Enzymatic activity and thermoresistance of improved microbial transglutaminase variants
Author:
Funder
FNR, BMEL Germany
Publisher
Springer Science and Business Media LLC
Subject
Organic Chemistry,Clinical Biochemistry,Biochemistry
Link
http://link.springer.com/content/pdf/10.1007/s00726-019-02764-9.pdf
Reference50 articles.
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3. Baker D, Agard DA (1994) Kinetics versus thermodynamics in protein folding. Biochemistry 33:7505–7509. https://doi.org/10.1021/bi00190a002
4. Brissos V, Gonçalves N, Melo EP, Martins LO (2014) Improving kinetic or thermodynamic stability of an azoreductase by directed evolution. PLoS One 9:e87209. https://doi.org/10.1371/journal.pone.0087209
5. Buettner K, Hertel T, Pietzsch M (2012) Increased thermostability of microbial transglutaminase by combination of several hot spots evolved by random and saturation mutagenesis. Amino Acids 42:987–996
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