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Id Subject Object Predicate Lexical cue
TextSentencer_T1 0-142 Sentence denotes An exo-alpha-sialidase from bifidobacteria involved in the degradation of sialyloligosaccharides in human milk and intestinal glycoconjugates.
T1 0-142 Sentence denotes An exo-alpha-sialidase from bifidobacteria involved in the degradation of sialyloligosaccharides in human milk and intestinal glycoconjugates.
T1 0-142 Sentence denotes An exo-alpha-sialidase from bifidobacteria involved in the degradation of sialyloligosaccharides in human milk and intestinal glycoconjugates.
TextSentencer_T2 143-385 Sentence denotes Bifidobacteria are health-promoting enteric commensals that are assumed to proliferate predominantly in the intestines of breast-fed infants by assimilating human milk oligosaccharides (HMOs) that are frequently fucosylated and/or sialylated.
T2 143-385 Sentence denotes Bifidobacteria are health-promoting enteric commensals that are assumed to proliferate predominantly in the intestines of breast-fed infants by assimilating human milk oligosaccharides (HMOs) that are frequently fucosylated and/or sialylated.
T2 143-385 Sentence denotes Bifidobacteria are health-promoting enteric commensals that are assumed to proliferate predominantly in the intestines of breast-fed infants by assimilating human milk oligosaccharides (HMOs) that are frequently fucosylated and/or sialylated.
TextSentencer_T3 386-563 Sentence denotes We previously identified two different α-l-fucosidases in Bifidobacterium bifidum and showed that the strain furnishes an extracellular degradation pathway for fucosylated HMOs.
T3 386-563 Sentence denotes We previously identified two different α-l-fucosidases in Bifidobacterium bifidum and showed that the strain furnishes an extracellular degradation pathway for fucosylated HMOs.
T3 386-563 Sentence denotes We previously identified two different α-l-fucosidases in Bifidobacterium bifidum and showed that the strain furnishes an extracellular degradation pathway for fucosylated HMOs.
TextSentencer_T4 564-649 Sentence denotes However, the catabolism of sialylated HMOs by bifidobacteria has remained unresolved.
T4 564-649 Sentence denotes However, the catabolism of sialylated HMOs by bifidobacteria has remained unresolved.
T4 564-649 Sentence denotes However, the catabolism of sialylated HMOs by bifidobacteria has remained unresolved.
TextSentencer_T5 650-747 Sentence denotes Here we describe the identification and characterization of an exo-α-sialidase in bifidobacteria.
T5 650-747 Sentence denotes Here we describe the identification and characterization of an exo-α-sialidase in bifidobacteria.
T5 650-747 Sentence denotes Here we describe the identification and characterization of an exo-α-sialidase in bifidobacteria.
TextSentencer_T6 748-959 Sentence denotes By expression cloning, we isolated a novel exo-α-sialidase gene (siabb2) from B. bifidum JCM1254, which encodes a protein (SiaBb2) consisting of 835-amino-acid residues with a predicted molecular mass of 87 kDa.
T6 748-959 Sentence denotes By expression cloning, we isolated a novel exo-α-sialidase gene (siabb2) from B. bifidum JCM1254, which encodes a protein (SiaBb2) consisting of 835-amino-acid residues with a predicted molecular mass of 87 kDa.
T6 748-959 Sentence denotes By expression cloning, we isolated a novel exo-α-sialidase gene (siabb2) from B. bifidum JCM1254, which encodes a protein (SiaBb2) consisting of 835-amino-acid residues with a predicted molecular mass of 87 kDa.
TextSentencer_T7 960-1212 Sentence denotes SiaBb2 possesses an N-terminal signal sequence, a sialidase catalytic domain classified into the glycoside hydrolase family 33 (GH33) and a C-terminal transmembrane region, indicating that the mature SiaBb2 is an extracellular membrane-anchored enzyme.
T7 960-1212 Sentence denotes SiaBb2 possesses an N-terminal signal sequence, a sialidase catalytic domain classified into the glycoside hydrolase family 33 (GH33) and a C-terminal transmembrane region, indicating that the mature SiaBb2 is an extracellular membrane-anchored enzyme.
T7 960-1212 Sentence denotes SiaBb2 possesses an N-terminal signal sequence, a sialidase catalytic domain classified into the glycoside hydrolase family 33 (GH33) and a C-terminal transmembrane region, indicating that the mature SiaBb2 is an extracellular membrane-anchored enzyme.
TextSentencer_T8 1213-1346 Sentence denotes The recombinant enzyme expressed in Escherichia coli showed the highest activity in an acidic pH range from 4.0 to 5.0, and at 50 °C.
T8 1213-1346 Sentence denotes The recombinant enzyme expressed in Escherichia coli showed the highest activity in an acidic pH range from 4.0 to 5.0, and at 50 °C.
T8 1213-1462 Sentence denotes The recombinant enzyme expressed in Escherichia coli showed the highest activity in an acidic pH range from 4.0 to 5.0, and at 50 °C. Notably, 80% activity remained after 30 min incubation at 80 °C, indicating that the enzyme is highly thermostable.
TextSentencer_T9 1347-1462 Sentence denotes Notably, 80% activity remained after 30 min incubation at 80 °C, indicating that the enzyme is highly thermostable.
T9 1347-1462 Sentence denotes Notably, 80% activity remained after 30 min incubation at 80 °C, indicating that the enzyme is highly thermostable.
TextSentencer_T10 1463-1698 Sentence denotes SiaBb2 liberated sialic acids from sialyloligosaccharides, gangliosides, glycoproteins and colominic acid; however, the linkage preference of the enzyme was remarkably biased toward the α2,3-linkage rather than α2,6- and α2,8-linkages.
T9 1463-1698 Sentence denotes SiaBb2 liberated sialic acids from sialyloligosaccharides, gangliosides, glycoproteins and colominic acid; however, the linkage preference of the enzyme was remarkably biased toward the α2,3-linkage rather than α2,6- and α2,8-linkages.
T10 1463-1698 Sentence denotes SiaBb2 liberated sialic acids from sialyloligosaccharides, gangliosides, glycoproteins and colominic acid; however, the linkage preference of the enzyme was remarkably biased toward the α2,3-linkage rather than α2,6- and α2,8-linkages.
TextSentencer_T11 1699-1857 Sentence denotes Expression of siabb2 in B. longum 105-A, which has no endogenous exo-α-sialidase, enabled this strain to degrade sialyloligosaccharides present in human milk.
T10 1699-1857 Sentence denotes Expression of siabb2 in B. longum 105-A, which has no endogenous exo-α-sialidase, enabled this strain to degrade sialyloligosaccharides present in human milk.
T11 1699-1857 Sentence denotes Expression of siabb2 in B. longum 105-A, which has no endogenous exo-α-sialidase, enabled this strain to degrade sialyloligosaccharides present in human milk.
TextSentencer_T12 1858-1960 Sentence denotes Our results suggest that SiaBb2 plays a crucial role in bifidobacterial catabolism of sialylated HMOs.
T11 1858-1960 Sentence denotes Our results suggest that SiaBb2 plays a crucial role in bifidobacterial catabolism of sialylated HMOs.
T12 1858-1960 Sentence denotes Our results suggest that SiaBb2 plays a crucial role in bifidobacterial catabolism of sialylated HMOs.