| dc.contributor.author | More, N. | |
| dc.contributor.author | Daniel, Roy M. | |
| dc.contributor.author | Petach, Helen H. | |
| dc.date.accessioned | 2010-08-30T21:51:52Z | |
| dc.date.available | 2010-08-30T21:51:52Z | |
| dc.date.issued | 1995 | |
| dc.identifier.citation | More, N., Daniel, R.M., Petach, H.H. (1995). The effect of low temperatures on enzyme activity. Biochemical Journal, 305(1), 17-20. | en_NZ |
| dc.identifier.issn | 0264-6021 | |
| dc.identifier.uri | https://hdl.handle.net/10289/4473 | |
| dc.description.abstract | The stability of two enzymes from extreme thermophiles (glutamate dehydrogenase from Thermococcales strain AN1 and beta-glucosidase from Caldocellum saccharolyticum expressed in Escherichia coli) has been exploited to allow measurement of activity over a 175 degrees C temperature range, from +90 degrees C to -85 degrees C for the glutamate dehydrogenase and from +90 degrees C to -70 degrees C for the beta-glucosidase. The Arrhenius plots of these enzymes, and those for two mesophilic enzymes (glutamate dehydrogenase from bovine liver and beta-galactosidase from Escherichia coli), exhibit no downward deflection corresponding to the glass transition, found by biophysical measurements of several non-enzymic mesophilic proteins at about -65 degrees C and reflecting a sharp decrease in protein flexibility as the overall motion of groups of atoms ceases. | en_NZ |
| dc.language.iso | en | |
| dc.relation.uri | http://www.biochemj.org/bj/305/bj3050017.htm | en_NZ |
| dc.subject | enzyme | en_NZ |
| dc.title | The effect of low temperatures on enzyme activity | en_NZ |
| dc.type | Journal Article | en_NZ |
| dc.identifier.doi | 10.1042/bj3050017 | |
