| Title : Purification and characterization of a Penicillium sp. lipase which discriminates against diglycerides - Gulomova_1996_Lipids_31_379 |
| Author(s) : Gulomova K , Ziomek E , Schrag JD , Davranov K , Cygler M |
| Ref : Lipids , 31 :379 , 1996 |
|
Abstract :
A lipase was isolated from Penicillium sp. strain UZLM-4 and characterized. This lipase has a molecular weight of 27,344 (determined by mass spectrometry) and hydrolyzes triglycerides in preference to mono- and diglyceride substrates. Among various triglyceride substrates, tributyrin is hydrolyzed about four times faster than any other tested. The lipase has a preference for hydrolysis at the 1,3 positions of the lipids and shows a weak stereoselectivity for the S enantiomer. Unlike most other lipases, this lipase is stable and has a high activity at low surface pressures (5-10 mN/m). |
| PubMedSearch : Gulomova_1996_Lipids_31_379 |
| PubMedID: 8743049 |
Gulomova K, Ziomek E, Schrag JD, Davranov K, Cygler M (1996)
Purification and characterization of a Penicillium sp. lipase which discriminates against diglycerides
Lipids
31 :379
Gulomova K, Ziomek E, Schrag JD, Davranov K, Cygler M (1996)
Lipids
31 :379