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1 to the design of highly active and specific polysaccharide lyases.
2 the first representatives of a new family of polysaccharide lyases.
4 mong enzymes within this unexplored class of polysaccharide lyases and reinforces the notion of a str
5 nts a significant enzymatic challenge to the polysaccharide lyases and sulfatases that mediate degrad
6 lases, lytic polysaccharide mono-oxygenases, polysaccharide lyases, and carbohydrate esterases, as we
7 -acting and exo-acting glycoside hydrolases, polysaccharide lyases, carbohydrate esterases, and lytic
9 ride by digestion with a recently discovered polysaccharide lyase derived from a bacteriophage specif
12 l, and functional screening, we identified a polysaccharide lyase family 7 enzyme that is unique to V
14 54 glycoside hydrolases, 11 sulfatases and 1 polysaccharide lyase from A. muciniphila to provide a ho
16 enzymes (CAZymes) (glycoside hydrolases and polysaccharide lyases) in the fecal microbiome, mass spe
18 ncluding symbionts and pathogens has evolved polysaccharide lyases (PL) that cleave their 1,4 glycosi
20 ism of mannuronan-specific ALs from family 7 polysaccharide lyases (PL7), employing time-resolved NMR
24 f VPS production and surface trimming by the polysaccharide lyase RbmB cause surface remodeling as bi
27 lude five glycoside hydrolases (GHs) and one polysaccharide lyase, the genes for which were transcrib
28 degree of polymerization involves the use of polysaccharide lyases, which catalyze the depolymerizati