81131-46-6Relevant articles and documents
Characterization of a bacterial laminaribiose phosphorylase
Kitaoka, Motomitsu,Matsuoka, Yasuyuki,Mori, Kiyotaka,Nishimoto, Mamoru,Hayashi, Kiyoshi
, p. 343 - 348 (2012/08/08)
Bacterial laminaribiose phosphorylase (LBPbac) was first identified and purified from cell-free extract of Paenibacillus sp. YM-1. It phosphorolyzed laminaribiose into α-glucose 1-phosphate and glucose, but did not phosphorolyze other glucobioses. It slightly phosphorolyzed laminaritriose and higher laminarioligosaccharides. The specificity of the degree of polymerization of the substrate was clearly different from that of the enzyme of Euglena gracilis (LBPEug): LBPbac was more specific to laminaribiose than LBPEug. It showed acceptor specificity in reverse phosphorolysis similar to LBPEug. Cloning of the gene encoding LBPbac (lbpA) has revealed that LBPbac is a member of the glucoside hydrolase family 94, which includes cellobiose phosphorylase, cellodextrin phosphorylase, and N,N0-diacetylchitobiose phosphorylase. The genes that encode the components of an ATP-binding cassette sugar transporter specific to laminarioligosaccharides were identified upstream of lbpA, suggesting that the role of LBPbac is to utilize laminaribiose generated outside the cell. This role is different from that of LBPEug, which participates in the utilization of paramylon, the intracellular storage 1,3-β-glucan.
Enzymatic syntheses and selective hydrolysis of O-β-d- galactopyranosides using a marine mollusc β-galactosidase
Giordano, Assunta,Tramice, Annabella,Andreotti, Giuseppina,Mollo, Ernesto,Trincone, Antonio
, p. 139 - 143 (2007/10/03)
The use of crude extract of the hepatopancreas of Aplysia fasciata, a large mollusc belonging to the order Anaspidea containing a β-galactosidase activity, was reported for the synthesis of different galactosides. Good yields with polar acceptors and the
1-O-Acetyl-β-D-galactopyranose: A novel substrate for the transglycosylation reaction catalyzed by the β-galactosidase from Penicillium sp.
Zinin, Alexander I.,Eneyskaya, Elena V.,Shabalin, Konstantin A.,Kulminskaya, Anna A.,Shishlyannikov, Sergei M.,Neustroev, Kirill N.
, p. 635 - 642 (2007/10/03)
1-O-Acetyl-β-D-galactopyranose (AcGal), a new substrate for β-galactosidase, was synthesized in a stereoselective manner by the trichloroacetimidate procedure. Kinetic parameters (KM and kcat) for the hydrolysis of 1-O-acetyl-β-D-galactopyranose catalyzed by the β-D-galactosidase from Penicillium sp. were compared with similar characteristics for a number of natural and synthetic substrates. The value for kcat in the hydrolysis of AcGal was three orders of magnitude greater than for other known substrates. The β-galactosidase hydrolyzes AcGal with retention of anomeric configuration. The transglycosylation activity of the β-D-galactosidase in the reaction of AcGal and methyl β-D-galactopyranoside (1) as substrates was investigated by 1H NMR spectroscopy and HPLC techniques. The transglycosylation product using AcGal as a substrate was β-D-galactopyranosyl-(1→6)-1-O-acetyl-β-D-galactopyranose (with a yield of ～70%). In the case of 1 as a substrate, the main transglycosylation product was methyl β-D-galactopyranosyl-(1→6)-β-D-galactopyranoside. Methyl β-D-galactopyranosyl-(1→3)-β-D-galactopyranoside was found to be minor product in the latter reaction.
