Characterization of membrane-bound lipase from a thermophilic Rhizopus oryzae isolated from palm oil mill effluent

The characteristics of the membrane‐bound lipase from a thermophilic Rhizopus oryzae were studied. The pH and temperature optima for lipase activity were at 7.0 and 37°C, respectively. The enzyme was stable and acidic conditions, retaining more than 80% of its initial activity at pH 4.0 after 30 min...

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Bibliographic Details
Published in:Journal of the American Oil Chemists' Society 1999-02, Vol.76 (2), p.171-174
Main Authors: Razak, C.N.A. (Universiti Putra Malaysia, Selangor, Malaysia.), Musani, R, Basri, M, Salleh, A.B
Format: Article
Language:English
Subjects:
AGUAS RESIDUALES
Biological and medical sciences
Biotechnology
CHAMPIGNON
Characterization
EAU USEE
Enzyme engineering
Food industries
Fundamental and applied biological sciences. Psychology
FUNGI
HONGOS
lipase
LIPOLYTIC FUNGI
membrane‐bound lipase
Methods. Procedures. Technologies
MICROORGANISME THERMOPHILE
MICROORGANISMOS TERMOFILOS
Miscellaneous
RHIZOPUS ORYZAE
THERMOPHILIC MICROORGANISMS
TRIACILGLICEROL LIPASA
TRIACYLGLYCEROL LIPASE
Use and upgrading of agricultural and food by-products. Biotechnology
WASTEWATER
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Summary:The characteristics of the membrane‐bound lipase from a thermophilic Rhizopus oryzae were studied. The pH and temperature optima for lipase activity were at 7.0 and 37°C, respectively. The enzyme was stable and acidic conditions, retaining more than 80% of its initial activity at pH 4.0 after 30 min incubation. It was stable up to 50°C with 70% of initial activity retained after 3 h incubation. The enzyme is 1,3 specific and exhibits substrate preference. Monoacid triglyceride substrates were hydrolyzed better than methyl esters, polyoxysorbitan and sorbitan substrates.
ISSN:0003-021X
1558-9331
DOI:10.1007/s11746-999-0214-0