBMB
During infection, the fungal pathogen Aspergillus fumigatus forms biofilms that enhance its
resistance to antimicrobials and host defenses. An integral component of the biofilm matrix is …

Restoration of the Activity of Active-Site Mutants of the Hyperthermophilic β-Glycosidase from Sulfolobus solfataricus:  Dependence of the Mechanism on the Action …

M Moracci, A Trincone, G Perugino, M Ciaramella… - Biochemistry, 1998 - ACS Publications
The β-glycosidase from the hyperthermophilic Archaeon Sulfolobus solfataricus hydrolyzes
β-glycosides following a retaining mechanism based upon the action of two amino acids …

Residue Effect-Guided Design: Engineering of S. Solfataricus β-Glycosidase to Enhance Its Thermostability and Bioproduction of Ginsenoside Compound K

W Shen, PA Dalby, Z Guo, W Li, C Zhu… - Journal of Agricultural …, 2023 - ACS Publications
β-Glycosidase from Sulfolobus solfataricus (SS-BGL) is a highly effective biocatalyst for the
synthesis of compound K (CK) from glycosylated protopanaxadiol ginsenosides. In order to …

Comparative Structural Analysis and Substrate Specificity Engineering of the Hyperthermostable β-Glucosidase CelB from Pyrococcus furiosus

T Kaper, JHG Lebbink, J Pouwels, J Kopp… - Biochemistry, 2000 - ACS Publications
The substrate specificity of the β-glucosidase (CelB) from the hyperthermophilic archaeon
Pyrococcus furiosus, a family 1 glycosyl hydrolase, has been studied at a molecular level …

Substrate specificity and transglycosylation catalyzed by a thermostable β-glucosidase from marine hyperthermophile Thermotoga neapolitana

TH Park, KW Choi, CS Park, SB Lee, HY Kang… - Applied microbiology …, 2005 - Springer
The gene encoding β-glucosidase of the marine hyperthermophilic eubacterium
Thermotoga neapolitana (bglA) was subcloned and expressed in Escherichia coli. The …

Identification and molecular characterization of the first α-xylosidase from an archaeon

M Moracci, BC Ponzano, A Trincone, S Fusco… - Journal of Biological …, 2000 - ASBMB
We here report the first molecular characterization of an α-xylosidase (XylS) from an
Archaeon. Sulfolobus solfataricus is able to grow at temperatures higher than 80° C on …