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Purification and properties of lipase from the anaerobe Propionibacterium acidi-propionici.

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Title Purification and properties of lipase from the anaerobe Propionibacterium acidi-propionici.
 
Creator Sarada, R.
Joseph, R.
 
Subject 05 Enzymes
07 Waste utilization
 
Description A lipase secreted by Propionibacterium acidi-propionici was purified 52-fold with 27% recovery by employing a 3-step purification protocol. The enzyme has a small molecular mass (Mr = 6000-8000) as determined by gel filtration and ultracentrifugation. It hydrolysed palm oil, coconut oil, castor oil, olive oil, groundnut oil and tributyrin. Enzyme activity was inhibited by Ni2+, Ba2+, Mg2+, Cu2+, EDTA, iodoacetamide, N-acetylimidazole and nonidet P-40 but stimulated by Ca2+, Co2+, K+, Fe2+, SDS and N-bromosuccinamide. The enzyme showed substrate inhibition for both tributyrin and p-nitrophenyl acetate.
 
Date 1992
 
Type Article
PeerReviewed
 
Format pdf
 
Language en
 
Identifier http://ir.cftri.com/7961/1/JAOCS%2C%20Vol.%2069%2C%20no.%2010%20%28October%201992%29.pdf
Sarada, R. and Joseph, R. (1992) Purification and properties of lipase from the anaerobe Propionibacterium acidi-propionici. Journal of the American Oil Chemists' Society, 69 (10). 974-977, 9 ref..