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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Does single-amino-acid replacement work in favor of or against improvement of the thermostability of immobilized enzyme?

Thermostabilities of kanamycin nucleotidyltransferase and of its mutants that became thermostable, in the free state, because of single-amino-acid replacements were studied after immobilization of the enzymes on cyanogen bromide-activated Sephadex G-200 particles. Lys in place of Gln at position 102 decreased the thermostability of the immobilized enzyme, whereas replacement with other amino acids enhanced it.[1]

References

  1. Does single-amino-acid replacement work in favor of or against improvement of the thermostability of immobilized enzyme? Koizumi, J., Zhang, M., Imanaka, T., Aiba, S. Appl. Environ. Microbiol. (1990) [Pubmed]
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