Biochemical characterisation of four rhamnosidases from thermophilic bacteria of the genera Thermotoga, Caldicellulosiruptor and Thermoclostridium

  title={Biochemical characterisation of four rhamnosidases from thermophilic bacteria of the genera Thermotoga, Caldicellulosiruptor and Thermoclostridium},
  author={Melanie Baudrexl and Wolfgang H Schwarz and Vladimir V. Zverlov and Wolfgang Liebl},
  journal={Scientific Reports},
Carbohydrate active enzymes are classified in databases based on sequence and structural similarity. However, their function can vary considerably within a similarity-based enzyme family, which makes biochemical characterisation indispensable to unravel their physiological role and to arrive at a meaningful annotation of the corresponding genes. In this study, we biochemically characterised the four related enzymes Tm_Ram106B, Tn_Ram106B, Cb_Ram106B and Ts_Ram106B from the thermophilic bacteria… Expand
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Ruminiclostridium herbifermentans sp. nov., a mesophilic and moderately thermophilic cellulolytic and xylanolytic bacterium isolated from a lab-scale biogas fermenter fed with maize silage.
This strain represents a novel species in the genus Ruminiclostridium, family Oscillospiraceae, class Clostridia and can be clustered into one clade with other species of the genus JCM 39124T. Expand
Milling byproducts are an economically viable substrate for butanol production using clostridial ABE fermentation
Wheat milling byproducts are suitable substrates for clostridial ABE fermentation and ABE fermentation plants using wheat red dog as substrate are economically viable, and a profitability analysis was performed for small- to mid-scale Abe fermentation plants that utilize enzymatically pretreated wheat redDog as substrate. Expand


The thermostable α‐l‐rhamnosidase RamA of Clostridium stercorarium: biochemical characterization and primary structure of a bacterial α‐l‐rhamnoside hydrolase, a new type of inverting glycoside hydrolase
An α‐l‐rhamnosidase clone was isolated from a genomic library of the thermophilic anaerobic bacterium Clostridium stercorarium and its primary structure was determined, indicating a single displacement mechanism. Expand
Characterization of Two Distinct Glycosyl Hydrolase Family 78 α-l-Rhamnosidases from Pediococcus acidilactici
Detailed kinetic data is presented on two novel rhamnosidases from Pediococcus acidilactici DSM 20284, probably representing two subclasses within GH 78, which could be relevant for the further study of bacterial glycosidases. Expand
Structural and functional insights into RHA-P, a bacterial GH106 α-L-rhamnosidase from Novosphingobium sp. PP1Y.
Functional and structural characterization of RHA-P and a kinetic characterization of the enzyme on natural flavonoids such as naringin, rutin, hesperidin and quercitrin suggest that the enzyme may locate different polyphenolic aromatic moities in the active site. Expand
RHA-P: Isolation, expression and characterization of a bacterial α-l-rhamnosidase from Novosphingobium sp. PP1Y
Abstract α- l -Rhamnosidases (α-RHAs) are a group of glycosyl hydrolases of biotechnological potential in industrial processes, which catalyze the hydrolysis of α- l -rhamnose terminal residues fromExpand
Two new thermostable α-l-rhamnosidases from a novel thermophilic bacterium
Two new thermostable alpha-L-rhamnosidases with novel substrate hydrolysis pattern were cloned and expressed from a new thermophilic bacterium and their enzymes produced and purified. Expand
Molecular identification of an alpha-L-rhamnosidase from Bacillus sp strain GL1 as an enzyme involved in complete metabolism of gellan.
Both RhaA and RhaB were highly specific for rhamnosyl saccharides, including gellan disaccharide and naringin, and released rhamnose from substrates most efficiently at pH 6.5-7.0 and 40 degrees C. Expand
Purification and Characterization of an α-L-Rhamnosidase from Aspergillus terreus of Interest in Winemaking
An enzyme with α-L-rhamnoside activity was purified to homogeneity a culture filtrate of Aspergillus terreus after growth in a medium containing L-rhamnose as the sole carbon source. The biosynthesisExpand
The hemicellulose-degrading enzyme system of the thermophilic bacterium Clostridium stercorarium: comparative characterisation and addition of new hemicellulolytic glycoside hydrolases
Investigation of the substrate and product specificity of arabinoxylan-degrading enzymes revealed that only the GH10 xylanases were able to degrade arabinxylooligosaccharides, which may lead to synergistic effects and influence the enzyme choice for biotechnological applications. Expand
Characterization of a glycoside hydrolase family 78 α-l-rhamnosidase from Bacteroides thetaiotaomicron VPI-5482 and identification of functional residues
Recombinant BtRha78A exhibited a good pH stability and relatively high thermostability and could be tolerant of a low concentration of alcohols, which made it a promising alternative biocatalyst for industrial applications. Expand
Petroclostridium xylanilyticum gen. nov., sp. nov., a xylan-degrading bacterium isolated from an oilfield, and reclassification of clostridial cluster III members into four novel genera in a new Hungateiclostridiaceae fam. nov.
  • Xue Zhang, Bo Tu, +6 authors Lei Cheng
  • Biology, Medicine
  • International journal of systematic and evolutionary microbiology
  • 2018
Strain SK-Y3T is proposed as the type strain of a novel species of a new genus, Petroclostridium xylanilyticum gen. nov, and analysis through 16S rRNA gene, ribosomal protein and whole genome sequences indicated that clostridial cluster III members should be reclassified into four novel genera for which the names Hungateiclostridium gen.Nov. Expand