Thermostability enhancement of an endo-1,4-β-galactanase from Talaromyces stipitatus by site-directed mutagenesis
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Computational tools help improve protein stability but with a solubility tradeoff.Effect of mutations on the thermostability of Aspergillus aculeatus β-1,4-galactanase.Engineering the thermostability of β-glucuronidase from Penicillium purpurogenum Li-3 by loop transplant.Rational Substitution of Surface Acidic Residues for Enhancing the Thermostability of Thermolysin.Penicillium purpurogenum produces a highly stable endo-β-(1,4)-galactanase.
P2860
Thermostability enhancement of an endo-1,4-β-galactanase from Talaromyces stipitatus by site-directed mutagenesis
description
im Dezember 2014 veröffentlichter wissenschaftlicher Artikel
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wetenschappelijk artikel
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наукова стаття, опублікована в грудні 2014
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name
Thermostability enhancement of ...... s by site-directed mutagenesis
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Thermostability enhancement of ...... s by site-directed mutagenesis
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type
label
Thermostability enhancement of ...... s by site-directed mutagenesis
@en
Thermostability enhancement of ...... s by site-directed mutagenesis
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prefLabel
Thermostability enhancement of ...... s by site-directed mutagenesis
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Thermostability enhancement of ...... s by site-directed mutagenesis
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P2093
P2860
P1476
Thermostability enhancement of ...... s by site-directed mutagenesis
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P2093
Anders Thygesen
Christian Nyffenegger
Dorte M. Larsen
Jørn D. Mikkelsen
Maria M. Swiniarska
P2860
P2888
P304
P356
10.1007/S00253-014-6244-Z
P407
P577
2014-12-02T00:00:00Z