| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-141 |
Sentence |
denotes |
The activity of barley alpha-amylase on starch granules is enhanced by fusion of a starch binding domain from Aspergillus niger glucoamylase. |
| T2 |
142-260 |
Sentence |
denotes |
High affinity for starch granules of certain amylolytic enzymes is mediated by a separate starch binding domain (SBD). |
| T3 |
261-388 |
Sentence |
denotes |
In Aspergillus niger glucoamylase (GA-I), a 70 amino acid O-glycosylated peptide linker connects SBD with the catalytic domain. |
| T4 |
389-520 |
Sentence |
denotes |
A gene was constructed to encode barley alpha-amylase 1 (AMY1) fused C-terminally to this SBD via a 37 residue GA-I linker segment. |
| T5 |
521-640 |
Sentence |
denotes |
AMY1-SBD was expressed in A. niger, secreted using the AMY1 signal sequence at 25 mg x L(-1) and purified in 50% yield. |
| T6 |
641-785 |
Sentence |
denotes |
AMY1-SBD contained 23% carbohydrate and consisted of correctly N-terminally processed multiple forms of isoelectric points in the range 4.1-5.2. |
| T7 |
786-1065 |
Sentence |
denotes |
Activity and apparent affinity of AMY1-SBD (50 nM) for barley starch granules of 0.034 U x nmol(-1) and K(d) = 0.13 mg x mL(-1), respectively, were both improved with respect to the values 0.015 U x nmol(-1) and 0.67 mg x mL(-1) for rAMY1 (recombinant AMY1 produced in A. niger). |
| T8 |
1066-1178 |
Sentence |
denotes |
AMY1-SBD showed a 2-fold increased activity for soluble starch at low (0.5%) but not at high (1%) concentration. |
| T9 |
1179-1288 |
Sentence |
denotes |
AMY1-SBD hydrolysed amylose DP440 with an increased degree of multiple attack of 3 compared to 1.9 for rAMY1. |
| T10 |
1289-1492 |
Sentence |
denotes |
Remarkably, at low concentration (2 nM), AMY1-SBD hydrolysed barley starch granules 15-fold faster than rAMY1, while higher amounts of AMY-SBD caused molecular overcrowding of the starch granule surface. |
