Investigations of heat treatment to improve the isolation of intracellular enzymes

✍ Scribed by M.-R. Kula; J. Schnell

• Book ID: 104744374
• Publisher: Springer
• Year: 1990
• Tongue: English
• Weight: 695 KB
• Volume: 5
• Category: Article
• ISSN: 1615-7605
• DOI: 10.1007/bf00369644

✦ Synopsis

Heat conditioning of cell homogenates of B. cereus and a recombinant E. coli was studied for the isolation of leucine dehydrogenase and alanine racemase, respectively. The strain of E. coli carried the gene of the thermostable alanine racemase from B. stearothermophilus. Activity loss can be minimized (<5%) and aggregation and flocculation of soluble proteins (70-80%) and other cell components can be achieved, depending on temperature, biomass concentration and pH-value.

Thereby a 3-6 fold increase in specific activity was obtained. The resulting extract after solid-liquid separation showed lower viscosity and less turbidity than unheated controls, making it more suitable for chromatographic separations.