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

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..

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Abstract

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.

Item Type: Article
Uncontrolled Keywords: BACTERIA-; ENZYMES-; LIPASES-; MICROORGANISMS-; PROPIONIBACTERIUM-
Subjects: 600 Technology > 08 Food technology > 16 Nutritive value > 05 Enzymes
600 Technology > 08 Food technology > 16 Nutritive value > 07 Waste utilization
Divisions: Fermentation Technology and Bioengineering
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 27 Feb 2018 04:07
Last Modified: 27 Feb 2018 04:07
URI: http://ir.cftri.com/id/eprint/7961

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