Reversibility of Heat-Inactivation of Bacterial α-Amylase
نویسندگان
چکیده
منابع مشابه
Effects of Substrate on Heat Inactivation of Taka-amylase A
methan nicht größer wählt als angegeben, da sonst die dunkelbraunen, öligen Additionsprodukte von Diazomethan an Chinone, die stets auftreten, zum Hauptumsetzungsprodukt werden. Wichtig ist außerdem, daß man eine durch Destillation hergestellte Diazomethanlösung verwendet, da die übliche, durch Dekantieren des Äthers von der alkalischen Entwicklungslösung dargestellte Lösung stets noch so viel ...
متن کاملEffects of substrate on heat inactivation of Taka-amylase A.
methan nicht größer wählt als angegeben, da sonst die dunkelbraunen, öligen Additionsprodukte von Diazomethan an Chinone, die stets auftreten, zum Hauptumsetzungsprodukt werden. Wichtig ist außerdem, daß man eine durch Destillation hergestellte Diazomethanlösung verwendet, da die übliche, durch Dekantieren des Äthers von der alkalischen Entwicklungslösung dargestellte Lösung stets noch so viel ...
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Previous studies have shown that a number of factors can affect the rate, extent, or reversibility of denaturation. These factors include the nature and concentration of salt present (l-4), the concentration of protein (3, 5), the pH (6), and the nature of the denaturing agent (2). The return of enzymic activity after its loss through a process leading to denaturation is generally regarded as e...
متن کاملDynamic model of heat inactivation kinetics for bacterial adaptation.
The Weibullian-log logistic (WeLL) inactivation model was modified to account for heat adaptation by introducing a logistic adaptation factor, which rendered its "rate parameter" a function of both temperature and heating rate. The resulting model is consistent with the observation that adaptation is primarily noticeable in slow heat processes in which the cells are exposed to sublethal tempera...
متن کاملCrystalline Trypsin Iv. Reversibility of the Inactivation and Denaturation of Trypsin by Heat
I t was noted by Mellanby and Wooley (1) that trypsin solutions in dilute acid could be heated nearly to boiling with very little loss in activity, and this observation was confirmed by Eddie (2). At temperatures below 40°C., on the other hand, the enzyme is more stable near pH 4 or 5 than it is in acid solution. This latter result has also been obtained by the writer (3) and by Pace (4). In th...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1964
ISSN: 0002-1369
DOI: 10.1080/00021369.1964.10858287