Abstract
When Brevibacterium linens ATCC 9172 was grown in shake flasks, it produced a cell-associated lipase with a specific activity of 152 to 188 U g−1 cells depending on the composition of the growth medium. There was no growth in media containing tributyrine as the sole carbon source. The cell-associated lipase had maximum activity at pH 8.0 and 37 °C and was strongly inhibited by 3,4-dichloroisocoumarin, an inhibitor specific for serine esterases. Cell-associated activity was released from the cells by treatment with lysozyme. The kinetics of lipase formation was closely related to the amount of biomass formed during growth.
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Adamitsch, B.F., Hampel, W.A. Formation of lipolytic enzymes by Brevibacterium linens. Biotechnology Letters 22, 1643–1646 (2000). https://doi.org/10.1023/A:1005633828125
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DOI: https://doi.org/10.1023/A:1005633828125