Cloning, molecular modeling, and docking analysis of alkali-thermostable β-mannanase from Bacillus nealsonii PN-11
Gespeichert in:
Verfasser / Beitragende:
[Prakram Chauhan, Satya Tripathi, Abhays Sangamwar, Neena Puri, Prince Sharma, Naveen Gupta]
Ort, Verlag, Jahr:
2015
Enthalten in:
Applied Microbiology and Biotechnology, 99/21(2015-11-01), 8917-8925
Format:
Artikel (online)
Online Zugang:
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| 024 | 7 | 0 | |a 10.1007/s00253-015-6613-2 |2 doi |
| 035 | |a (NATIONALLICENCE)springer-10.1007/s00253-015-6613-2 | ||
| 245 | 0 | 0 | |a Cloning, molecular modeling, and docking analysis of alkali-thermostable β-mannanase from Bacillus nealsonii PN-11 |h [Elektronische Daten] |c [Prakram Chauhan, Satya Tripathi, Abhays Sangamwar, Neena Puri, Prince Sharma, Naveen Gupta] |
| 520 | 3 | |a An alkali-thermostable β-mannanase gene from Bacillus nealsonii PN-11 was cloned by functional screening of E. coli cells transformed with pSMART/HaeIII genomic library. The ORF encoding mannanase consisted of 1100bp, corresponding to protein of 369 amino acids and has a catalytic domain belonging to glycoside hydrolase family 5. Cloned mannanase was smaller in size than the native mannanase by 10kDa. This change in molecular mass could be because of difference in the glycosylation. The tertiary structure of the β-mannanase (MANPN11) was designed and it showed a classical (α/β) TIM-like barrel motif. Active site of MANPN11 was represented by 8 amino acid residues viz., Glu152, Trp189, His217, Tyr219, Glu247, Trp276, Trp285, and Tyr287. Model surface charge of MANPN11 predicted that surface near active site was mostly negative, and the opposite side was positive which might be responsible for the stability of the enzymes at high pH. Stability of MANPN11 at alkaline pH was further supported by the formation of a hydrophobic pocket near active site of the enzyme. To understand the ability of MANPN11 to bind with different substrates, docking studies were performed and found that mannopentose fitted properly into active site and form stable enzyme substrate complex. | |
| 540 | |a Springer-Verlag Berlin Heidelberg, 2015 | ||
| 690 | 7 | |a Bacillus nealsonii |2 nationallicence | |
| 690 | 7 | |a Alkali-thermostable enzyme |2 nationallicence | |
| 690 | 7 | |a Cloning |2 nationallicence | |
| 690 | 7 | |a β-Mannanase gene |2 nationallicence | |
| 690 | 7 | |a Homology modeling |2 nationallicence | |
| 690 | 7 | |a Docking |2 nationallicence | |
| 700 | 1 | |a Chauhan |D Prakram |u Department of Microbiology, BMS Block, Panjab University South Campus, Chandigarh, India |4 aut | |
| 700 | 1 | |a Tripathi |D Satya |u Department of Pharmacoinformatics, National Institute of Pharmaceutical Science Education and Research, S.A.S, Nagar, Mohali, Punjab, India |4 aut | |
| 700 | 1 | |a Sangamwar |D Abhays |u Department of Pharmacoinformatics, National Institute of Pharmaceutical Science Education and Research, S.A.S, Nagar, Mohali, Punjab, India |4 aut | |
| 700 | 1 | |a Puri |D Neena |u Department of Industrial Microbiology, Guru Nanak Khalsa College, Yamunanagar, Haryana, India |4 aut | |
| 700 | 1 | |a Sharma |D Prince |u Department of Microbiology, BMS Block, Panjab University South Campus, Chandigarh, India |4 aut | |
| 700 | 1 | |a Gupta |D Naveen |u Department of Microbiology, BMS Block, Panjab University South Campus, Chandigarh, India |4 aut | |
| 773 | 0 | |t Applied Microbiology and Biotechnology |d Springer Berlin Heidelberg |g 99/21(2015-11-01), 8917-8925 |x 0175-7598 |q 99:21<8917 |1 2015 |2 99 |o 253 | |
| 856 | 4 | 0 | |u https://doi.org/10.1007/s00253-015-6613-2 |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/s00253-015-6613-2 |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Chauhan |D Prakram |u Department of Microbiology, BMS Block, Panjab University South Campus, Chandigarh, India |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Tripathi |D Satya |u Department of Pharmacoinformatics, National Institute of Pharmaceutical Science Education and Research, S.A.S, Nagar, Mohali, Punjab, India |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Sangamwar |D Abhays |u Department of Pharmacoinformatics, National Institute of Pharmaceutical Science Education and Research, S.A.S, Nagar, Mohali, Punjab, India |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Puri |D Neena |u Department of Industrial Microbiology, Guru Nanak Khalsa College, Yamunanagar, Haryana, India |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Sharma |D Prince |u Department of Microbiology, BMS Block, Panjab University South Campus, Chandigarh, India |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Gupta |D Naveen |u Department of Microbiology, BMS Block, Panjab University South Campus, Chandigarh, India |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t Applied Microbiology and Biotechnology |d Springer Berlin Heidelberg |g 99/21(2015-11-01), 8917-8925 |x 0175-7598 |q 99:21<8917 |1 2015 |2 99 |o 253 | ||