Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-73 |
Sentence |
denotes |
Characterisation of a 1,4-beta-fucoside hydrolase degrading colanic acid. |
TextSentencer_T2 |
74-244 |
Sentence |
denotes |
A novel colanic acid-degrading enzyme was isolated from a mixed culture filtrate obtained by enrichment culturing of a compost sample using colanic acid as carbon source. |
TextSentencer_T3 |
245-332 |
Sentence |
denotes |
The enzyme was partially purified resulting in a 17-fold increase in specific activity. |
TextSentencer_T4 |
333-487 |
Sentence |
denotes |
Further purification by Native PAGE revealed that the enzyme is part of a high-molecular weight multi protein complex of at least six individual proteins. |
TextSentencer_T5 |
488-624 |
Sentence |
denotes |
The enzyme showed a temperature optimum at 50 degrees C while after 5h at 50 degrees C and pH7 still 70% of the total activity was left. |
TextSentencer_T6 |
625-660 |
Sentence |
denotes |
The pH optimum was found to be pH7. |
TextSentencer_T7 |
661-843 |
Sentence |
denotes |
Analysis of the degradation products showed that the enzyme is a novel 1,4-beta-fucoside hydrolase that liberates repeating units of colanic acid with varying degrees of acetylation. |
TextSentencer_T8 |
844-968 |
Sentence |
denotes |
Km and Vmax of the enzyme were determined against the native substrate as well as its de-O-acetylated and depyruvated forms. |
TextSentencer_T9 |
969-1072 |
Sentence |
denotes |
Compared to the native substrate the affinity of the enzyme for the modified substrates was much lower. |
TextSentencer_T10 |
1073-1170 |
Sentence |
denotes |
However, for the de-O-acetylated sample a dramatic increase in catalytic efficiency was observed. |
TextSentencer_T11 |
1171-1323 |
Sentence |
denotes |
The native form of the substrate showed substrate inhibition at high concentrations, probably due to the formation of nonproductive substrate complexes. |
TextSentencer_T12 |
1324-1426 |
Sentence |
denotes |
Removal of the acetyl groups probably prevents this effect resulting in a higher catalytic efficiency. |
T1 |
0-73 |
Sentence |
denotes |
Characterisation of a 1,4-beta-fucoside hydrolase degrading colanic acid. |
T2 |
74-244 |
Sentence |
denotes |
A novel colanic acid-degrading enzyme was isolated from a mixed culture filtrate obtained by enrichment culturing of a compost sample using colanic acid as carbon source. |
T3 |
245-332 |
Sentence |
denotes |
The enzyme was partially purified resulting in a 17-fold increase in specific activity. |
T4 |
333-487 |
Sentence |
denotes |
Further purification by Native PAGE revealed that the enzyme is part of a high-molecular weight multi protein complex of at least six individual proteins. |
T5 |
488-624 |
Sentence |
denotes |
The enzyme showed a temperature optimum at 50 degrees C while after 5h at 50 degrees C and pH7 still 70% of the total activity was left. |
T6 |
625-660 |
Sentence |
denotes |
The pH optimum was found to be pH7. |
T7 |
661-843 |
Sentence |
denotes |
Analysis of the degradation products showed that the enzyme is a novel 1,4-beta-fucoside hydrolase that liberates repeating units of colanic acid with varying degrees of acetylation. |
T8 |
844-968 |
Sentence |
denotes |
Km and Vmax of the enzyme were determined against the native substrate as well as its de-O-acetylated and depyruvated forms. |
T9 |
969-1072 |
Sentence |
denotes |
Compared to the native substrate the affinity of the enzyme for the modified substrates was much lower. |
T10 |
1073-1170 |
Sentence |
denotes |
However, for the de-O-acetylated sample a dramatic increase in catalytic efficiency was observed. |
T11 |
1171-1323 |
Sentence |
denotes |
The native form of the substrate showed substrate inhibition at high concentrations, probably due to the formation of nonproductive substrate complexes. |
T12 |
1324-1426 |
Sentence |
denotes |
Removal of the acetyl groups probably prevents this effect resulting in a higher catalytic efficiency. |