Dictyoglomus turgidum DSM 6724 α-Glucan Phosphorylase: Characterization and Its Application in Multi-enzyme Cascade Reaction for D-Tagatose Production.

Phosphorylase is a type of enzyme-producing sugar phosphates through the reversible phosphorolysis reactions of glycosides, which makes it an important starting enzyme in multi-enzyme systems for rare sugar biomanufacturing. To investigate its application in D-tagatose biosynthesis from maltodextrin using in vitro multi-enzyme cascade biosystem, the α-glucan phosphorylase (αGP; EC 2.4.

Genetic and biochemical characterization of thermophilic β-cyclodextrin glucanotransferase from Gracilibacillus alcaliphilus SK51.001.

Background: Gracilibacillus alcaliphilus SK51.001, a strain that produces β-CGTase (β-cyclodextrin glucanotransferase) (EC 2.4.

Characteristics of a fructose 6-phosphate 4-epimerase from Caldilinea aerophila DSM 14535 and its application for biosynthesis of tagatose.

Tagatose is a rare hexoketose with potential health benefits. Here, an enzyme, GatZ subunit ofd-tagatose-1,6-bisphosphate aldolase, was characterized. GatZ is involved in a multi-enzyme cascade reaction system that can produce tagatose from maltodextrin.

Lactulose production by a thermostable glycoside hydrolase from the hyperthermophilic archaeon Caldivirga maquilingensis IC-167.

Background: Lactulose has various uses in the food and pharmaceutical fields. Thermostable enzymes have many advantages for industrial exploitation, including high substrate solubilities as well as reduced risk of process contamination.

Results: Enzymatic synthesis of lactulose employing a transgalactosylation reaction by a recombinant thermostable glycoside hydrolase (GH1) from the hyperthermophilic archaeon Caldivirga maquilingensis IC-167 was investigated.

Characterization of a thermostable glycoside hydrolase (CMbg0408) from the hyperthermophilic archaeon Caldivirga maquilingensis IC-167.

Background: Hyperthermophilic archaea capable of functioning optimally at very high temperatures are a good source of unique and industrially important thermostable enzymes.

Results: A glycoside hydrolase family 1 β-galactosidase gene (BglB) from a hyperthermophilic archaeon Caldivirga maquilingensis IC-167 was cloned and expressed in Escherichia coli. The recombinant enzyme (CMbg0408) displayed optimum activity at 110 °C and pH 5.

Cloning and characterization of a new ribitol dehydrogenase from Providencia alcalifaciens RIMD 1656011.

Background: A new ribitol dehydrogenase gene was cloned from Providencia alcalifaciens RIMD 1656011 and expressed in Escherichia coli BL21. This study aimed to purify and characterize the ribitol dehydrogenase from P. alcalifaciens RIMD 1656011 and investigate its substrate specificity for potential use as an industrial enzyme.