Thermoadaptation-directed evolution of chloramphenicol acetyltransferase in an error-prone thermophi...
Thermoadaptation-directed evolution of chloramphenicol acetyltransferase in an error-prone thermophile using improved procedures
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Berlin/Heidelberg: Springer Berlin Heidelberg
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English
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Berlin/Heidelberg: Springer Berlin Heidelberg
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Contents
Enhancing the thermostability of thermolabile enzymes extends their practical utility. We previously demonstrated that an error-prone thermophile derived from Geobacillus kaustophilus HTA426 can generate mutant genes encoding enzyme variants that are more thermostable than the parent enzyme. Here, we used this approach, termed as thermoadaptation-d...
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Thermoadaptation-directed evolution of chloramphenicol acetyltransferase in an error-prone thermophile using improved procedures
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TN_cdi_proquest_journals_2511643205
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2511643205
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ISSN
0175-7598
E-ISSN
1432-0614
DOI
10.1007/s00253-015-6522-4