Artikel
Open Access
Recapitulation of stability diversity of microbial α-amylases
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Dhanya Gangadharan
Veröffentlicht/Copyright:
17. Dezember 2020
Received: 2020-08-26
Accepted: 2020-11-25
Published Online: 2020-12-17
© 2020 Dhanya Gangadharan et al., published by De Gruyter
Artikel in diesem Heft
- Production and characterization of psychrophilic α-amylase from a psychrophilic bacterium, Shewanella sp. ISTPL2
- Recapitulation of stability diversity of microbial α-amylases
- The structures of the GH13_36 amylases from Eubacterium rectale and Ruminococcus bromii reveal subsite architectures that favor maltose production
- TK-PUL, a pullulan hydrolase type III from Thermococcus kodakarensis, a potential candidate for simultaneous liquefaction and saccharification of starch
Schlagwörter für diesen Artikel
amylase;
extremophiles;
metagenomics;
protein engineering;
stability;
directed evolution
Creative Commons
BY-NC-ND 4.0
Artikel in diesem Heft
- Production and characterization of psychrophilic α-amylase from a psychrophilic bacterium, Shewanella sp. ISTPL2
- Recapitulation of stability diversity of microbial α-amylases
- The structures of the GH13_36 amylases from Eubacterium rectale and Ruminococcus bromii reveal subsite architectures that favor maltose production
- TK-PUL, a pullulan hydrolase type III from Thermococcus kodakarensis, a potential candidate for simultaneous liquefaction and saccharification of starch
