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dc.contributor.author |
Zhao, Hong-Yan |
|
dc.contributor.author |
Wu, Li-Ying |
|
dc.contributor.author |
Liu, Gang |
|
dc.date.accessioned |
2018-07-11T10:14:51Z |
|
dc.date.available |
2018-07-11T10:14:51Z |
|
dc.date.issued |
2016 |
|
dc.identifier.issn |
0916-8451 |
|
dc.identifier.uri |
http://hdl.handle.net/123456789/6525 |
|
dc.description |
p. 2480-2485 |
fr_FR |
dc.language.iso |
en |
fr_FR |
dc.relation.ispartofseries |
in:Bioscience, Biotechnology, and Biochemistry, Vol.80, n°12. (Déc.2016); |
|
dc.subject |
Protéases |
fr_FR |
dc.subject |
Protéase alcaline |
fr_FR |
dc.subject |
Bacillus pumilus |
fr_FR |
dc.subject |
Mutagénèse dirigée |
fr_FR |
dc.title |
Single-site substitutions improve cold activity and increase thermostability of the dehairing alkaline protease (DHAP) |
fr_FR |
dc.type |
Article |
fr_FR |
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