Formation of lipolytic enzymes by Brevibacterium linens

Authors: Adamitsch B.F.¹; Hampel W.A.²

Source: Biotechnology Letters, Volume 22, Number 20, October 2000 , pp. 1643-1646(4)

Publisher: Springer

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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.

Keywords: Brevibacterium linens; lipase-formation; lipase-location

Language: English

Document Type: Regular paper

Affiliations: 1: E-mail: badamits@mail.zserv.tuwien.ac.at) 2: Institute of Biochemical Technology and Microbiology, Vienna University of Technology, Getreidemarkt 9/172, A-1060 Vienna, Austria (Fax: +43 1 58801 17299

Publication date: 2000-10-01