A new method to evaluate the thermal stability of lyophilized enzymes

Research output: Contribution to journalArticle

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.

Details

Authors
Organisations
External organisations
  • Lund University
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Biocatalysis and Enzyme Technology
Original languageEnglish
Pages (from-to)947-952
Number of pages6
JournalBiotechnology Techniques
Volume10
Issue number12
Publication statusPublished - 1996 Jan 1
Publication categoryResearch
Peer-reviewedYes