A new method to evaluate the thermal stability of lyophilized enzymes

Ernst Wehtje, Hugo De Wit, Patrick Adlercreutz

    Research output: Contribution to journalArticlepeer-review

    Abstract

    The thermal inactivation of lyophilized chymotrypsin was studied at controlled water activities. At 60 °C the enzyme showed good stability except at aw 0.97, whereas at 75 °C considerable inactivation occured at most water activities. Increasing the amount of buffer on the preparation decreased the stability significantly. The optimal temperature of enzymatic activity was increased 14 °C, when the water activity was decreased from 1 to 0.5.

    Original languageEnglish
    Pages (from-to)947-952
    Number of pages6
    JournalBiotechnology Techniques
    Volume10
    Issue number12
    DOIs
    Publication statusPublished - 1996 Jan 1

    Subject classification (UKÄ)

    • Biocatalysis and Enzyme Technology

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