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dc.contributor.authorDaniel, Roy M.
dc.date.accessioned2010-08-30T03:08:11Z
dc.date.available2010-08-30T03:08:11Z
dc.date.issued1996
dc.identifier.citationDaniel, R.M. (1996). The upper limits of enzyme thermal stability. Enzyme and Microbial Technology, 19(1), 74-49.en_NZ
dc.identifier.urihttps://hdl.handle.net/10289/4467
dc.description.abstractSome enzymes, such as those from extreme thermophiles, have significant half-lives above 100°C. The differences in structure and function between these very stable and less stable enzymes are relatively small and are comparable with those differences found among enzymes of similar stability. Recent evidence suggests that protein degradative reactions at high temperatures (>80°C) occur only slowly in conformationally intact proteins, so that conformational stability may still dictate the upper temperature limit for enzyme activity. The interrelationship of both conformational stability and enzymatic activity with protein flexibility suggests that in naturally occurring enzymes, we cannot expect to find stability at temperatures far above those which are optimum for the growth of the organism. Genetic and enzyme engineering studies are promising in terms of enhancing conformational stability, but are likely to require case-by-case knowledge of the enzyme concerned, and stability enhancements achieved so far are relatively small. Furthermore, engineered increases in stability may well be accompanied by a decrease in specific activity. Nevertheless, it should be feasible to engineer enzymes to be substantially more stable than any of those found so far in nature where useful half-lives above 120°C are already available.en_NZ
dc.language.isoen
dc.publisherElsevieren_NZ
dc.subjectenzymesen_NZ
dc.subjectstabilityen_NZ
dc.subjectenzyme engineeringen_NZ
dc.subjectthermophilesen_NZ
dc.subjectdenaturationen_NZ
dc.subjectdegradationen_NZ
dc.titleThe upper limits of enzyme thermal stabilityen_NZ
dc.typeJournal Articleen_NZ
dc.identifier.doi10.1016/0141-0229(95)00174-3en_NZ


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