The role of N1 domain on the activity, stability, substrate specificity and raw starch binding of amylopullulanase of the extreme thermophile Geobacillus thermoleovorans
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| 024 | 7 | 0 | |a 10.1007/s00253-014-6345-8 |2 doi |
| 035 | |a (NATIONALLICENCE)springer-10.1007/s00253-014-6345-8 | ||
| 245 | 0 | 4 | |a The role of N1 domain on the activity, stability, substrate specificity and raw starch binding of amylopullulanase of the extreme thermophile Geobacillus thermoleovorans |h [Elektronische Daten] |c [M. Nisha, T. Satyanarayana] |
| 520 | 3 | |a In order to understand the role of N1 domain (1-257 aa) in the amylopullulanase (gt-apu) of the extremely thermophilic bacterium Geobacillus thermoleovorans NP33, N1 deletion construct (gt-apuΔN) has been generated and expressed in Escherichia coli. The truncated amylopullulanase (gt-apuΔN) exhibits similar pH and temperature optima like gt-apu, but enhanced thermostability. The gt-apuΔN has greater hydrolytic action and specific activity on pullulan than gt-apu. The k cat (starch and pullulan) and K m (starch) values of gt-apuΔN increased, while K m (pullulan) decreased. The enzyme upon N1 deletion hydrolyzed maltotetraose as the smallest substrate in contrast to maltopentaose of gt-apu. The role of N1 domain of gt-apu in raw starch binding has been confirmed, for the first time, based on deletion and Langmuir-Hinshelwood kinetics. Furthermore, N1 domain appears to exert a negative influence on the thermostability of gt-apu because N1 truncation significantly improves thermostability. | |
| 540 | |a Springer-Verlag Berlin Heidelberg, 2015 | ||
| 690 | 7 | |a Amylopullulanase |2 nationallicence | |
| 690 | 7 | |a Truncation |2 nationallicence | |
| 690 | 7 | |a Geobacillus thermoleovorans |2 nationallicence | |
| 690 | 7 | |a X25 domain |2 nationallicence | |
| 690 | 7 | |a Thermostable |2 nationallicence | |
| 690 | 7 | |a Raw starch binding |2 nationallicence | |
| 700 | 1 | |a Nisha |D M. |u Department of Microbiology, University of Delhi South Campus, Benito Juarez Road, 110 021, New Delhi, India |4 aut | |
| 700 | 1 | |a Satyanarayana |D T. |u Department of Microbiology, University of Delhi South Campus, Benito Juarez Road, 110 021, New Delhi, India |4 aut | |
| 773 | 0 | |t Applied Microbiology and Biotechnology |d Springer Berlin Heidelberg |g 99/13(2015-07-01), 5461-5474 |x 0175-7598 |q 99:13<5461 |1 2015 |2 99 |o 253 | |
| 856 | 4 | 0 | |u https://doi.org/10.1007/s00253-014-6345-8 |q text/html |z Onlinezugriff via DOI |
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 900 | 7 | |a Metadata rights reserved |b Springer special CC-BY-NC licence |2 nationallicence | |
| 908 | |D 1 |a research-article |2 jats | ||
| 949 | |B NATIONALLICENCE |F NATIONALLICENCE |b NL-springer | ||
| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1007/s00253-014-6345-8 |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Nisha |D M. |u Department of Microbiology, University of Delhi South Campus, Benito Juarez Road, 110 021, New Delhi, India |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Satyanarayana |D T. |u Department of Microbiology, University of Delhi South Campus, Benito Juarez Road, 110 021, New Delhi, India |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t Applied Microbiology and Biotechnology |d Springer Berlin Heidelberg |g 99/13(2015-07-01), 5461-5474 |x 0175-7598 |q 99:13<5461 |1 2015 |2 99 |o 253 | ||