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. 1971 Jan;21(1):9–12. doi: 10.1128/am.21.1.9-12.1971

Glycerol Ester Hydrolase Activity of Microbacterium thermosphactum

D L Collins-Thompson 1, T Sørhaug 1, L D Witter 1, Z J Ordal 1
PMCID: PMC377107  PMID: 16349896

Abstract

Microbacterium thermosphactum possesses a significant glycerol ester hydrolase (lipase, EC 3.1.1.3) activity and a weak but definite carboxylic ester hydrolase (esterase, EC 3.1.1.1) activity. Harvested whole cell preparations contained 53 units of lipase activity with tripropionin as the substrate. This activity decreased with an increasing chain length of fatty acid in the triglyceride to 13 units with trilaurin as the substrate and no activity with tripalmitin. Maximum lipase activity was found at a temperature of 35 to 37 C and at a pH of 7.1 to 7.3. Lipase activity was associated with three different protein peaks when the protein of cell-free extract was fractionated by polyacrylamide gel electrophoresis.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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