47491-70-3Relevant articles and documents
Sustainable synthesis of N-acetyllactosamine using an immobilized β-galactosidase on a tailor made porous polymer
Aires-Trapote, Antonio,Tamayo, Aitana,Rubio, Juan,Rumbero, Angel,Hernáiz, María J.
, p. 40375 - 40383 (2015/05/20)
Porous polymer particles containing surface epoxy groups were synthesized for immobilizing β-galactosidase from Bacillus circulans. Enzyme immobilization was achieved by covalent attachment to a custom made porous polymer and the biocatalyst was character
Characterization of a novel Salmonella Typhimurium chitinase which hydrolyzes chitin, chitooligosaccharides and an N-acetyllactosamine conjugate
Larsen, Tanja,Petersen, Bent O.,Storgaard, Birgit G.,Duus, Jens,Palcic, Monica M.,Leisner, Jorgen J.
scheme or table, p. 426 - 436 (2012/01/13)
Salmonella contain genes annotated as chitinases; however, their chitinolytic activities have never been verified. We now demonstrate such an activity for a chitinase assigned to glycoside hydrolase family 18 encoded by the SL0018 (chiA) gene in Salmonella enterica Typhimurium SL1344. A C-terminal truncated form of chiA lacking a putative chitin-binding domain was amplified by PCR, cloned and expressed in Escherichia coli BL21 (DE3) with an N-terminal (His)6 tag. The purified enzyme hydrolyzes 4-nitrophenyl N,N′-diacetyl - d-chitobioside, 4-nitrophenyl -d-N,N′,N″-triacetylchitotriose and carboxymethyl chitin Remazol Brilliant Violet but does not act on 4-nitrophenyl N-acetyl - d-glucosaminide, peptidoglycan or 4-nitrophenyl -d-cellobioside. Enzyme activity was also characterized by directly monitoring product formation using 1H-nuclear magnetic resonance which showed that chitin is a substrate with the release of N,N′-diacetylchitobiose. Hydrolysis occurs with the retention of configuration and the enzyme acts on only the -anomers of chitooligosaccharide substrates. The enzyme also released N-acetyllactosamine disaccharide from Gal1 → 4GlcNAc-O-(CH2)8CONH(CH 2)2NHCO-tetramethylrhodamine, a model substrate for LacNAc terminating glycoproteins and glycolipids.
The efficient enzymatic synthesis of N-acetyllactosamine in an organic co-solvent
Yoon, Jung Hae,Rhee, Joon Shick
, p. 377 - 383 (2007/10/03)
In the presence of β-galactosidase from Bifidobacterium bifidum, N-acetyllactosamine was synthesized in significantly enhanced yield compared with earlier routes. Different proportions of the (1→4)- and (1→6)-linked forms were obtained depending on the choice of enzyme and reaction conditions, viz. the nature of added organic co-solvent (20-80% of 2-ethoxy ethyl ether, trimethyl phosphate, or acetone). The β-(1→4)-linked disaccharide was the major product and the β-(1→6)-linked disaccharide was the minor product. With β-galactosidases from P. multicolor, A. oryzae, B. longum the β-(1→6) linkage was exclusively synthesized. Procedures for optimising the yield of N-acetyllactosamine are discussed. An immobilized enzyme on a nylon powder column was used for the efficient recycling of enzyme and synthesizing the disaccharide. Copyright (C) 2000 Elsevier Science Ltd.
